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Conserved domains on  [gi|1784428039|pdb|6LES|Y]
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Chain Y, Maltose/maltodextrin-binding periplasmic protein,Focal adhesion kinase 1

Protein Classification

maltose/maltodextrin ABC transporter substrate-binding protein( domain architecture ID 11484205)

maltose/maltodextrin ABC transporter substrate-binding protein functions as the primary receptor for the active transport of maltose and higher maltodextrins such as maltotriose

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
malE PRK09474
maltose/maltodextrin ABC transporter substrate-binding protein MalE;
1-359 0e+00

maltose/maltodextrin ABC transporter substrate-binding protein MalE;


:

Pssm-ID: 236533 [Multi-domain]  Cd Length: 396  Bit Score: 766.10  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y         1 MKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEI 80
Cdd:PRK09474  26 AKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEV 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y        81 TPAAAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWP 160
Cdd:PRK09474 106 TPSKAFKDKLVPFTWDAVRYNGKLIGYPIAVEALSLIYNKDLVPTPPKTWEEIPALDKELKAKGKSAIMWNLQEPYFTWP 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y       161 LIAADGGYAFKYAAGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSA 240
Cdd:PRK09474 186 LIAADGGYAFKFENGGYDVKDVGVNNAGAKAGLQFLVDLVKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDKSG 265

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y       241 VNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLGAVALKSYEEELAKDPRIAA 320
Cdd:PRK09474 266 INYGVTVLPTFNGKPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLETVNKDKPLGAVALKSFQEELAKDPRIAA 345

                        330       340       350
                 ....*....|....*....|....*....|....*....
6LES_Y       321 TMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVD 359
Cdd:PRK09474 346 TMDNAQNGEIMPNIPQMSAFWYAMRTAIINATSGRQTVD 384
 
Name Accession Description Interval E-value
malE PRK09474
maltose/maltodextrin ABC transporter substrate-binding protein MalE;
1-359 0e+00

maltose/maltodextrin ABC transporter substrate-binding protein MalE;


Pssm-ID: 236533 [Multi-domain]  Cd Length: 396  Bit Score: 766.10  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y         1 MKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEI 80
Cdd:PRK09474  26 AKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEV 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y        81 TPAAAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWP 160
Cdd:PRK09474 106 TPSKAFKDKLVPFTWDAVRYNGKLIGYPIAVEALSLIYNKDLVPTPPKTWEEIPALDKELKAKGKSAIMWNLQEPYFTWP 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y       161 LIAADGGYAFKYAAGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSA 240
Cdd:PRK09474 186 LIAADGGYAFKFENGGYDVKDVGVNNAGAKAGLQFLVDLVKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDKSG 265

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y       241 VNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLGAVALKSYEEELAKDPRIAA 320
Cdd:PRK09474 266 INYGVTVLPTFNGKPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLETVNKDKPLGAVALKSFQEELAKDPRIAA 345

                        330       340       350
                 ....*....|....*....|....*....|....*....
6LES_Y       321 TMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVD 359
Cdd:PRK09474 346 TMDNAQNGEIMPNIPQMSAFWYAMRTAIINATSGRQTVD 384
PBP2_MBP cd13656
The periplasmic binding component of ABC tansport system specific for maltose; possess the ...
 6-368 0e+00

The periplasmic binding component of ABC tansport system specific for maltose; possess the type 2 periplasmic binidng fold; This group includes the periplasmic maltose-binding protein of an ATP-binding cassette transporter. Maltose is a disaccharide formed from two units of glucose. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270374 [Multi-domain]  Cd Length: 364  Bit Score: 669.30  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y        6 GKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPAAA 85
Cdd:cd13656   1 GKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPDKA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y       86 FQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAAD 165
Cdd:cd13656  81 FQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAAD 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y      166 GGYAFKYAAGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSAVNYGV 245
Cdd:cd13656 161 GGYAFKYENGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKVNYGV 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y      246 TVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLGAVALKSYEEELAKDPRIAATMENA 325
Cdd:cd13656 241 TVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLGAVALKSYEEELAKDPRIAATMENA 320

                       330       340       350       360
                ....*....|....*....|....*....|....*....|...
6LES_Y      326 QKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDAALAAAQTN 368
Cdd:cd13656 321 QKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAQTR 363
MalE COG2182
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
4-359 7.15e-138

Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];


Pssm-ID: 441785 [Multi-domain]  Cd Length: 410  Bit Score: 399.71  E-value: 7.15e-138
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y        4 EEGKLVIWINGDKGyNGLAEVGKKFEKDTGIKVTVEHP--DKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEIT 81
Cdd:COG2182  37 AGGTLTVWVDDDEA-EALEEAAAAFEEEPGIKVKVVEVpwDDLREKLTTAAPAGKGPDVFVGAHDWLGELAEAGLLAPLD 115

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y       82 PAAAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLP-NPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWP 160
Cdd:COG2182 116 DDLADKDDFLPAALDAVTYDGKLYGVPYAVETLALYYNKDLVKaEPPKTWDELIAAAKKLTAAGKYGLAYDAGDAYYFYP 195

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y      161 LIAADGGYAFKYAAGkyDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSA 240
Cdd:COG2182 196 FLAAFGGYLFGKDGD--DPKDVGLNSPGAVAALEYLKDLIKDGVLPADADYDAADALFAEGKAAMIINGPWAAADLKKAL 273

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y      241 -VNYGVTVLPTF-KGQPSKPFVGVLSAGINAASPNKELAKEFLeNYLLTDEGLEAVNKDKPLgAVALKSY--EEELAKDP 316
Cdd:COG2182 274 gIDYGVAPLPTLaGGKPAKPFVGVKGFGVSAYSKNKEAAQEFA-EYLTSPEAQKALFEATGR-IPANKAAaeDAEVKADP 351

                       330       340       350       360
                ....*....|....*....|....*....|....*....|...
6LES_Y      317 RIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVD 359
Cdd:COG2182 352 LIAAFAEQAEYAVPMPNIPEMGAVWTPLGTALQAIASGKADPA 394
SBP_bac_8 pfam13416
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 23-316 2.36e-32

Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins.


Pssm-ID: 433189 [Multi-domain]  Cd Length: 281  Bit Score: 123.28  E-value: 2.36e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y         23 EVGKKFEKDTGIKVTVEHP--DKLEEKFPQVAATGDGPDI--IFWAHDRFGGYAQSGLLAEITP---AAAFQDKLYPFTW 95
Cdd:pfam13416   1 ALAKAFEKKTGVTVEVEPQasNDLQAKLLAAAAAGNAPDLdvVWIAADQLATLAEAGLLADLSDvdnLDDLPDALDAAGY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y         96 DavrynGKLIAYPIAVEA-LSLIYNKDLLP---NPPKTWEEIPALDKELKAKgksalmfnlqepyFTWPLIAADGGYAFK 171
Cdd:pfam13416  81 D-----GKLYGVPYAASTpTVLYYNKDLLKkagEDPKTWDELLAAAAKLKGK-------------TGLTDPATGWLLWAL 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y        172 YAAGKyDIKDVGVDNAGAKAGLTFLVDLIKN-KHMNADTDysiAEAAFNKGETAMTINGPWAWSNIDTSAVNYGVTVLpt 250
Cdd:pfam13416 143 LADGV-DLTDDGKGVEALDEALAYLKKLKDNgKVYNTGAD---AVQLFANGEVAMTVNGTWAAAAAKKAGKKLGAVVP-- 216

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
6LES_Y        251 fkgqPSKPFVGVLSAGINAASPNKEL-AKEFLeNYLLTDEGLEAVNKDKPLGAVALKSYE-EELAKDP 316
Cdd:pfam13416 217 ----KDGSFLGGKGLVVPAGAKDPRLaALDFI-KFLTSPENQAALAEDTGYIPANKSAALsDEVKADP 279
 
Name Accession Description Interval E-value
malE PRK09474
maltose/maltodextrin ABC transporter substrate-binding protein MalE;
1-359 0e+00

maltose/maltodextrin ABC transporter substrate-binding protein MalE;


Pssm-ID: 236533 [Multi-domain]  Cd Length: 396  Bit Score: 766.10  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y         1 MKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEI 80
Cdd:PRK09474  26 AKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEV 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y        81 TPAAAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWP 160
Cdd:PRK09474 106 TPSKAFKDKLVPFTWDAVRYNGKLIGYPIAVEALSLIYNKDLVPTPPKTWEEIPALDKELKAKGKSAIMWNLQEPYFTWP 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y       161 LIAADGGYAFKYAAGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSA 240
Cdd:PRK09474 186 LIAADGGYAFKFENGGYDVKDVGVNNAGAKAGLQFLVDLVKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDKSG 265

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y       241 VNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLGAVALKSYEEELAKDPRIAA 320
Cdd:PRK09474 266 INYGVTVLPTFNGKPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLETVNKDKPLGAVALKSFQEELAKDPRIAA 345

