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Conserved domains on  [gi|291417114|gb|EFE90833|]
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ABC transporter, solute-binding protein [Oribacterium sp. oral taxon 078 str. F0262]

Protein Classification

ABC transporter substrate-binding protein( domain architecture ID 11447308)

ABC transporter substrate-binding protein functions as the initial receptor in the ABC transport of one or more from a variety of substrates including carbohydrates

Gene Ontology:  GO:0140359|GO:0042626|GO:0055052
PubMed:  26517916|24638992|25750732|26517916
SCOP:  3000083
TCDB:  3.A.1

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
 82-408 2.64e-37

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


:

Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 140.56  E-value: 2.64e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114  82 GKESKADGKGGKELRLVNGKIEVDAALKELAAKYEEET-GVKVNIESMGGGiNIQGTLKGYYQAGNMPDIFVNGAdPDFE 160
Cdd:COG1653   22 GGSGAAAAAGKVTLTVWHTGGGEAAALEALIKEFEAEHpGIKVEVESVPYD-DYRTKLLTALAAGNAPDVVQVDS-GWLA 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 161 NWCGQDLLEDLSDQP---------WVSDTDAAYKYkDGKIYGFPYTVEAIGLAYNADILEKAGID-PKSItgpESMKKAF 230
Cdd:COG1653  100 EFAAAGALVPLDDLLdddgldkddFLPGALDAGTY-DGKLYGVPFNTDTLGLYYNKDLFEKAGLDpPKTW---DELLAAA 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 231 ETLDSKKSELGLDAVIGYCAEATNLYWSTGNhlfgvyedeglkrddskyfDLLKDGGK--LDSDR----FEKYAEMVGlf 304
Cdd:COG1653  176 KKLKAKDGVYGFALGGKDGAAWLDLLLSAGG-------------------DLYDEDGKpaFDSPEaveaLEFLKDLVK-- 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 305 NKYSDPNLLvSGTYDQQILNFSSGKYAFVTQGSWIGATMTTDDKDayekagkFKVGMIPY-AFEEGQDTILTNSPSWWSV 383
Cdd:COG1653  235 DGYVPPGAL-GTDWDDARAAFASGKAAMMINGSWALGALKDAAPD-------FDVGVAPLpGGPGGKKPASVLGGSGLAI 306

                        330       340
                 ....*....|....*....|....*.
gi 291417114 384 FKN-DNAEEAKKFLNWVAGEKGQDIL 408
Cdd:COG1653  307 PKGsKNPEAAWKFLKFLTSPEAQAKW 332
 
Name Accession Description Interval E-value
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
 82-408 2.64e-37

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


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 140.56  E-value: 2.64e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114  82 GKESKADGKGGKELRLVNGKIEVDAALKELAAKYEEET-GVKVNIESMGGGiNIQGTLKGYYQAGNMPDIFVNGAdPDFE 160
Cdd:COG1653   22 GGSGAAAAAGKVTLTVWHTGGGEAAALEALIKEFEAEHpGIKVEVESVPYD-DYRTKLLTALAAGNAPDVVQVDS-GWLA 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 161 NWCGQDLLEDLSDQP---------WVSDTDAAYKYkDGKIYGFPYTVEAIGLAYNADILEKAGID-PKSItgpESMKKAF 230
Cdd:COG1653  100 EFAAAGALVPLDDLLdddgldkddFLPGALDAGTY-DGKLYGVPFNTDTLGLYYNKDLFEKAGLDpPKTW---DELLAAA 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 231 ETLDSKKSELGLDAVIGYCAEATNLYWSTGNhlfgvyedeglkrddskyfDLLKDGGK--LDSDR----FEKYAEMVGlf 304
Cdd:COG1653  176 KKLKAKDGVYGFALGGKDGAAWLDLLLSAGG-------------------DLYDEDGKpaFDSPEaveaLEFLKDLVK-- 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 305 NKYSDPNLLvSGTYDQQILNFSSGKYAFVTQGSWIGATMTTDDKDayekagkFKVGMIPY-AFEEGQDTILTNSPSWWSV 383
Cdd:COG1653  235 DGYVPPGAL-GTDWDDARAAFASGKAAMMINGSWALGALKDAAPD-------FDVGVAPLpGGPGGKKPASVLGGSGLAI 306

                        330       340
                 ....*....|....*....|....*.
gi 291417114 384 FKN-DNAEEAKKFLNWVAGEKGQDIL 408
Cdd:COG1653  307 PKGsKNPEAAWKFLKFLTSPEAQAKW 332
PBP2_UgpB cd14748
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ...
 106-479 1.75e-29

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: 119.32  E-value: 1.75e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 106 AALKELAAKYEEE-TGVKVNIESMGGGINIQGTLKGYYQAGNMPDIFVNGADpDFENWCGQDLLEDLSD--QPWVSDTD- 181
Cdd:cd14748   14 KALEELVDEFNKShPDIKVKAVYQGSYDDTLTKLLAALAAGTAPDVAQVDAS-WVAQLADSGALEPLDDyiDKDGVDDDd 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 182 ------AAYKYkDGKIYGFPYTVEAIGLAYNADILEKAGIDPksITGPESMKKAFETLDSKKSELGLDAVIGYCAEATNL 255
Cdd:cd14748   93 fypaalDAGTY-DGKLYGLPFDTSTPVLYYNKDLFEEAGLDP--EKPPKTWDELEEAAKKLKDKGGKTGRYGFALPPGDG 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 256 YWSTGNHLFGvyedeglkrDDSKYFDllKDGGK--LDSDRFEKYAE-MVGLFNKYSDPNLLVSGTYDQQilnFSSGKYAF 332
Cdd:cd14748  170 GWTFQALLWQ---------NGGDLLD--EDGGKvtFNSPEGVEALEfLVDLVGKDGVSPLNDWGDAQDA---FISGKVAM 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 333 VTQGSWIGATMTTDDKDAyekagKFKVGMIPYaFEEGQDTILTNSPSWWsVFKND--NAEEAKKFLNWVAGEKGQDILVN 410
Cdd:cd14748  236 TINGTWSLAGIRDKGAGF-----EYGVAPLPA-GKGKKGATPAGGASLV-IPKGSskKKEAAWEFIKFLTSPENQAKWAK 308