                        330       340       350
                 ....*....|....*....|....*....|....*....
6LES_Y       321 TMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVD 359
Cdd:PRK09474 346 TMDNAQNGEIMPNIPQMSAFWYAMRTAIINATSGRQTVD 384
PBP2_MBP cd13656
The periplasmic binding component of ABC tansport system specific for maltose; possess the ...
 6-368 0e+00

The periplasmic binding component of ABC tansport system specific for maltose; possess the type 2 periplasmic binidng fold; This group includes the periplasmic maltose-binding protein of an ATP-binding cassette transporter. Maltose is a disaccharide formed from two units of glucose. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270374 [Multi-domain]  Cd Length: 364  Bit Score: 669.30  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y        6 GKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPAAA 85
Cdd:cd13656   1 GKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPDKA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y       86 FQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAAD 165
Cdd:cd13656  81 FQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAAD 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y      166 GGYAFKYAAGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSAVNYGV 245
Cdd:cd13656 161 GGYAFKYENGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKVNYGV 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y      246 TVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLGAVALKSYEEELAKDPRIAATMENA 325
Cdd:cd13656 241 TVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLGAVALKSYEEELAKDPRIAATMENA 320

                       330       340       350       360
                ....*....|....*....|....*....|....*....|...
6LES_Y      326 QKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDAALAAAQTN 368
Cdd:cd13656 321 QKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAQTR 363
MalE COG2182
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
4-359 7.15e-138

Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];


Pssm-ID: 441785 [Multi-domain]  Cd Length: 410  Bit Score: 399.71  E-value: 7.15e-138
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y        4 EEGKLVIWINGDKGyNGLAEVGKKFEKDTGIKVTVEHP--DKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEIT 81
Cdd:COG2182  37 AGGTLTVWVDDDEA-EALEEAAAAFEEEPGIKVKVVEVpwDDLREKLTTAAPAGKGPDVFVGAHDWLGELAEAGLLAPLD 115

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y       82 PAAAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLP-NPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWP 160
Cdd:COG2182 116 DDLADKDDFLPAALDAVTYDGKLYGVPYAVETLALYYNKDLVKaEPPKTWDELIAAAKKLTAAGKYGLAYDAGDAYYFYP 195

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y      161 LIAADGGYAFKYAAGkyDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSA 240
Cdd:COG2182 196 FLAAFGGYLFGKDGD--DPKDVGLNSPGAVAALEYLKDLIKDGVLPADADYDAADALFAEGKAAMIINGPWAAADLKKAL 273

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y      241 -VNYGVTVLPTF-KGQPSKPFVGVLSAGINAASPNKELAKEFLeNYLLTDEGLEAVNKDKPLgAVALKSY--EEELAKDP 316
Cdd:COG2182 274 gIDYGVAPLPTLaGGKPAKPFVGVKGFGVSAYSKNKEAAQEFA-EYLTSPEAQKALFEATGR-IPANKAAaeDAEVKADP 351

                       330       340       350       360
                ....*....|....*....|....*....|....*....|...
6LES_Y      317 RIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVD 359
Cdd:COG2182 352 LIAAFAEQAEYAVPMPNIPEMGAVWTPLGTALQAIASGKADPA 394
PBP2_ABC_oligosaccharides cd13522
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
 7-369 2.52e-137

The periplasmic-binding component of ABC transport systems specific for maltose and related oligosaccharides; possess type 2 periplasmic binding fold; This family represents the periplasmic binding component of ABC transport systems involved in uptake of oligosaccharides including maltose, trehalose, maltodextrin, and cyclodextrin. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270240 [Multi-domain]  Cd Length: 368  Bit Score: 396.78  E-value: 2.52e-137
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y        7 KLVIWINGDKG-YNGLAEVGKKFEKDT-GIKVTVEHPDK--LEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITP 82
Cdd:cd13522   1 TITVWHQYDTGeNQAVNELIAKFEKAYpGITVEVTYQDTeaRRQFFSTAAAGGKGPDVVFGPSDSLGPFAAAGLLAPLDE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y       83 AAAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLP-NPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPL 161
Cdd:cd13522  81 YVSKSGKYAPNTIAAMKLNGKLYGVPVSVGAHLMYYNKKLVPkNPPKTWQELIALAQGLKAKNVWGLVYNQNEPYFFAAW 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y      162 IAADGGYAFKYAAGKYDIkdvGVDNAGAKAGLTFLVDLI-KNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNID-TS 239
Cdd:cd13522 161 IGGFGGQVFKANNGKNNP---TLDTPGAVEALQFLVDLKsKYKIMPPETDYSIADALFKAGKAAMIINGPWDLGDYRqAL 237

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y      240 AVNYGVTVLPTFKG-QPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLeaVNKDKPLGAVALKSYEEELAKDPRI 318
Cdd:cd13522 238 KINLGVAPLPTFSGtKHAAPFVGGKGFGINKESQNKAAAVEFVKYLTSYQAQL--VLFDDAGDIPANLQAYESPAVQNKP 315

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|...
6LES_Y      319 A--ATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDAALAAAQTNA 369
Cdd:cd13522 316 AqkASAEQAAYGVPMPNIPEMRAVWDAFRIAVNSVLAGKVTPEAAAKDAQQEA 368
PBP2_Maltose_binding_like cd13586
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
 7-369 6.79e-127

The periplasmic-binding component of ABC transport systems specific for maltose and related polysaccharides; possess type 2 periplasmic binding fold; This subfamily represents the periplasmic binding component of ABC transport systems involved in uptake of polysaccharides including maltose, maltodextrin, and cyclodextrin. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270304 [Multi-domain]  Cd Length: 367  Bit Score: 370.09  E-value: 6.79e-127
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y        7 KLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPD--KLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPAA 84
Cdd:cd13586   1 TITVWTDEDGELEYLKELAEEFEKKYGIKVEVVYVDsgDTREKFITAGPAGKGPDVFFGPHDWLGELAAAGLLAPIPEYL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y       85 AFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDK--ELKAKGKSALMFNLQEPYFTWPLI 162
Cdd:cd13586  81 AVKIKNLPVALAAVTYNGKLYGVPVSVETIALFYNKDLVPEPPKTWEELIALAKkfNDKAGGKYGFAYDQTNPYFSYPFL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y      163 AADGGYAFKYAAGkyDIKDVGVDNAGAKAGLTFLVDLI-KNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSAV 241
Cdd:cd13586 161 AAFGGYVFGENGG--DPTDIGLNNEGAVKGLKFIKDLKkKYKVLPPDLDYDIADALFKEGKAAMIINGPWDLADYKDAGI 238

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y      242 NYGVTVLPTFKG-QPSKPFVGVLSAGINAASPNKELAKEFLEnYLLTDEGLEAVNKDKPlGAVALKSYEE--ELAKDPRI 318
Cdd:cd13586 239 NFGVAPLPTLPGgKQAAPFVGVQGAFVSAYSKNKEAAVEFAE-YLTSDEAQLLLFEKTG-RIPALKDALNdaAVKNDPLV 316

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|.
6LES_Y      319 AATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDAALAAAQTNA 369
Cdd:cd13586 317 KAFAEQAQYGVPMPNIPEMAAVWDAMGNALNLVASGKATPEEAAKDAVAAI 367
PBP2_CMBP cd13658
The periplasmic binding component of ABC transport systems specific for cyclo/maltodextrin; ...
 7-357 1.48e-82

The periplasmic binding component of ABC transport systems specific for cyclo/maltodextrin; possess the type 2 periplasmic binding fold; This group includes the periplasmic cyclo/maltodextrin-binding protein of Thermoactinomyces vulgaris ATP-binding cassette transporter and related proteins. Cyclodextrins are a family of compounds composed of glucose units connected by 1, 4 glycosidic linkages to form a series of oligosaccharide rings, and their cavity is hydrophibic which allows cyclodextrins to accomodate hydrophobic molecules/moieties in the cavity. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270376 [Multi-domain]  Cd Length: 372  Bit Score: 257.03  E-value: 1.48e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y        7 KLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLE--EKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPAA 84
Cdd:cd13658   1 QLTVWVDEDKKMAFIKKIAKQYTKKTGVKVKLVEVDQLDqlEKLSLDGPAGKGPDVMVAPHDRIGSAVLQGLLSPIKLSK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y       85 AFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKEL--KAKGKSALMFNLQEPYFTWPLI 162
Cdd:cd13658  81 DKKKGFTDQALKALTYDGKLYGLPAAVETLALYYNKDLVKNAPKTFDELEALAKDLtkEKGKQYGFLADATNFYYSYGLL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y      163 AADGGYAFKYAAGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSAVN 242
Cdd:cd13658 161 AGNGGYIFKKNGSDLDINDIGLNSPGAVKAVKFLKKWYTEGYLPKGMTGDVIQGLFKEGKAAAVIDGPWAIQEYQEAGVN 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y      243 YGVTVLPTF-KGQPSKPFVGVLSAGINAASPNKELAKEFLEnYLLTDEGLEAVNKDK---PlGAVALKSYEEElAKDPRI 318
Cdd:cd13658 241 YGVAPLPTLpNGKPMAPFLGVKGWYLSAYSKHKEWAQKFME-FLTSKENLKKRYDETneiP-PRKDVRSDPEI-KNNPLT 317

                       330       340       350
                ....*....|....*....|....*....|....*....
6LES_Y      319 AATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQT 357
Cdd:cd13658 318 SAFAKQASRAVPMPNIPEMGAVWEPANNALFFILSGKKT 356
PBP2_Maltodextrin cd13657
The periplasmic binding component of ABC transport system specific for maltodextrin; This ...
 7-347 6.51e-68

The periplasmic binding component of ABC transport system specific for maltodextrin; This group includes the periplasmic maltodextrin-binding protein of a binding protein-dependent ATP-binding cassette transporter. Maltodextrin is a polysaccharide that is used as a food addtive and can be enzymatically produced from any starch . Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270375 [Multi-domain]  Cd Length: 368  Bit Score: 219.17  E-value: 6.51e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y        7 KLVIWINGDKGY-NGLAEVGKKFEKDTGI---KVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITP 82
Cdd:cd13657   1 TITIWHALTGAEeDALQQIIDEFEAKYPVpnvKVPFEKKPDLQNKLLTAIPAGEGPDLFIWAHDWIGQFAEAGLLVPISD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y       83 AAAFQD--KLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKEL--KAKGKSALMFNLQEPYFT 158
Cdd:cd13657  81 YLSEDDfeNYLPTAVEAVTYKGKVYGLPEAYETVALIYNKALVDQPPETTDELLAIMKDHtdPAAGSYGLAYQVSDAYFV 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y      159 WPLIAADGGYAFKYAAGKydikdVGVDNAGAKAGLTFLVDLIKnKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDT 238
Cdd:cd13657 161 SAWIFGFGGYYFDDETDK-----PGLDTPETIKGIQFLKDFSW-PYMPSDPSYNTQTSLFNEGKAAMIINGPWFIGGIKA 234

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y      239 SAVNYGVTVLPTFKGQ-PSKPFVGVLSAGI--NAASPNKELAKEFLENYLLTDEGLEAVNKDKPLGAVALKSYEEELAKD 315
Cdd:cd13657 235 AGIDLGVAPLPTVDGTnPPRPYSGVEGIYVtkYAERKNKEAALDFAKFFTTAEASKILADENGYVPAATNAYDDAEVAAD 314

                       330       340       350
                ....*....|....*....|....*....|..
6LES_Y      316 PRIAATMENAQKGEIMPNIPQMSAFWYAVRTA 347
Cdd:cd13657 315 PVIAAFKAQAEHGVPMPNSPEMASVWGPVTLA 346
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
 4-295 6.70e-53

ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport and metabolism];


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 179.85  E-value: 6.70e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y        4 EEGKLVIWINGDKGYNGLAEVGKKFEKDT-GIKVTVEHP--DKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEI 80
Cdd:COG1653  31 GKVTLTVWHTGGGEAAALEALIKEFEAEHpGIKVEVESVpyDDYRTKLLTALAAGNAPDVVQVDSGWLAEFAAAGALVPL 110

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y       81 TPAAA----FQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLP----NPPKTWEEIPALDKELKAK-GKSALMFN 151
Cdd:COG1653 111 DDLLDddglDKDDFLPGALDAGTYDGKLYGVPFNTDTLGLYYNKDLFEkaglDPPKTWDELLAAAKKLKAKdGVYGFALG 190

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y      152 LQEPYFTWPLIAADGGYAFKyaagkyDIKDVGVDNAGAKAGLTFLVDLIKNKHMNAD---TDYSIAEAAFNKGETAMTIN 228
Cdd:COG1653 191 GKDGAAWLDLLLSAGGDLYD------EDGKPAFDSPEAVEALEFLKDLVKDGYVPPGalgTDWDDARAAFASGKAAMMIN 264

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y      229 GPWAWSNIDTSA--VNYGVTVLPTFK-GQPSKPFVGVLSAGINAASPNKELAKEFLEnYLLTDEGLEAVN 295
Cdd:COG1653 265 GSWALGALKDAApdFDVGVAPLPGGPgGKKPASVLGGSGLAIPKGSKNPEAAWKFLK-FLTSPEAQAKWD 333
PBP2_TMBP_like cd13585
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ...
 7-359 4.06e-52

The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and similar oligosaccharides; possess type 2 periplasmic binding fold; This family includes the periplasmic trehalose/maltose-binding component of an ABC transport system and related proteins from archaea and bacteria. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270303 [Multi-domain]  Cd Length: 383  Bit Score: 178.37  E-value: 4.06e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y        7 KLVIWINGDKGY-NGLAEVGKKFEK-DTGIKVTVEHP--DKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITP 82
Cdd:cd13585   1 TLTFWDWGQPAEtAALKKLIDAFEKeNPGVKVEVVPVpyDDYWTKLTTAAAAGTAPDVFYVDGPWVPEFASNGALLDLDD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y       83 ---AAAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLL------PNPPKTWEEIPALDKELKAKGKS----ALM 149
Cdd:cd13585  81 yieKDGLDDDFPPGLLDAGTYDGKLYGLPFDADTLVLFYNKDLFdkagpgPKPPWTWDELLEAAKKLTDKKGGqygfALR 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y      150 FNLQEPYFTWPLIAADGGYAFKYAAGKydikdVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEA--AFNKGETAMTI 227
Cdd:cd13585 161 GGSGGQTQWYPFLWSNGGDLLDEDDGK-----ATLNSPEAVEALQFYVDLYKDGVAPSSATTGGDEAvdLFASGKVAMMI 235

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y      228 NGPWAWSNIDTSAV--NYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLEnYLLTDEG---LEAVNKDKPLGA 302
Cdd:cd13585 236 DGPWALGTLKDSKVkfKWGVAPLPAGPGGKRASVLGGWGLAISKNSKHPEAAWKFIK-FLTSKENqlkLGGAAGPAALAA 314

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*..
6LES_Y      303 VALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVD 359
Cdd:cd13585 315 AAASAAAPDAKPALALAAAADALAAAVPPPVPPPWPEVYPILSEALQEALLGALGKS 371
PBP2_UgpB cd14748
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ...
 26-359 2.42e-48

The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; possesses type 2 periplasmic binding fold; This group includes the periplasmic component of an ABC transport system specific for sn-glycerol-3-phosphate (G3P) and closely related proteins from archaea and bacteria. Under phophate starvation conditions, Escherichia coli can utilize G3P as phosphate source when exclusively imported by an ATP-binding cassette (ABC) transporter composed of the periplasmic binding protein, UgpB, the transmembrane subunits, UgpA and UgpE, and a homodimer of the nucleotide binding subunit, UgpC. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 proteins are comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270451 [Multi-domain]  Cd Length: 385  Bit Score: 168.62  E-value: 2.42e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y       26 KKFEK-DTGIKVTVEHP---DKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPAAA----FQDKLYPFTWDA 97
Cdd:cd14748  21 DEFNKsHPDIKVKAVYQgsyDDTLTKLLAALAAGTAPDVAQVDASWVAQLADSGALEPLDDYIDkdgvDDDDFYPAALDA 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y       98 VRYNGKLIAYPIAVEALSLIYNKDLL-------PNPPKTWEEI----PALDKELKAKGKSALMFNLQEPYFTW-PLIAAD 165
Cdd:cd14748 101 GTYDGKLYGLPFDTSTPVLYYNKDLFeeagldpEKPPKTWDELeeaaKKLKDKGGKTGRYGFALPPGDGGWTFqALLWQN 180

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y      166 GGYAFKYAAGKydikdVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNI--DTSAVNY 243
Cdd:cd14748 181 GGDLLDEDGGK-----VTFNSPEGVEALEFLVDLVGKDGVSPLNDWGDAQDAFISGKVAMTINGTWSLAGIrdKGAGFEY 255

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y      244 GVTVLPTFKGQPSKPFVGVLSAGINAASP-NKELAKEFLEnYLLTDEGLEAVNKDK---PLGAVALKSYEEELAKDPRIA 319
Cdd:cd14748 256 GVAPLPAGKGKKGATPAGGASLVIPKGSSkKKEAAWEFIK-FLTSPENQAKWAKATgylPVRKSAAEDPEEFLAENPNYK 334

                       330       340       350       360
                ....*....|....*....|....*....|....*....|.
6LES_Y      320 ATMENAQKG-EIMPNIPQMSAFWYAVRTAVINAASGRQTVD 359
Cdd:cd14748 335 VAVDQLDYAkPWGPPVPNGAEIRDELNEALEAALLGKKTPE 375
PBP2_XBP1_like cd14749
The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; ...
 7-317 1.02e-36