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 291417114 411 KAGFISPFKS-----CSFVAEDPFAQTIVDyqKAEKTSGWHWLGNKDGIAQNALGVVYQDYAQGNIKDAKAFTD 479
Cdd:cd14748  309 ATGYLPVRKSaaedpEEFLAENPNYKVAVD--QLDYAKPWGPPVPNGAEIRDELNEALEAALLGKKTPEEALKE 380
SBP_bac_8 pfam13416
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 110-428 5.25e-27

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


Pssm-ID: 433189 [Multi-domain]  Cd Length: 281  Bit Score: 109.80  E-value: 5.25e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114  110 ELAAKYEEETGVKVNIESMGGGiNIQGTLKGYYQAGNMPDIFVN-GADPDFENWCGQDLLEDLSDQPWVSDTDAAYKY-- 186
Cdd:pfam13416   1 ALAKAFEKKTGVTVEVEPQASN-DLQAKLLAAAAAGNAPDLDVVwIAADQLATLAEAGLLADLSDVDNLDDLPDALDAag 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114  187 KDGKIYGFPYTVEA-IGLAYNADILEKAGIDPKSItgpESMKKAFETLDSKKSELGldavigycaeatnlyWSTGNHLFG 265
Cdd:pfam13416  80 YDGKLYGVPYAASTpTVLYYNKDLLKKAGEDPKTW---DELLAAAAKLKGKTGLTD---------------PATGWLLWA 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114  266 VYEDEGLKRDDSKYFDLLKDGgkldsdrFEKYAEMVglfnkysdPNLLVSGTYDQQILNFSSGKYAFVTQGSWIGAtmtt 345
Cdd:pfam13416 142 LLADGVDLTDDGKGVEALDEA-------LAYLKKLK--------DNGKVYNTGADAVQLFANGEVAMTVNGTWAAA---- 202

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114  346 ddkdAYEKAGKfKVGMIPyafeeGQDTILTNSpSWWSVFKNDNAEE--AKKFLNWVAGEKGQDILVNKAGFISPFKSCS- 422
Cdd:pfam13416 203 ----AAKKAGK-KLGAVV-----PKDGSFLGG-KGLVVPAGAKDPRlaALDFIKFLTSPENQAALAEDTGYIPANKSAAl 271


                  ....*...
gi 291417114  423 --FVAEDP 428
Cdd:pfam13416 272 sdEVKADP 279
malE PRK09474
maltose/maltodextrin ABC transporter substrate-binding protein MalE;
108-219 3.84e-07

maltose/maltodextrin ABC transporter substrate-binding protein MalE;


Pssm-ID: 236533 [Multi-domain]  Cd Length: 396  Bit Score: 52.32  E-value: 3.84e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 108 LKELAAKYEEETGVKVNIESMGGginiqgtLKGYYQ----AGNMPDIFVNGADpDFENWCGQDLLEDLSDQPWVSD---- 179
Cdd:PRK09474  46 LAEVGKKFEKDTGIKVTVEHPDK-------LEEKFPqvaaTGDGPDIIFWAHD-RFGGYAQSGLLAEVTPSKAFKDklvp 117

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 291417114 180 -TDAAYKYkDGKIYGFPYTVEAIGLAYNADILEKAgidPKS 219
Cdd:PRK09474 118 fTWDAVRY-NGKLIGYPIAVEALSLIYNKDLVPTP---PKT 154
 
Name Accession Description Interval E-value
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
 82-408 2.64e-37

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


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 140.56  E-value: 2.64e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114  82 GKESKADGKGGKELRLVNGKIEVDAALKELAAKYEEET-GVKVNIESMGGGiNIQGTLKGYYQAGNMPDIFVNGAdPDFE 160
Cdd:COG1653   22 GGSGAAAAAGKVTLTVWHTGGGEAAALEALIKEFEAEHpGIKVEVESVPYD-DYRTKLLTALAAGNAPDVVQVDS-GWLA 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 161 NWCGQDLLEDLSDQP---------WVSDTDAAYKYkDGKIYGFPYTVEAIGLAYNADILEKAGID-PKSItgpESMKKAF 230
Cdd:COG1653  100 EFAAAGALVPLDDLLdddgldkddFLPGALDAGTY-DGKLYGVPFNTDTLGLYYNKDLFEKAGLDpPKTW---DELLAAA 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 231 ETLDSKKSELGLDAVIGYCAEATNLYWSTGNhlfgvyedeglkrddskyfDLLKDGGK--LDSDR----FEKYAEMVGlf 304
Cdd:COG1653  176 KKLKAKDGVYGFALGGKDGAAWLDLLLSAGG-------------------DLYDEDGKpaFDSPEaveaLEFLKDLVK-- 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 305 NKYSDPNLLvSGTYDQQILNFSSGKYAFVTQGSWIGATMTTDDKDayekagkFKVGMIPY-AFEEGQDTILTNSPSWWSV 383
Cdd:COG1653  235 DGYVPPGAL-GTDWDDARAAFASGKAAMMINGSWALGALKDAAPD-------FDVGVAPLpGGPGGKKPASVLGGSGLAI 306