The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; possesses type 2 periplasmic binding fold; This group represents the periplasmic component of an ABC transport system XBP1 that shows preference for xylo-oligosaccharides in the order of xylotriose > xylobiose > xylotetraose. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 proteins are comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270452 [Multi-domain]  Cd Length: 388  Bit Score: 137.51  E-value: 1.02e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y        7 KLVIW--INGDKGYNGLAEVGKKFEK---DTGIKVTVEHPDKLEEKFPQVAATGDGPDII-FWAHDRFGGYAQSGLLAEI 80
Cdd:cd14749   1 TITYWqyFTGDTKKKYMDELIADFEKenpNIKVKVVVFPYDNYKTKLKTAVAAGEGPDVFnLWPGGWLAEFVKAGLLLPL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y       81 TPAA---AFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLP-----NPPKTWEEIPALDKELKAKGK------S 146
Cdd:cd14749  81 TDYLdpnGVDKRFLPGLADAVTFNGKVYGIPFAARALALFYNKDLFEeaggvKPPKTWDELIEAAKKDKFKAKgqtgfgL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y      147 ALMFNLQEPYFTWPLIAADGGYAFKYAAGKYDIKdvgvDNAGAKAgLTFLVDLIKNKHMNADT---DYSIAEAAFNKGET 223
Cdd:cd14749 161 LLGAQGGHWYFQYLVRQAGGGPLSDDGSGKATFN----DPAFVQA-LQKLQDLVKAGAFQEGFegiDYDDAGQAFAQGKA 235

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y      224 AMTINGPWAWSNIDTS--AVNYGVTVLPTFK--GQPSKPFVGVLSAGINAASPNKELAKEFLeNYLLTDEGLEAVNKDkp 299
Cdd:cd14749 236 AMNIGGSWDLGAIKAGepGGKIGVFPFPTVGkgAQTSTIGGSDWAIAISANGKKKEAAVKFL-KYLTSPEVMKQYLED-- 312

                       330
                ....*....|....*...
6LES_Y      300 lgaVALKSYEEELAKDPR 317
Cdd:cd14749 313 ---VGLLPAKEVVAKDED 327
PBP2_MalE cd14747
Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes ...
 7-336 2.23e-35

Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes the periplasmic maltose-binding component of an ABC transport system from the phytopathogen Xanthomonas citri and its related bacterial proteins. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 proteins are comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270450 [Multi-domain]  Cd Length: 386  Bit Score: 133.98  E-value: 2.23e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y        7 KLVIWINGDKGYNG-LAEVGKKFEKDT-GIKVTVEH------PDKLEEKfpqvAATGDGPDIIFWAHDRFGGYAQSGLLA 78
Cdd:cd14747   1 TLTVWAMGNSAEAElLKELADEFEKENpGIEVKVQVlpwgdaHTKITTA----AASGDGPDVVQLGNTWVAEFAAMGALE 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y       79 EITP--AAAFQDKLYPF-TWDAVRYNGKLIAYPIAVEALSLIYNKDLL-----PNPPKTWEEIPALDKELKAKG--KSAL 148
Cdd:cd14747  77 DLTPylEDLGGDKDLFPgLVDTGTVDGKYYGVPWYADTRALFYRTDLLkkaggDEAPKTWDELEAAAKKIKADGpdVSGF 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y      149 MF----NLQEPYFTWpLIAADGGYAfkyaagKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIA--EAAFNKGE 222
Cdd:cd14747 157 AIpgknDVWHNALPF-VWGAGGDLA------TKDKWKATLDSPEAVAGLEFYTSLYQKGLSPKSTLENSAdvEQAFANGK 229

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y      223 TAMTINGPWAWSNIDTS----AVNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLEnYLLTDEGLEAVNKDK 298
Cdd:cd14747 230 VAMIISGPWEIGAIREAgpdlAGKWGVAPLPGGPGGGSPSFAGGSNLAVFKGSKNKDLAWKFIE-FLSSPENQAAYAKAT 308

                       330       340       350       360
                ....*....|....*....|....*....|....*....|
6LES_Y      299 PLGAvALKSY--EEELAKDPRIAATMENAQKGEIMPNIPQ 336
Cdd:cd14747 309 GMLP-ANTSAwdDPSLANDPLLAVFAEQLKTGKATPATPE 347
PBP2_TMBP cd14750
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; ...
 16-359 1.38e-33

The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; possesses type 2 periplasmic binding fold; This group represents the periplasmic trehalose/maltose-binding component of an ABC transport system and related proteins from archaea and bacteria. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 proteins are comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270453 [Multi-domain]  Cd Length: 385  Bit Score: 128.95  E-value: 1.38e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y       16 KGYNGLAEVGKKFEKDT-GIKVTVEH----PDKLEEKFPQVAATGD-GPDII----FWAhdrfGGYAQSGLLAEITP--A 83
Cdd:cd14750  11 QEGELLKKAIAAFEKKHpDIKVEIEElpasSDDQRQQLVTALAAGSsAPDVLgldvIWI----PEFAEAGWLLPLTEylK 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y       84 AAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLP----NPPKTWEEIPALDKELKAKGKSALMFNLQ----EP 155
Cdd:cd14750  87 EEEDDDFLPATVEANTYDGKLYALPWFTDAGLLYYRKDLLEkygpEPPKTWDELLEAAKKRKAGEPGIWGYVFQgkqyEG 166

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y      156 YFT--WPLIAADGGYAFKYAAGKydikdVGVDNAGAKAGLTFLVDLIKNKHM-NADTDYSIAEA--AFNKGETAMTINGP 230
Cdd:cd14750 167 LVCnfLELLWSNGGDIFDDDSGK-----VTVDSPEALEALQFLRDLIGEGISpKGVLTYGEEEAraAFQAGKAAFMRNWP 241

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y      231 WAW--SNIDTSAVN--YGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLEnYLLTDEGLEAVNKDKPLGAVALK 306
Cdd:cd14750 242 YAYalLQGPESAVAgkVGVAPLPAGPGGGSASTLGGWNLAISANSKHKEAAWEFVK-FLTSPEVQKRRAINGGLPPTRRA 320

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*
6LES_Y      307 SYEEE--LAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVD 359
Cdd:cd14750 321 LYDDPevLEAYPFLPALLEALENAVPRPVTPKYPEVSTAIQIALSAALSGQATPE 375
SBP_bac_8 pfam13416
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 23-316 2.36e-32

Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins.


Pssm-ID: 433189 [Multi-domain]  Cd Length: 281  Bit Score: 123.28  E-value: 2.36e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y         23 EVGKKFEKDTGIKVTVEHP--DKLEEKFPQVAATGDGPDI--IFWAHDRFGGYAQSGLLAEITP---AAAFQDKLYPFTW 95
Cdd:pfam13416   1 ALAKAFEKKTGVTVEVEPQasNDLQAKLLAAAAAGNAPDLdvVWIAADQLATLAEAGLLADLSDvdnLDDLPDALDAAGY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y         96 DavrynGKLIAYPIAVEA-LSLIYNKDLLP---NPPKTWEEIPALDKELKAKgksalmfnlqepyFTWPLIAADGGYAFK 171
Cdd:pfam13416  81 D-----GKLYGVPYAASTpTVLYYNKDLLKkagEDPKTWDELLAAAAKLKGK-------------TGLTDPATGWLLWAL 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y        172 YAAGKyDIKDVGVDNAGAKAGLTFLVDLIKN-KHMNADTDysiAEAAFNKGETAMTINGPWAWSNIDTSAVNYGVTVLpt 250
Cdd:pfam13416 143 LADGV-DLTDDGKGVEALDEALAYLKKLKDNgKVYNTGAD---AVQLFANGEVAMTVNGTWAAAAAKKAGKKLGAVVP-- 216

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
6LES_Y        251 fkgqPSKPFVGVLSAGINAASPNKEL-AKEFLeNYLLTDEGLEAVNKDKPLGAVALKSYE-EELAKDP 316
Cdd:pfam13416 217 ----KDGSFLGGKGLVVPAGAKDPRLaALDFI-KFLTSPENQAALAEDTGYIPANKSAALsDEVKADP 279
SBP_bac_1 pfam01547
Bacterial extracellular solute-binding protein; This family also includes the bacterial ...
 18-290 1.76e-30

Bacterial extracellular solute-binding protein; This family also includes the bacterial extracellular solute-binding protein family POTD/POTF.


Pssm-ID: 460248 [Multi-domain]  Cd Length: 294  Bit Score: 118.67  E-value: 1.76e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y         18 YNGLAEVGKKFEKD-TGIKVTVE--HPDKLEEKFPQVAATGDGP-DIIFWAHDRFGGYAQSGLLAEITPAAAFQDKLYPf 93
Cdd:pfam01547   7 AAALQALVKEFEKEhPGIKVEVEsvGSGSLAQKLTTAIAAGDGPaDVFASDNDWIAELAKAGLLLPLDDYVANYLVLGV- 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y         94 twdavrynGKLIAYPIAVEALSLIYNKDLLPN----PPKTWEEIPALDKELKAKGKSALMFNLQEP-----YFTWPLIAA 164
Cdd:pfam01547  86 --------PKLYGVPLAAETLGLIYNKDLFKKagldPPKTWDELLEAAKKLKEKGKSPGGAGGGDAsgtlgYFTLALLAS 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y        165 DGGYAFKYAAGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNA-DTDYSIAEAAFNKGETAMTINGPWAWSNIDTSAV-- 241
Cdd:pfam01547 158 LGGPLFDKDGGGLDNPEAVDAITYYVDLYAKVLLLKKLKNPGVaGADGREALALFEQGKAAMGIVGPWAALAANKVKLkv 237

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y        242 -----------NYGVTVLPTFKGQPskpfVGVLSAGINAASPNKELAKEFLeNYLLTDEG 290
Cdd:pfam01547 238 afaapapdpkgDVGYAPLPAGKGGK----GGGYGLAIPKGSKNKEAAKKFL-DFLTSPEA 292
PBP2_GacH cd14751
The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; ...
 28-359 8.06e-28

The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; possesses type 2 periplasmic binding fold; This group represents the periplasmic component GacH of an ABC import system. GacH is identified as a maltose/maltodextrin-binding protein with a low affinity for acarbose. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 proteins are comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270454 [Multi-domain]  Cd Length: 376  Bit Score: 112.86  E-value: 8.06e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y       28 FEKDT-GIKVTVE-HP-DKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPAAAFQD--KLYPFTWDAVRYNG 102
Cdd:cd14751  23 FEKEYpKIKVKAVrVPfDGLHNQIKTAAAGGQAPDVMRADIAWVPEFAKLGYLQPLDGTPAFDDivDYLPGPMETNRYNG 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y      103 KLIAYPIAVEALSLIYNKDLLPN----PPKTWEEIPALDKE-LKAKGKSALMFNLQEPYFTWPLIAADGGyafKYAAGky 177
Cdd:cd14751 103 HYYGVPQVTNTLALFYNKRLLEEagteVPKTMDELVAAAKAiKKKKGRYGLYISGDGPYWLLPFLWSFGG---DLTDE-- 177

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y      178 DIKDVGVDNAGAKAGLTFLVDLIKNKHMN--ADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSAV-----NYGVTVLPT 250
Cdd:cd14751 178 KKATGYLNSPESVRALETIVDLYDEGAITpcASGGYPNMQDGFKSGRYAMIVNGPWAYADILGGKEfkdpdNLGIAPVPA 257

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y      251 FKGQPSKPfVGVLSAGINAASPNKELAKEFLEnYLLTDEGLEAVNKDKPLGAVALKSYE-EELAKDPRIAATMENAQKGE 329
Cdd:cd14751 258 GPGGSGSP-VGGEDLVIFKGSKNKDAAWKFVK-FMSSAEAQALTAAKLGLLPTRTSAYEsPEVANNPMVAAFKPALETAV 335

                       330       340       350
                ....*....|....*....|....*....|
6LES_Y      330 IMPNIPQMSAFWYAVRTAVINAASGRQTVD 359
Cdd:cd14751 336 PRPPIPEWGELFEPLTLAFAKVLRGEKSPR 365
PBP2_oligosaccharide_1 cd13655
The periplasmic binding component of ABC tansport system specific for an unknown ...
 57-341 5.27e-25

The periplasmic binding component of ABC tansport system specific for an unknown oligosaccharide; possess the type 2 periplasmic binidng fold; This group represents an uncharacterized periplasmic-binding protein of an ATP-binding cassette transporter predicted to be involved in uptake of an unknown oligosaccharide molecule. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270373 [Multi-domain]  Cd Length: 363  Bit Score: 104.73  E-value: 5.27e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y       57 GPDIIFWAHDRFGGYAQSGLLAEITPAAAFQDK--LYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLL-PNPPKTWEEI 133
Cdd:cd13655  53 AADVFAFANDQLGELVDAGAIYPLTGSAVDKIKntNSEATVDAVTYNGKLYGYPFTANTWFMYYDKSKLtEDDVKSLDTM 132

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y      134 paLDKELKAKGKSAlmFNLQEPYFTWPLIAADGGYAFkyAAGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSi 213
Cdd:cd13655 133 --LAKAPDAKGKVS--FDLSNSWYLYAFFFGAGCKLF--GNNGGDTAGCDFNNEKGVAVTNYLVDLVANPKFVNDADGD- 205

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y      214 AEAAFNKGETAMTINGPWAWSNI-DTSAVNYGVTVLPTFK--GQ--PSKPFVGVLSAGINAASPNKELAKEFLEnYLLTD 288
Cdd:cd13655 206 AISGLKDGTLGAGVSGPWDAANLkKALGDNYAVAKLPTYTlgGKdvQMKSFAGYKAIGVNSNTKNPEAAMALAD-YLTNE 284

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
6LES_Y      289 EGLEAV---NKDKPLGAVALKSyeEELAKDPRIAATMENAQKGEI-MPNIPQMSAFW 341
Cdd:cd13655 285 ESQLTRfekRGIGPTNKEAAES--DAVKADPAAKALIAQSNEASVvQPKLPKMSNFW 339
PotD COG0687
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism];
4-336 1.69e-15

Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism];


Pssm-ID: 440451 [Multi-domain]  Cd Length: 348  Bit Score: 76.87  E-value: 1.69e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y        4 EEGKLVIWINGdkGYNGlAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPA 83
Cdd:COG0687  27 AEGTLNVYNWG--GYID-PDVLEPFEKETGIKVVYDTYDSNEEMLAKLRAGGSGYDVVVPSDYFVARLIKAGLLQPLDKS 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y       84 --AAFQDkLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIpaLDKELkaKGKSALmfnLQEPYFTWPL 161
Cdd:COG0687 104 klPNLAN-LDPRFKDPPFDPGNVYGVPYTWGTTGIAYNTDKVKEPPTSWADL--WDPEY--KGKVAL---LDDPREVLGA 175

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y      162 IAADGGYAFkyaagkYDIKDVGVDNAGAKagltflvdLIKNKHMNA--DTDYSIAEAAFNKGET--AMTINGPWAWSNID 237
Cdd:COG0687 176 ALLYLGYDP------NSTDPADLDAAFEL--------LIELKPNVRafWSDGAEYIQLLASGEVdlAVGWSGDALALRAE 241

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y      238 TSAVNYgvtVLPTfkgqpSKPFVGVLSAGINAASPNKELAKEFLeNYLLTDEGLEAVNKDKPLGAV---ALKSYEEELAK 314
Cdd:COG0687 242 GPPIAY---VIPK-----EGALLWFDNMAIPKGAPNPDLAYAFI-NFMLSPEVAAALAEYVGYAPPnkaARELLPPELAA 312

                       330       340
                ....*....|....*....|..
6LES_Y      315 DPRIAATMENAQKGEIMPNIPQ 336
Cdd:COG0687 313 NPAIYPPEEVLDKLEFWNPLPP 334
AfuA COG1840
ABC-type Fe3+ transport system, periplasmic component [Inorganic ion transport and metabolism]; ...
 26-290 5.37e-14

ABC-type Fe3+ transport system, periplasmic component [Inorganic ion transport and metabolism];


Pssm-ID: 441445 [Multi-domain]  Cd Length: 286  Bit Score: 71.89  E-value: 5.37e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y       26 KKFEKDTGIKVTVEHPDKLEEkFPQVAATGDGP--DIIF-WAHDRFGGYAQSGLLAEITPA------AAFQDKLYpfTWd 96
Cdd:COG1840   3 EAFEKKTGIKVNVVRGGSGEL-LARLKAEGGNPpaDVVWsGDADALEQLANEGLLQPYKSPeldaipAEFRDPDG--YW- 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y       97 avryngkliaYPIAVEALSLIYNKDLLP--NPPKTWEEIpaLDKELKAKgksalmfnlqepyFTWPLIAADG-GYAFKYA 173
Cdd:COG1840  79 ----------FGFSVRARVIVYNTDLLKelGVPKSWEDL--LDPEYKGK-------------IAMADPSSSGtGYLLVAA 133

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y      174 AgkydikdvgVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAfNKGETAMTINGPWAWSNIDTSAVNYGVtVLPTFKG 253
Cdd:COG1840 134 L---------LQAFGEEKGWEWLKGLAANGARVTGSSSAVAKAV-ASGEVAIGIVNSYYALRAKAKGAPVEV-VFPEDGT 202