                        330       340
                 ....*....|....*....|....*.
gi 291417114 384 FKN-DNAEEAKKFLNWVAGEKGQDIL 408
Cdd:COG1653  307 PKGsKNPEAAWKFLKFLTSPEAQAKW 332
PBP2_UgpB cd14748
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ...
 106-479 1.75e-29

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: 119.32  E-value: 1.75e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 106 AALKELAAKYEEE-TGVKVNIESMGGGINIQGTLKGYYQAGNMPDIFVNGADpDFENWCGQDLLEDLSD--QPWVSDTD- 181
Cdd:cd14748   14 KALEELVDEFNKShPDIKVKAVYQGSYDDTLTKLLAALAAGTAPDVAQVDAS-WVAQLADSGALEPLDDyiDKDGVDDDd 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 182 ------AAYKYkDGKIYGFPYTVEAIGLAYNADILEKAGIDPksITGPESMKKAFETLDSKKSELGLDAVIGYCAEATNL 255
Cdd:cd14748   93 fypaalDAGTY-DGKLYGLPFDTSTPVLYYNKDLFEEAGLDP--EKPPKTWDELEEAAKKLKDKGGKTGRYGFALPPGDG 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 256 YWSTGNHLFGvyedeglkrDDSKYFDllKDGGK--LDSDRFEKYAE-MVGLFNKYSDPNLLVSGTYDQQilnFSSGKYAF 332
Cdd:cd14748  170 GWTFQALLWQ---------NGGDLLD--EDGGKvtFNSPEGVEALEfLVDLVGKDGVSPLNDWGDAQDA---FISGKVAM 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 333 VTQGSWIGATMTTDDKDAyekagKFKVGMIPYaFEEGQDTILTNSPSWWsVFKND--NAEEAKKFLNWVAGEKGQDILVN 410
Cdd:cd14748  236 TINGTWSLAGIRDKGAGF-----EYGVAPLPA-GKGKKGATPAGGASLV-IPKGSskKKEAAWEFIKFLTSPENQAKWAK 308

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 291417114 411 KAGFISPFKS-----CSFVAEDPFAQTIVDyqKAEKTSGWHWLGNKDGIAQNALGVVYQDYAQGNIKDAKAFTD 479
Cdd:cd14748  309 ATGYLPVRKSaaedpEEFLAENPNYKVAVD--QLDYAKPWGPPVPNGAEIRDELNEALEAALLGKKTPEEALKE 380
PBP2_TMBP_like cd13585
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ...
 105-474 5.06e-29

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: 117.89  E-value: 5.06e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 105 DAALKELAAKYEEE-TGVKVNIESMGGGiniqgtlkGYYQ-------AGNMPDIFVNGaDPDFENWCGQDLLEDLSD--Q 174
Cdd:cd13585   13 TAALKKLIDAFEKEnPGVKVEVVPVPYD--------DYWTklttaaaAGTAPDVFYVD-GPWVPEFASNGALLDLDDyiE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 175 PWVSDTD-----AAYKYKDGKIYGFPYTVEAIGLAYNADILEKAGIDPKsitGPESMKKAFEtlDSKKSELGLDAVIGYC 249
Cdd:cd13585   84 KDGLDDDfppglLDAGTYDGKLYGLPFDADTLVLFYNKDLFDKAGPGPK---PPWTWDELLE--AAKKLTDKKGGQYGFA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 250 AEAtnlyWSTGNHLFGVYedegLKRDDSKYFDLLKDGGKLDSDRFEKYAE-MVGLFNKYSDPNlLVSGTYDQQILNFSSG 328
Cdd:cd13585  159 LRG----GSGGQTQWYPF----LWSNGGDLLDEDDGKATLNSPEAVEALQfYVDLYKDGVAPS-SATTGGDEAVDLFASG 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 329 KYAFVTQGSWIGATMTTDDKDayekaGKFKVGMIPYAFEEGQDTILTNSPswWSVFKN-DNAEEAKKFLNWVAGEKGQDI 407
Cdd:cd13585  230 KVAMMIDGPWALGTLKDSKVK-----FKWGVAPLPAGPGGKRASVLGGWG--LAISKNsKHPEAAWKFIKFLTSKENQLK 302

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 291417114 408 LVNKAGFISPFKSCSFVAEDPFAQTIVDYQKAEKTSGWHWLGNKDG------IAQNALGVVYQDYAQGNIKDA 474
Cdd:cd13585  303 LGGAAGPAALAAAAASAAAPDAKPALALAAAADALAAAVPPPVPPPwpevypILSEALQEALLGALGKSPEEA 375
SBP_bac_8 pfam13416
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 110-428 5.25e-27

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


Pssm-ID: 433189 [Multi-domain]  Cd Length: 281  Bit Score: 109.80  E-value: 5.25e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114  110 ELAAKYEEETGVKVNIESMGGGiNIQGTLKGYYQAGNMPDIFVN-GADPDFENWCGQDLLEDLSDQPWVSDTDAAYKY-- 186
Cdd:pfam13416   1 ALAKAFEKKTGVTVEVEPQASN-DLQAKLLAAAAAGNAPDLDVVwIAADQLATLAEAGLLADLSDVDNLDDLPDALDAag 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114  187 KDGKIYGFPYTVEA-IGLAYNADILEKAGIDPKSItgpESMKKAFETLDSKKSELGldavigycaeatnlyWSTGNHLFG 265
Cdd:pfam13416  80 YDGKLYGVPYAASTpTVLYYNKDLLKKAGEDPKTW---DELLAAAAKLKGKTGLTD---------------PATGWLLWA 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114  266 VYEDEGLKRDDSKYFDLLKDGgkldsdrFEKYAEMVglfnkysdPNLLVSGTYDQQILNFSSGKYAFVTQGSWIGAtmtt 345
Cdd:pfam13416 142 LLADGVDLTDDGKGVEALDEA-------LAYLKKLK--------DNGKVYNTGADAVQLFANGEVAMTVNGTWAAA---- 202

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114  346 ddkdAYEKAGKfKVGMIPyafeeGQDTILTNSpSWWSVFKNDNAEE--AKKFLNWVAGEKGQDILVNKAGFISPFKSCS- 422
Cdd:pfam13416 203 ----AAKKAGK-KLGAVV-----PKDGSFLGG-KGLVVPAGAKDPRlaALDFIKFLTSPENQAALAEDTGYIPANKSAAl 271


                  ....*...
gi 291417114  423 --FVAEDP 428
Cdd:pfam13416 272 sdEVKADP 279
MalE COG2182
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
56-435 1.71e-26

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


Pssm-ID: 441785 [Multi-domain]  Cd Length: 410  Bit Score: 111.19  E-value: 1.71e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114  56 CGssqsdsagssaaktdesageSKADGKESKADGKGGKELRLVNGKIEVDaALKELAAKYEEETGVKVNIESMGGGiNIQ 135
Cdd:COG2182   22 CG--------------------SGSSSSGSSSAAGAGGTLTVWVDDDEAE-ALEEAAAAFEEEPGIKVKVVEVPWD-DLR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 136 GTLKGYYQAGNMPDIFVnGADPDFENWCGQDLLEDLSDQpwVSDTD-------AAYKYkDGKIYGFPYTVEAIGLAYNAD 208
Cdd:COG2182   80 EKLTTAAPAGKGPDVFV-GAHDWLGELAEAGLLAPLDDD--LADKDdflpaalDAVTY-DGKLYGVPYAVETLALYYNKD 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 209 ILEKAgiDPKSitgpesmkkaFETLDSKKSELGLDAVIGYCAEATNLY------WSTGNHLFGVyedeglKRDDSKYFDL 282
Cdd:COG2182  156 LVKAE--PPKT----------WDELIAAAKKLTAAGKYGLAYDAGDAYyfypflAAFGGYLFGK------DGDDPKDVGL 217

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 283 LKDGGKldsDRFEKYAEMVGlfNKYSDPNLlvsgTYDQQILNFSSGKYAFVTQGSWigatmttdDKDAYEKAGKFKVGMI 362
Cdd:COG2182  218 NSPGAV---AALEYLKDLIK--DGVLPADA----DYDAADALFAEGKAAMIINGPW--------AAADLKKALGIDYGVA 280

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 363 PY-AFEEGQDtiltnSPSW-----WSVFKN-DNAEEAKKFLNWVAGEKGQDILVNKAGFISPFKSC---SFVAEDPFAQT 432
Cdd:COG2182  281 PLpTLAGGKP-----AKPFvgvkgFGVSAYsKNKEAAQEFAEYLTSPEAQKALFEATGRIPANKAAaedAEVKADPLIAA 355


                 ...
gi 291417114 433 IVD 435
Cdd:COG2182  356 FAE 358
PBP2_XBP1_like cd14749
The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; ...
 105-486 3.98e-22

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: 97.84  E-value: 3.98e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 105 DAALKELAAKYEEET-GVKVNIESMGGGiNIQGTLKGYYQAGNMPDIFVNGADPDFENWCGQDLLEDLSDqPWVSDTD-- 181
Cdd:cd14749   14 KKYMDELIADFEKENpNIKVKVVVFPYD-NYKTKLKTAVAAGEGPDVFNLWPGGWLAEFVKAGLLLPLTD-YLDPNGVdk 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 182 -------AAYKYkDGKIYGFPYTVEAIGLAYNADILEKAGIDpksiTGPESMKKAFEtlDSKKSELGLDAVIGYcaeATN 254
Cdd:cd14749   92 rflpglaDAVTF-NGKVYGIPFAARALALFYNKDLFEEAGGV----KPPKTWDELIE--AAKKDKFKAKGQTGF---GLL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 255 LYWSTGNhlfgvYEDEGLKRDDS--KYFDLLKDGGKLDSDRF----EKYAEMVglFNKYSDPNLLvSGTYDQQILNFSSG 328
Cdd:cd14749  162 LGAQGGH-----WYFQYLVRQAGggPLSDDGSGKATFNDPAFvqalQKLQDLV--KAGAFQEGFE-GIDYDDAGQAFAQG 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 329 KYAFVTQGSWIGATMTTDdkdayEKAGKFKVGMIPYAfeEGQDTILTNSPSWWSVFKN---DNAEEAKKFLNWVAGEKGQ 405
Cdd:cd14749  234 KAAMNIGGSWDLGAIKAG-----EPGGKIGVFPFPTV--GKGAQTSTIGGSDWAIAISangKKKEAAVKFLKYLTSPEVM 306

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 406 DILVNKAGfISPFKSCSFVAEDP---FAQTIVDYQKAEKTSGWHWLGNKDGIAQNALGVVyqDYAQGNIKDAKAFTDTMS 482
Cdd:cd14749  307 KQYLEDVG-LLPAKEVVAKDEDPdpvAILGPFADVLNAAGSTPFLDEYWPAAAQVHKDAV--QKLLTGKIDPEQVVKQAQ 383


                 ....
gi 291417114 483 QVCA 486
Cdd:cd14749  384 SAAA 387
SBP_bac_1 pfam01547
Bacterial extracellular solute-binding protein; This family also includes the bacterial ...
 99-405 2.48e-19