                       250       260       270
                ....*....|....*....|....*....|....*..
6LES_Y      254 qpskpFVGVLSAGINAASPNKELAKEFLEnYLLTDEG 290
Cdd:COG1840 203 -----LVNPSGAAILKGAPNPEAAKLFID-FLLSDEG 233
PBP2_PotD_PotF_like cd13590
The periplasmic-binding component of ABC transporters involved in uptake of polyamines; ...
 23-286 5.44e-10

The periplasmic-binding component of ABC transporters involved in uptake of polyamines; possess the type 2 periplasmic binding fold; This family represents the periplasmic substrate-binding domain that functions as the primary high-affinity receptors of ABC-type polyamine transport systems. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, and plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270308 [Multi-domain]  Cd Length: 315  Bit Score: 59.94  E-value: 5.44e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y       23 EVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGP-DIIFWAHDRFGGYAQSGLLAEITPAA-AFQDKLYPFTWDAVRY 100
Cdd:cd13590  14 EVLKAFEKETGVKVNYDTYDSNEEMLAKLRAGGGSGyDLVVPSDYMVERLIKQGLLEPLDHSKlPNLKNLDPQFLNPPYD 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y      101 NGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEiPALDKELkaKGKSAlMFNLQEPYFTWPLIAAdgGYAFkyaagkYDIK 180
Cdd:cd13590  94 PGNRYSVPYQWGTTGIAYNKDKVKEPPTSWDL-DLWDPAL--KGRIA-MLDDAREVLGAALLAL--GYSP------NTTD 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y      181 DVGVDNAGAKagltflvdLIKNKHMNADTDYSIAEAAFNKGET--AMTINGPWAWSNIDTSAVNYgvtVLPTFKGQpskp 258
Cdd:cd13590 162 PAELAAAAEL--------LIKQKPNVRAFDSDSYVQDLASGEIwlAQAWSGDALQANRENPNLKF---VIPKEGGL---- 226

                       250       260
                ....*....|....*....|....*...
6LES_Y      259 fVGVLSAGINAASPNKELAKEFLeNYLL 286
Cdd:cd13590 227 -LWVDNMAIPKGAPNPELAHAFI-NFLL 252
PBP2_AlgQ_like_1 cd13580
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 26-298 2.18e-09

Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 periplasmic binding fold; This subgroup includes uncharacterized periplasmic-binding proteins that are closely related to high molecular weight (HMW) alginate bining proteins (AlgQ1 and AlgQ2) found in gram-negative soil bacteria. The HMW alginate uptake system is composed of a novel pit formed on the cell surface and a pit-dependent ATP-binding cassette (ABC) transporter in the inner membrane. The transportation of HMW alginate from the pit to the ABC transporter is mediated by periplasmic HMW alginate-binding proteins (AlgQ1 and AlgQ2). Alginate is an anionic polysaccharide that is made up of alpha-L-mannuronate and its 5'-epimer, alpha-L-guluronate. Alginate is present in the cell walls of brown seaweeds, where it forms a viscous gum by binding water. Alginate is also produced by two bacteria genera Pseudomonas and Azotobacter. AlgQ1 and AlgQ2 belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. However, unlike other bacterial periplasmic-binding proteins that deliver small solutes to ABC transporters, AlgQ1/2 can bind a macromolecule and may have specificity for either sugar or a certain type of polysaccharide.


Pssm-ID: 270298 [Multi-domain]  Cd Length: 471  Bit Score: 58.88  E-value: 2.18e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y       26 KKFEKDTGIKVTVEH--PDKLEEKFPQVAATGDGPDIIF-WAHDRFGGYAQSGLLAEITPaaaFQDKLYP--------FT 94
Cdd:cd13580  26 KYLEEKTNIDVKVKWvpDSSYDEKLNLALASGDLPDIVVvNDPQLSITLVKQGALWDLTD---YLDKYYPnlkkiieqEG 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y       95 WDAVRYNGKLIAYPIAVEALS---LIYNKDLLPN----PPKTWEEipaLDKELKAkgksalmFNLQEP-------YFTWP 160
Cdd:cd13580 103 WDSASVDGKIYGIPRKRPLIGrngLWIRKDWLDKlgleVPKTLDE---LYEVAKA-------FTEKDPdgngkkdTYGLT 172

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y      161 LIAADGGYAFKYAAGKYDIKDVG--VDNAG----------AKAGLTFLVDLIKNKHMNAD---TDYSIAEAAFNKGETAM 225
Cdd:cd13580 173 DTKDLIGSGFTGLFGAFGAPPNNwwKDEDGklvpgsiqpeMKEALKFLKKLYKEGLIDPEfavNDGTKANEKFISGKAGI 252

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y      226 TInGPWAWSNIDTSAVNYGV-----TVLPTFKGqPSKPFVGVLSAG------INAASPNKELAKEFL------ENYLLTD 288
Cdd:cd13580 253 FV-GNWWDPAWPQASLKKNDpdaewVAVPIPSG-PDGKYGVWAESGvngffvIPKKSKKPEAILKLLdflsdpEVQKLLD 330

                       330
                ....*....|
6LES_Y      289 EGLEAVNKDK 298
Cdd:cd13580 331 YGIEGVHYTV 340
PBP2_polyamine_RpCGA009 cd13589
The periplasmic-binding component of an uncharacterized ABC transport system from ...
 22-301 1.03e-08

The periplasmic-binding component of an uncharacterized ABC transport system from Rhodopseudomonas palustris CGA009 and related proteins; contains the type 2 periplasmic-binding fold; This group represents the periplasmic binding domain that serves as the primary high-affinity receptor of an uncharacterized ABC-type polyamine transporter from Rhodopseudomonas palustris Cga009 and related proteins from other bacteria. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, and plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270307 [Multi-domain]  Cd Length: 268  Bit Score: 55.70  E-value: 1.03e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y       22 AEVGKKFEKDTGIKVTVEHPDKLEEKfPQVAATGDGP--DIIFWAHDRFGGYAQSGLLAEITPAA-AFQDKLYPFTWDAV 98
Cdd:cd13589  17 KAVIEPFEKETGIKVVYDTGTSADRL-AKLQAQAGNPqwDVVDLDDGDAARAIAEGLLEPLDYSKiPNAAKDKAPAALKT 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y       99 RYngkliAYPIAVEALSLIYNKDLLPNPPKTWeeiPALDKELKAKgksalmfnlqepyFTWPLIAADGGYAFKYAAGKYD 178
Cdd:cd13589  96 GY-----GVGYTLYSTGIAYNTDKFKEPPTSW---WLADFWDVGK-------------FPGPRILNTSGLALLEAALLAD 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y      179 ikdvGVDNA--GAKAGLTFLVDLIKnkhmNADTDY-SIAEAA--FNKGETAMtinGPWAWSNIDtSAVNYGVTVLPTFKG 253
Cdd:cd13589 155 ----GVDPYplDVDRAFAKLKELKP----NVVTWWtSGAQLAqlLQSGEVDM---APAWNGRAQ-ALIDAGAPVAFVWPK 222

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
6LES_Y      254 qpSKPFVGVLSAGINAASPNKELAKEFLeNYLLTDEGLEAVNKDKPLG 301
Cdd:cd13589 223 --EGAILGPDTLAIVKGAPNKELAMKFI-NFALSPEVQAALAEALGYG 267
PBP2_Fe3_thiamine_like cd13518
Substrate binding domain of iron and thiamine transporters-like, a member of the type 2 ...
 7-295 8.12e-08

Substrate binding domain of iron and thiamine transporters-like, a member of the type 2 periplasmic binding fold superfamily; The periplasmic iron binding protein plays an essential role in the iron uptake pathway of Gram-negative pathogenic bacteria from the Pasteurellaceae and Neisseriaceae families and is critical for survival of these pathogens within the host. On the other hand, thiamin is an essential cofactor in all living systems. Thiamin diphosphate (ThDP)-dependent enzymes play an important role in carbohydrate and branched-chain amino acid metabolism. Most prokaryotes, plants, and fungi can synthesize thiamin, but it is not synthesized in vertebrates. These periplasmic domains have high affinities for their respective substrates and serve as the primary receptor for transport. After binding iron and thiamine with high affinity, they interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The iron- and thiamine-binding proteins belong to the PBPI2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270236 [Multi-domain]  Cd Length: 260  Bit Score: 53.07  E-value: 8.12e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y        7 KLVIWINGDKgyNGLAEVGKKFEKDTGIKVTVEHpDKLEEKFPQVAATGDGP--DIiFWAHD--RFGGYAQSGLLAEITP 82
Cdd:cd13518   1 ELVVYTASDR--DFAEPVLKAFEEKTGIKVKAVY-DGTGELANRLIAEKNNPqaDV-FWGGEiiALEALKEEGLLEPYTP 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y       83 AAAFQDklyPFTWDAVryNGKLiaYPIAVEALSLIYNKDLLPNP--PKTWEEIpaLDKELKakgksalmfnlqepyftwp 160
Cdd:cd13518  77 KVIEAI---PADYRDP--DGYW--VGFAARARVFIYNTDKLKEPdlPKSWDDL--LDPKWK------------------- 128