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: 88.24  E-value: 2.48e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114   99 NGKIEVDAALKELAAKYEEE-TGVKVNIESMGGGiNIQGTLKGYYQAGNMPDIFVNGADPDFENWCGQDLLEDLSDqpwv 177
Cdd:pfam01547   1 AASLTEAAALQALVKEFEKEhPGIKVEVESVGSG-SLAQKLTTAIAAGDGPADVFASDNDWIAELAKAGLLLPLDD---- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114  178 sDTDAAYKYKDGKIYGFPYTVEAIGLAYNADILEKAGIDPksitgpesmKKAFETLDSKKSELGLDAVIGYCAEATNLYW 257
Cdd:pfam01547  76 -YVANYLVLGVPKLYGVPLAAETLGLIYNKDLFKKAGLDP---------PKTWDELLEAAKKLKEKGKSPGGAGGGDASG 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114  258 STGNHLFGVYEDEGLKRDDSKYFDLLKDGGKlDSDRFEKYAEMVGLFNKYSDPNLLVSGTYDQQILNFSSGKYAFVTQGS 337
Cdd:pfam01547 146 TLGYFTLALLASLGGPLFDKDGGGLDNPEAV-DAITYYVDLYAKVLLLKKLKNPGVAGADGREALALFEQGKAAMGIVGP 224

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 291417114  338 WIGATMTTDDKDAYEKA----GKFKVGMIPYAFEEGQDTIltnsPSWWSVFKN-DNAEEAKKFLNWVAGEKGQ 405
Cdd:pfam01547 225 WAALAANKVKLKVAFAApapdPKGDVGYAPLPAGKGGKGG----GYGLAIPKGsKNKEAAKKFLDFLTSPEAQ 293
PBP2_MalE cd14747
Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes ...
 105-435 9.32e-18

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: 85.06  E-value: 9.32e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 105 DAALKELAAKYEEET-GVKVNIES--MGGGIN-IQGTLkgyyQAGNMPDI----------FVN-GADPDFenwcgQDLLE 169
Cdd:cd14747   13 AELLKELADEFEKENpGIEVKVQVlpWGDAHTkITTAA----ASGDGPDVvqlgntwvaeFAAmGALEDL-----TPYLE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 170 DLS-DQPWVSDTDAAYKYkDGKIYGFPYTVEAIGLAYNADILEKAGIDpksitgpesmkKAFETLDS-----KKSELGLD 243
Cdd:cd14747   84 DLGgDKDLFPGLVDTGTV-DGKYYGVPWYADTRALFYRTDLLKKAGGD-----------EAPKTWDEleaaaKKIKADGP 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 244 AVIGYCAEATNLYWstgnHLFG--VYEDEG-LKRDDSKYFDLLKDGGKldsDRFEKYAEMVGlfNKYSDPNLLVSGTydQ 320
Cdd:cd14747  152 DVSGFAIPGKNDVW----HNALpfVWGAGGdLATKDKWKATLDSPEAV---AGLEFYTSLYQ--KGLSPKSTLENSA--D 220

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 321 QILNFSSGKYAFVTQGSWIGATMTTDDKDAYEKAGKF----KVGMIPYAFEEGQDtiltnspswWSVFKN-DNAEEAKKF 395
Cdd:cd14747  221 VEQAFANGKVAMIISGPWEIGAIREAGPDLAGKWGVAplpgGPGGGSPSFAGGSN---------LAVFKGsKNKDLAWKF 291

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 291417114 396 LNWVAGEKGQDILVNKAGFISPFKSC---SFVAEDPFAQTIVD 435
Cdd:cd14747  292 IEFLSSPENQAAYAKATGMLPANTSAwddPSLANDPLLAVFAE 334
PBP2_Maltose_binding_like cd13586
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
 105-420 1.52e-16

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: 81.19  E-value: 1.52e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 105 DAALKELAAKYEEETGVKVNIESmGGGINIQGTLKGYYQAGNMPDIFVnGADPDFENWCGQDLLEDLSDQPWVSDTD--- 181
Cdd:cd13586   12 LEYLKELAEEFEKKYGIKVEVVY-VDSGDTREKFITAGPAGKGPDVFF-GPHDWLGELAAAGLLAPIPEYLAVKIKNlpv 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 182 --AAYKYkDGKIYGFPYTVEAIGLAYNADILEKAgidPKSItgpESMKKAfetldSKKSELGLDAVIGYCAEATNLYWST 259
Cdd:cd13586   90 alAAVTY-NGKLYGVPVSVETIALFYNKDLVPEP---PKTW---EELIAL-----AKKFNDKAGGKYGFAYDQTNPYFSY 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 260 ------GNHLFGV----YEDEGLKRDDSkyfdllKDGGKLDSDRFEKYaemvglfnKYSDPNLlvsgTYDQQILNFSSGK 329
Cdd:cd13586  158 pflaafGGYVFGEnggdPTDIGLNNEGA------VKGLKFIKDLKKKY--------KVLPPDL----DYDIADALFKEGK 219

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 330 YAFVTQGSWigatmttdDKDAYEKAG-KFKVGMIPyAFEEGQD--------TILTNSPSwwsvfknDNAEEAKKFLNWVA 400
Cdd:cd13586  220 AAMIINGPW--------DLADYKDAGiNFGVAPLP-TLPGGKQaapfvgvqGAFVSAYS-------KNKEAAVEFAEYLT 283

                        330       340
                 ....*....|....*....|
gi 291417114 401 GEKGQDILVNKAGFISPFKS 420
Cdd:cd13586  284 SDEAQLLLFEKTGRIPALKD 303
PBP2_CMBP cd13658
The periplasmic binding component of ABC transport systems specific for cyclo/maltodextrin; ...
 106-419 4.73e-14

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: 73.67  E-value: 4.73e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 106 AALKELAAKYEEETGVKVNIESMGGgINIQGTLKGYYQAGNMPDIFVNGADpDFENWCGQDLLEDLSDQPWVSD--TDAA 183
Cdd:cd13658   13 AFIKKIAKQYTKKTGVKVKLVEVDQ-LDQLEKLSLDGPAGKGPDVMVAPHD-RIGSAVLQGLLSPIKLSKDKKKgfTDQA 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 184 YKY--KDGKIYGFPYTVEAIGLAYNADILEKAgidPKSITGPESMKKAFETLDSKKSelgldaviGYCAEATNLYWSTGn 261
Cdd:cd13658   91 LKAltYDGKLYGLPAAVETLALYYNKDLVKNA---PKTFDELEALAKDLTKEKGKQY--------GFLADATNFYYSYG- 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 262 hLFGVYEDEGLKRDDSKYFdlLKDGGkLDSDRFEKYAEMVglfNKYSDPNLLVSGTYDQQILN-FSSGKYAFVTQGSWIG 340
Cdd:cd13658  159 -LLAGNGGYIFKKNGSDLD--INDIG-LNSPGAVKAVKFL---KKWYTEGYLPKGMTGDVIQGlFKEGKAAAVIDGPWAI 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 341 AtmttddkdAYEKAGK-FKVGMIP--------YAFEEGQDTILtnspSWWSvfknDNAEEAKKFLNWVAGEKGQDILVNK 411
Cdd:cd13658  232 Q--------EYQEAGVnYGVAPLPtlpngkpmAPFLGVKGWYL----SAYS----KHKEWAQKFMEFLTSKENLKKRYDE 295


                 ....*...
gi 291417114 412 AGFISPFK 419
Cdd:cd13658  296 TNEIPPRK 303
PBP2_TMBP cd14750
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; ...
 107-433 5.90e-14

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: 73.48  E-value: 5.90e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 107 ALKELAAKYEEET-GVKVNIESMGGGINiqGTLKGYYQ---AGNM-PDIFvnGADpDFenWCGQD----LLEDLSD--QP 175
Cdd:cd14750   15 LLKKAIAAFEKKHpDIKVEIEELPASSD--DQRQQLVTalaAGSSaPDVL--GLD-VI--WIPEFaeagWLLPLTEylKE 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 176 WVSD-----TDAAYKYkDGKIYGFPYTVEAIGLAYNADILEKAGIDPksitgPESMKKAFETldSKKSELGLDAVIGYCA 250
Cdd:cd14750   88 EEDDdflpaTVEANTY-DGKLYALPWFTDAGLLYYRKDLLEKYGPEP-----PKTWDELLEA--AKKRKAGEPGIWGYVF 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 251 EATN----------LYWSTGNHLFGvyedeglkrDDSKYFDLLKDGGKldsDRFEKYAEMVGlfNKYSDPNLLvsgTYDQ 320
Cdd:cd14750  160 QGKQyeglvcnfleLLWSNGGDIFD---------DDSGKVTVDSPEAL---EALQFLRDLIG--EGISPKGVL---TYGE 222

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 321 QILN--FSSGKYAFvtQGSWIGAtMTTDDKDAYEKAGKFKVGMIPYAFEEGQDTILTNspsW-WSVFKN-DNAEEAKKFL 396
Cdd:cd14750  223 EEARaaFQAGKAAF--MRNWPYA-YALLQGPESAVAGKVGVAPLPAGPGGGSASTLGG---WnLAISANsKHKEAAWEFV 296

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 291417114 397 NWVAGEKGQDILVNKAGFI----SPFKSCSFVAEDPFAQTI 433
Cdd:cd14750  297 KFLTSPEVQKRRAINGGLPptrrALYDDPEVLEAYPFLPAL 337
PBP2_GacH cd14751
The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; ...
 109-443 1.32e-12

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: 68.95  E-value: 1.32e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 109 KELAAKYEEET-GVKVNIESMGGGINIQGTLKGYyQAGNMPDIFvnGAD----PDFENwcgQDLLEDLSDQPWVSDTDA- 182
Cdd:cd14751   17 EKLIPAFEKEYpKIKVKAVRVPFDGLHNQIKTAA-AGGQAPDVM--RADiawvPEFAK---LGYLQPLDGTPAFDDIVDy 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 183 -----AYKYKDGKIYGFPYTVEAIGLAYNADILEKAGIDPksitgPESMKkafETLDSKKSELGLDAVIGYCAEATNLYW 257
Cdd:cd14751   91 lpgpmETNRYNGHYYGVPQVTNTLALFYNKRLLEEAGTEV-----PKTMD---ELVAAAKAIKKKKGRYGLYISGDGPYW 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 258 STG--NHLFGVYEDEGLKRddskyfdllkdgGKLDS-DRFEKYAEMVGLFNKYsdpnLLV---SGTYDQQILNFSSGKYA 331
Cdd:cd14751  163 LLPflWSFGGDLTDEKKAT------------GYLNSpESVRALETIVDLYDEG----AITpcaSGGYPNMQDGFKSGRYA 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 332 FVTQGSWigatMTTDDKDAYEKAGKFKVGMIPY-AFEEGQDTILTNSPswWSVFKN-DNAEEAKKFLNWVAGEKGQDILV 409
Cdd:cd14751  227 MIVNGPW----AYADILGGKEFKDPDNLGIAPVpAGPGGSGSPVGGED--LVIFKGsKNKDAAWKFVKFMSSAEAQALTA 300

                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 291417114 410 NKAGFIsPFKSCSF----VAEDPFAQtivDYQKAEKTS 443
Cdd:cd14751  301 AKLGLL-PTRTSAYespeVANNPMVA---AFKPALETA 334
PBP2_Maltodextrin cd13657
The periplasmic binding component of ABC transport system specific for maltodextrin; This ...
 105-415 3.96e-11