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y      161 liaadggyafkyaaGKYdikdVGVDNAGAKAGLTFLVDLIKNKHmNADTDYSIAEAAFNKGE--------TAMTINGPWA 232
Cdd:cd13518 129 --------------GKI----VYPTPLRSGTGLTHVAALLQLMG-EEKGGWYLLKLLANNGKpvagnsdaYDLVAKGEVA 189

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
6LES_Y      233 WSNIDT----SAVNYGVTVLPTFKgqPSKPFVGVLSAGINAASPNKELAKEFLEnYLLTDEGLEAVN 295
Cdd:cd13518 190 VGLTDTyyaaRAAAKGEPVEIVYP--DQGALVIPEGVALLKGAPNPEAAKKFID-FLLSPEGQKALA 253
PBP2_polyamine_2 cd13587
The periplasmic-binding component of an uncharacterized ABC transporter involved in uptake of ...
 22-126 1.77e-07

The periplasmic-binding component of an uncharacterized ABC transporter involved in uptake of polyamines; contains the type 2 periplasmic binding fold; This family represents the periplasmic binding domain that functions as the primary polyamine receptor of an uncharacterized ABC-type transport system. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, and plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270305 [Multi-domain]  Cd Length: 292  Bit Score: 52.44  E-value: 1.77e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y       22 AEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAAT-GDGPDIIFWAHDRFGGYAQSGLLAEITPAAAFQDKLYPFTWDAVR- 99
Cdd:cd13587  13 EDLLEKFENETGIKVQVTTSNNNEEMISKLRATgGGGFDLAQPSQRIAPNYEEFGLYQPIDESKIKVAQFPPSLLESTKl 92

                        90       100       110
                ....*....|....*....|....*....|
6LES_Y      100 ---YNGKLIAYPIAVEALSLIYNKDLLPNP 126
Cdd:cd13587  93 gttINGKRYAVPFDWGTEGLTVNSTKAPDV 122
PBP2_polyamine_1 cd13588
The periplasmic-binding component of an uncharacterized ABC transporter involved in uptake of ...
 16-143 6.67e-06

The periplasmic-binding component of an uncharacterized ABC transporter involved in uptake of polyamines; contains the type 2 periplasmic binding fold; This group represents the periplasmic binding domain that functions as the primary high-affinity receptor of an uncharactertized ABC-type polyamine transport system. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, and plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270306 [Multi-domain]  Cd Length: 279  Bit Score: 47.29  E-value: 6.67e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y       16 KGYnGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPAA-AFQDKLYP-F 93
Cdd:cd13588   8 PGY-ADPDWVTAFEEATGCKVVVKFFGSEDEMVAKLRSGGGDYDVVTPSGDALLRLIAAGLVQPIDTSKiPNYANIDPrL 86

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
6LES_Y       94 TW-DAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPAlDKELKAK 143
Cdd:cd13588  87 RNlPWLTVDGKVYGVPYDWGANGLAYNTKKVKTPPTSWLALLW-DPKYKGR 136
PBP2_PotD_PotF_like_3 cd13664
TThe periplasmic substrate-binding component of an uncharacterized active transport system ...
 23-84 3.90e-05

TThe periplasmic substrate-binding component of an uncharacterized active transport system closely related to spermidine and putrescine transporters; contains the type 2 periplasmic binding fold; This family represents the periplasmic substrate-binding domain that functions as the primary high-affinity receptors of ABC-type polyamine transport systems. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, and plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270382 [Multi-domain]  Cd Length: 315  Bit Score: 45.04  E-value: 3.90e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
6LES_Y       23 EVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPAA 84
Cdd:cd13664  14 ELLDKFEKETGIKVTLDTYDSNETLLAKLKAGGQGYDVVVPSDSFVPILIKEGLLEPLDKSQ 75
PBP2_AlgQ_like cd13521
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 24-290 7.23e-05

Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 periplasmic binding fold; This family represents the periplasmic-binding component of high molecular weight (HMW) alginate uptake system found in gram-negative soil bacteria and related proteins. The HMW alginate uptake system is composed of a novel pit formed on the cell surface and a pit-dependent ATP-binding cassette (ABC) transporter in the inner membrane. In Sphingomonas sp. A1, the transportation of HMW alginate from the pit to the ABC transporter is mediated by periplasmic HMW alginate-binding proteins AlgQ1 and AlgQ2. Alginate is an anionic polysaccharide that is made up of alpha-L-mannuronate and its 5'-epimer, alpha-L-guluronate. Alginate is present in the cell walls of brown seaweeds, where it forms a viscous gum by binding water. Alginate is also produced by two bacteria genera Pseudomonas and Azotobacter. AlgQ1 and AlgQ2 belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. However, unlike other bacterial periplasmic-binding proteins that deliver small solutes to ABC transporters, AlgQ1/2 can bind a macromolecule and may have specificity for either sugar or a certain type of polysaccharide.


Pssm-ID: 270239 [Multi-domain]  Cd Length: 483  Bit Score: 44.75  E-value: 7.23e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y       24 VGKKFEKDTGIK-VTVEHPDKL-EEKFPQVAATGDGPDII---FWAhDRFGGYAQSGLLAEITP-------AAAFQDKLY 91
Cdd:cd13521  22 VAKEIEKLTNVKlEIVAVTAATsQQKLNLMLASGDLPDIVgadYLK-DKFIAYGMEGAFLPLSKyidqypnLKAFFKQHP 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y       92 --PFTWDAVRYNGKLIAY--PIAVEALSLIYNKDLLPN----PPKTWEEIPALDKELKAKGKSAlmfNLQEPyfTWPLIA 163
Cdd:cd13521 101 dvLRASTASDGKIYLIPYepPKDVPNQGYFIRKDWLDKlnlkTPKTLDELYNVLKAFKEKDPNG---NGKAD--EIPFID 175

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y      164 ADGGY-AFK-------YAAGKYDIKDVGVDNA---------GAKAGLTFLVDLIKNKHMNAD---TDYSIAEAAFNKGET 223
Cdd:cd13521 176 RDPLYgAFRlinswgaRSAGGSTDSDWYEDNGkfkhpfaseEYKDGMKYMNKLYTEGLIDKEsftQKDDQAEQKFSNGKL 255

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
6LES_Y      224 AMTINGPWAWSNIDTSAVNYGVTV---LPTFKGQPSKPFVGVLSAG--------INAASPNKELAKEFLeNYLLTDEG 290
Cdd:cd13521 256 GGFTHNWFASDNLFTAQLGKEKPMyilLPIAPAGNVKGRREEDSPGytgpdgvaISKKAKNPVAALKFF-DWLASEEG 332
PBP2_TbpA cd13545
Substrate binding domain of thiamin transporter, a member of the type 2 periplasmic binding ...
 23-294 2.66e-04

Substrate binding domain of thiamin transporter, a member of the type 2 periplasmic binding fold superfamily; Thiamin-binding protein TbpA is the periplasmic component of ABC-type transporter in E. coli, while the transmembrane permease and ATPase are ThiP and ThiQ, respectively. Thiamin (vitamin B1) is an essential confactor in all living systems that most prokaryotes, plants, and fungi can synthesized thiamin. However, in vertebrates, thiamine cannot be synthesized and must therefore be obtained through dietary absorption. In addition to thiamin biosynthesis, most organisms can import thiamin using specific transporters. After binding thiamine with high affinity, TbpA interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The thiamine-binding proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270263 [Multi-domain]  Cd Length: 269  Bit Score: 42.29  E-value: 2.66e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y       23 EVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGP--DIIFWAHDRFGGYAQS-GLLAEITPaaafqdKLYPFTWDAVR 99
Cdd:cd13545  19 EVKAEFEKETGCKVEFVKPGDAGELLNRLILEKNNPraDVVLGLDNNLLSRALKeGLFEPYRS------PALDVVPEVPV 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y      100 YNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEipaldkelkakgksalmfnLQEPYFTWPLIAADG-----GYAFKYAA 174
Cdd:cd13545  93 FDPEDRLIPYDYGYLAFNYDKKKFKEPPLSLED-------------------LTAPEYKGLIVVQDPrtsspGLGFLLWT 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y      175 gkydIKDVGVDNAgakagLTFLVDLIKNKHMNADTdYSIAEAAFNKGETAMTI---NGPwAWSNIDTSAVNYGVTVLPTf 251
Cdd:cd13545 154 ----IAVFGEEGY-----LEYWKKLKANGVTVTPG-WSEAYGLFTTGEAPMVVsyaTSP-AYHVYYEKDLRYTAVIFPE- 221