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: 64.32  E-value: 3.96e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 105 DAALKELAAKYEEETG---VKVNIESMGggiNIQGTLKGYYQAGNMPDIFVNGADpdfenWCGQ----DLLEDLSDqpwV 177
Cdd:cd13657   13 EDALQQIIDEFEAKYPvpnVKVPFEKKP---DLQNKLLTAIPAGEGPDLFIWAHD-----WIGQfaeaGLLVPISD---Y 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 178 SDTDAAYKYK---------DGKIYGFPYTVEAIGLAYNADILEKAgidPKSITGPESMKKAFETLDSKKSELGLDAVIGY 248
Cdd:cd13657   82 LSEDDFENYLptaveavtyKGKVYGLPEAYETVALIYNKALVDQP---PETTDELLAIMKDHTDPAAGSYGLAYQVSDAY 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 249 CAEAtnlyWSTGnhlFGVYedeglkrddskYFDLLKDGGKLDSDRFEKYAEmvgLFNKYSDPNLLVSGTYDQQILNFSSG 328
Cdd:cd13657  159 FVSA----WIFG---FGGY-----------YFDDETDKPGLDTPETIKGIQ---FLKDFSWPYMPSDPSYNTQTSLFNEG 217

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 329 KYAFVTQGSWIGATMttddkdayeKAGKFKVGMIPYAfeegqDTILTNSPSWWS------VFKND---NAEEAKKFLNWV 399
Cdd:cd13657  218 KAAMIINGPWFIGGI---------KAAGIDLGVAPLP-----TVDGTNPPRPYSgvegiyVTKYAerkNKEAALDFAKFF 283

                        330
                 ....*....|....*.
gi 291417114 400 AGEKGQDILVNKAGFI 415
Cdd:cd13657  284 TTAEASKILADENGYV 299
AfuA COG1840
ABC-type Fe3+ transport system, periplasmic component [Inorganic ion transport and metabolism]; ...
 111-416 9.37e-11

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


Pssm-ID: 441445 [Multi-domain]  Cd Length: 286  Bit Score: 62.65  E-value: 9.37e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 111 LAAKYEEETGVKVNIESMGGGiNIQGTLKGyyQAGNMP-DIFVNGADPDFENWCGQDLLEDLSDqPWVSDTDAAYKYKDG 189
Cdd:COG1840    1 LLEAFEKKTGIKVNVVRGGSG-ELLARLKA--EGGNPPaDVVWSGDADALEQLANEGLLQPYKS-PELDAIPAEFRDPDG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 190 KIYGFpyTVEAIGLAYNADILEKAGIdPKSI---TGPEsMKKAFETLDSKKSELGLdavigycaeatnlywstgNHLFGV 266
Cdd:COG1840   77 YWFGF--SVRARVIVYNTDLLKELGV-PKSWedlLDPE-YKGKIAMADPSSSGTGY------------------LLVAAL 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 267 YEDEGlkrdDSKYFDLLKdggkldsdrfekyaEMVGLFNKYSDpnllvSGTydQQILNFSSGKYAfvtqgswIGATMTTD 346
Cdd:COG1840  135 LQAFG----EEKGWEWLK--------------GLAANGARVTG-----SSS--AVAKAVASGEVA-------IGIVNSYY 182

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 291417114 347 dkDAYEKAGKFKVGMIPyaFEEGqdTILTNSPSwwSVFKN-DNAEEAKKFLNWVAGEKGQDILVNKAGFIS 416
Cdd:COG1840  183 --ALRAKAKGAPVEVVF--PEDG--TLVNPSGA--AILKGaPNPEAAKLFIDFLLSDEGQELLAEEGYEYP 245
PBP2_Fe3_thiamine_like cd13518
Substrate binding domain of iron and thiamine transporters-like, a member of the type 2 ...
 109-410 8.36e-10

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: 59.24  E-value: 8.36e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 109 KELAAKYEEETGVKVNIESMGGGInIQGTL---KGYYQAgnmpDIFVNGADPDFENWCGQDLLEDlSDQPWVSDTDAAYK 185
Cdd:cd13518   14 EPVLKAFEEKTGIKVKAVYDGTGE-LANRLiaeKNNPQA----DVFWGGEIIALEALKEEGLLEP-YTPKVIEAIPADYR 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 186 YKDGKIYGFpyTVEAIGLAYNADILEKAGIdPKSITgpesmkkafETLDSKKSELgldavIGYCAEATNlyWSTGNHLFG 265
Cdd:cd13518   88 DPDGYWVGF--AARARVFIYNTDKLKEPDL-PKSWD---------DLLDPKWKGK-----IVYPTPLRS--GTGLTHVAA 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 266 VYEDEGLKRDDSKYFDLLKDGGKldsdrfekyaemvglfnkYSDPNllvSGTYDQqilnFSSGKYAFVTqgswigatmtT 345
Cdd:cd13518  149 LLQLMGEEKGGWYLLKLLANNGK------------------PVAGN---SDAYDL----VAKGEVAVGL----------T 193

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 291417114 346 DDKDAY-EKAGKFKVGMIPyaFEEGqdTILTNSPSwwSVFKN-DNAEEAKKFLNWVAGEKGQDILVN 410
Cdd:cd13518  194 DTYYAArAAAKGEPVEIVY--PDQG--ALVIPEGV--ALLKGaPNPEAAKKFIDFLLSPEGQKALAA 254
PBP2_AlgQ_like cd13521
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 116-407 2.00e-09