                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
6LES_Y      252 kGQpskpFVGVLSAGINAASPNKELAKEFLEnYLLTDEGLEAV 294
Cdd:cd13545 222 -GH----YRQVEGAGILKGAKNPELAKKFVD-FLLSPEFQEVI 258
PRK15046 PRK15046
2-aminoethylphosphonate ABC transporter substrate-binding protein; Provisional
 26-166 3.95e-04

2-aminoethylphosphonate ABC transporter substrate-binding protein; Provisional


Pssm-ID: 237887 [Multi-domain]  Cd Length: 349  Bit Score: 41.98  E-value: 3.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y        26 KKFEKDTGIKV---------TVEHPDKlEEKFPQVAATGDGPDIIFWAhdrfggyAQSGLLAEITPAAAfqDKLYPFTWD 96
Cdd:PRK15046  54 PAFTKATGIKVnyveagsgeVVNRAAK-EKSNPQADVLVTLPPFIQQA-------AAEGLLQPYSSVNA--KAVPAIAKD 123

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y        97 AvryNGKLiaYPIAVEALSLIYNKDLLPNPPKTWEEIpaLDKELKAKgksalmfnLQepYFTwPLIAADG 166
Cdd:PRK15046 124 A---DGTY--APFVNNYLSFIYNPKVLKTAPATWADL--LDPKFKGK--------LQ--YST-PGQAGDG 175
PBP2_polyamines cd13523
The periplasmic-binding component of ABC transporters involved in uptake of polyamines; ...
 27-143 5.21e-04

The periplasmic-binding component of ABC transporters involved in uptake of polyamines; possess the type 2 periplasmic binding fold; This family represents the periplasmic substrate-binding proteins that function as the primary high-affinity receptors of ABC-type polyamine transport systems. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, as well as plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270241 [Multi-domain]  Cd Length: 268  Bit Score: 41.27  E-value: 5.21e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y       27 KFEKDTGIKVTVEHPDKLEEKFPQVAATGDGP-DIIFWAHDRFGGYAQSGLLAEIT----PAAAFQDKLYPfTWDAVRYN 101
Cdd:cd13523  18 PFEKETGIKVVVDTAANSERMIKKLSAGGSGGfDLVTPSDSYTSRQLGVGLMQPIDksllPSWATLDPHLT-LAAVLTVP 96

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
6LES_Y      102 GKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPaLDKELKAK 143
Cdd:cd13523  97 GKKYGVPYQWGATGLVYNTDKVKAPPKSYAADL-DDPKYKGR 137
SBP_bac_6 pfam13343
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 58-296 9.54e-04

Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins.


Pssm-ID: 463852 [Multi-domain]  Cd Length: 247  Bit Score: 40.42  E-value: 9.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y         58 PDIIFWAHDRFGG------YAQSGLLAEITPAaafQDKLYP--FTWDAVRYNGKLIaYPIAVEALSLIYNKDLLPN--PP 127
Cdd:pfam13343   4 PDIILSAGDLFFDkrflekFIEEGLFQPLDSA---NLPNVPkdFDDEGLRDPDGYY-TPYGVGPLVIAYNKERLGGrpVP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y        128 KTWEEIpaLDKELKakgKSALMFNLqePYFTWPLIAADGGYafkyaagkydiKDVGVDnagakAGLTFLVDLIKNKHMNA 207
Cdd:pfam13343  80 RSWADL--LDPEYK---GKVALPGP--NVGDLFNALLLALY-----------KDFGED-----GVRKLARNLKANLHPAQ 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y        208 DTDYSiaeAAFNKGETAMTInGPWAWSNIdTSAVNYGVTVLPTFKGqpskPFVGVLSAGINAAspNKELAKEFLeNYLLT 287
Cdd:pfam13343 137 MVKAA---GRLESGEPAVYL-MPYFFADI-LPRKKKNVEVVWPEDG----ALVSPIFMLVKKG--KKELADPLI-DFLLS 204


                  ....*....
6LES_Y        288 DEGLEAVNK 296
Cdd:pfam13343 205 PEVQAILAK 213
PBP2_TpPotD_like cd13662
The periplasmic substrate-binding component of an ABC-type polyamine transport system from ...
 26-130 1.64e-03

The periplasmic substrate-binding component of an ABC-type polyamine transport system from Treponema pallidum and related proteins; contains the type 2 periplasmic binding fold; This group includes the polyamine-binding component of an ABC-type polyamine transport system from Treponema pallidum and closely related proteins, which is homologous to the spermidine-preferring periplasmic substrate-binding protein component (PotD)of ABC transport system. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, as well as plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270380  Cd Length: 312  Bit Score: 40.19  E-value: 1.64e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y       26 KKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITpaaafQDKLYPFTWDAVRYNGKLI 105
Cdd:cd13662  17 EDFEKETGIRVVYDYYASNEEMYAKLKIGGGGYDIVSPSGDYVSIMKKEGLLEKLD-----KSKLPNVKEEKDNLMEASK 91

                        90       100       110
                ....*....|....*....|....*....|...
6LES_Y      106 AY--------PIAVEALSLIYNKDLLPNPPKTW 130
Cdd:cd13662  92 IYdpgleysvPYMFGATGIAVNKKIVKNYFRKW 124
PBP2_AlgQ_like_4 cd13583
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 26-292 2.86e-03

Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 periplasmic binding fold; This subgroup includes uncharacterized periplasmic-binding proteins that are closely related to high molecular weight (HMW) alginate bining proteins (AlgQ1 and AlgQ2) found in gram-negative soil bacteria. The HMW alginate uptake system is composed of a novel pit formed on the cell surface and a pit-dependent ATP-binding cassette (ABC) transporter in the inner membrane. The transportation of HMW alginate from the pit to the ABC transporter is mediated by periplasmic HMW alginate-binding proteins (AlgQ1 and AlgQ2). Alginate is an anionic polysaccharide that is made up of alpha-L-mannuronate and its 5'-epimer, alpha-L-guluronate. Alginate is present in the cell walls of brown seaweeds, where it forms a viscous gum by binding water. Alginate is also produced by two bacteria genera Pseudomonas and Azotobacter. AlgQ1 and AlgQ2 belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. However, unlike other bacterial periplasmic-binding proteins that deliver small solutes to ABC transporters, AlgQ1/2 can bind a macromolecule and may have specificity for either sugar or a certain type of polysaccharide.


Pssm-ID: 270301 [Multi-domain]  Cd Length: 478  Bit Score: 39.65  E-value: 2.86e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y       26 KKFEKDTGIKVTVEH--PDKLEEKFPQVAATGDGPDII--FWaHDRFGGYAQSGLLAEITP----AAAFQDKLYPFTW-- 95
Cdd:cd13583  24 KEIEEKTNVKFKRTPipSSDYETKRSLLIASGDAPDIIpvLY-PGEENEFVASGALLPISDyldyMPNYKKYVEKWGLgk 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y       96 --DAVRY-NGKLIAYPIAVEA----LSLIYNKDLLPN----PPKTWEEIPALDKELKAK----------GKSALMFNLQE 154
Cdd:cd13583 103 elATGRQsDGKYYSLPGLHEDpgvqYSFLYRKDIFEKagikIPTTWDEFYAALKKLKEKypdsypysdrWNSNALLLIAA 182

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y      155 PYFTWPLIAADGGYAFKYAAGKYDIkdvGVDNAGAKAGLTFLVDLIKNKHMN----ADTDySIAEAAFNKGETAMTINGP 230
Cdd:cd13583 183 PAFGTTAGWGFSNYTYDPDTDKFVY---GATTDEYKDMLQYFNKLYAEGLLDpesfTQTD-DQAKAKFLNGKSFVITTNP 258

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
6LES_Y      231 WAWSNIDTSAV-----NYGVTVLPTFKGQ------PSKPFVGVLSAGINAASPNKELAKEFLeNYLLTDEGLE 292
Cdd:cd13583 259 QTVDELQRNLRaadggNYEVVSITPPAGPagkainGSRLENGFMISSKAKDSKNFEALLQFL-DWLYSDEGQE 330
TbpA COG4143
ABC-type thiamine transport system, periplasmic component TbpA [Coenzyme transport and ...
 22-141 3.77e-03

ABC-type thiamine transport system, periplasmic component TbpA [Coenzyme transport and metabolism];


Pssm-ID: 443315 [Multi-domain]  Cd Length: 343  Bit Score: 39.06  E-value: 3.77e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6LES_Y       22 AEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGP--DIIFWAHDRFGGYA-QSGLLAEITPAAAFQDKLyPFTWDAv 98
Cdd:COG4143  48 PWLKAAFEAECGCTLEFVAPGDGGELLNRLRLEGANPkaDVVLGLDNNLLARAlDTGLFAPHGVDALDALAL-PLAWDP- 125

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
6LES_Y       99 ryNGKLIayPIAVEALSLIYNKDLLPNPPKTWEEIPALDKELK 141
Cdd:COG4143 126 --DDRFV--PYDYGYFAFVYDKTKLLNPPESLEDLVDPEYKDK 164
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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