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: 59.78  E-value: 2.00e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 116 EEETGVKVNIESMGGGINIQgTLKGYYQAGNMPDIFVNGADPDFENWCGQ-----DLLEDLSDQPWVS-------DTDAA 183
Cdd:cd13521   27 EKLTNVKLEIVAVTAATSQQ-KLNLMLASGDLPDIVGADYLKDKFIAYGMegaflPLSKYIDQYPNLKaffkqhpDVLRA 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 184 YKYKDGKIYGFPY----TVEAIGLAYNADILEKAGI-DPKSITGPESMKKAFETLDSKKSelGLDAVIGycaeaTNLYWS 258
Cdd:cd13521  106 STASDGKIYLIPYeppkDVPNQGYFIRKDWLDKLNLkTPKTLDELYNVLKAFKEKDPNGN--GKADEIP-----FIDRDP 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 259 TGNHLFGVYEDEGLKRDDSKYFDLLKDGGKLDSDRFEK-YAEMVGLFNKYSDPNLL----VSGTYDQQILNFSSGKyAFV 333
Cdd:cd13521  179 LYGAFRLINSWGARSAGGSTDSDWYEDNGKFKHPFASEeYKDGMKYMNKLYTEGLIdkesFTQKDDQAEQKFSNGK-LGG 257

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 291417114 334 TQGSWIGATMTTDDKDAYEKAGKFKVGMIPYAFEEGQDTILTNS-PSWWSVF---KNDNAEEAKKFLNWVAGEKGQDI 407
Cdd:cd13521  258 FTHNWFASDNLFTAQLGKEKPMYILLPIAPAGNVKGRREEDSPGyTGPDGVAiskKAKNPVAALKFFDWLASEEGREL 335
PBP2_polyamine_RpCGA009 cd13589
The periplasmic-binding component of an uncharacterized ABC transport system from ...
 105-417 6.06e-09

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: 56.85  E-value: 6.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 105 DAALKELAAKYEEETGVKVNIESmGGGINIQGTLKGyyQAGNMP-DIFVNGaDPDFENWCGQDLLEDLSDQPWVSDTDAA 183
Cdd:cd13589   13 DAQRKAVIEPFEKETGIKVVYDT-GTSADRLAKLQA--QAGNPQwDVVDLD-DGDAARAIAEGLLEPLDYSKIPNAAKDK 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 184 YKYKDGKIYGFPYTVEAIGLAYNADileKAGIDPKSitgpESMKKAFetlDSKKselgldaVIGYcaeatNLYWSTGNHL 263
Cdd:cd13589   89 APAALKTGYGVGYTLYSTGIAYNTD---KFKEPPTS----WWLADFW---DVGK-------FPGP-----RILNTSGLAL 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 264 FgvyedeglkrddskYFDLLKDGGK---LDSDR-FEKYAEMVglfnkysdPNLLVSGTYDQQILN-FSSGKYAFVTqgSW 338
Cdd:cd13589  147 L--------------EAALLADGVDpypLDVDRaFAKLKELK--------PNVVTWWTSGAQLAQlLQSGEVDMAP--AW 202

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 339 IGATmttddkDAYEKAGKfkvgMIPYAFEEGQDTILTNSpswWSVFKN-DNAEEAKKFLNWVAGEKGQDILVnKAGFISP 417
Cdd:cd13589  203 NGRA------QALIDAGA----PVAFVWPKEGAILGPDT---LAIVKGaPNKELAMKFINFALSPEVQAALA-EALGYGP 268
PBP2_AlgQ_like_1 cd13580
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 144-406 3.51e-07

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: 52.71  E-value: 3.51e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 144 AGNMPDIFVNGADPDFENWCGQDLLEDLSD-----QP----WVSDTDAAYKYKDGKIYGFPYTVEAI---GLAYNADILE 211
Cdd:cd13580   56 SGDLPDIVVVNDPQLSITLVKQGALWDLTDyldkyYPnlkkIIEQEGWDSASVDGKIYGIPRKRPLIgrnGLWIRKDWLD 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 212 KAGID-PKSITGPESMKKAFETLDSKKseLGLDAVIGYCAEATNLYWSTGNHL--FGVYEDEGLKRDDSK-YFDLLKDGG 287
Cdd:cd13580  136 KLGLEvPKTLDELYEVAKAFTEKDPDG--NGKKDTYGLTDTKDLIGSGFTGLFgaFGAPPNNWWKDEDGKlVPGSIQPEM 213

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 288 KldsDRFEKYAEMVGlfNKYSDPNLLVsGTYDQQILNFSSGKYAFV----TQGSWIGATMTTDDKDAYEKAGKFKVGmip 363
Cdd:cd13580  214 K---EALKFLKKLYK--EGLIDPEFAV-NDGTKANEKFISGKAGIFvgnwWDPAWPQASLKKNDPDAEWVAVPIPSG--- 284

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 291417114 364 yafEEGQDTILTNSPSW-WSVF--KNDNAEEAKKFLNWVAGEKGQD 406
Cdd:cd13580  285 ---PDGKYGVWAESGVNgFFVIpkKSKKPEAILKLLDFLSDPEVQK 327
PotD COG0687
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism];
89-237 3.79e-07

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


Pssm-ID: 440451 [Multi-domain]  Cd Length: 348  Bit Score: 51.84  E-value: 3.79e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114  89 GKGGKELRLVN--GKIEvdaalKELAAKYEEETGVKVNIESMGGGINIQGTLkgyyQAGNMP-DIFVngADPDF-ENWCG 164
Cdd:COG0687   25 AAAEGTLNVYNwgGYID-----PDVLEPFEKETGIKVVYDTYDSNEEMLAKL----RAGGSGyDVVV--PSDYFvARLIK 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 165 QDLLE--DLSDQPWVSDTDAAYK---YKDGKIYGFPYTVEAIGLAYNADILEKA-------------------------- 213
Cdd:COG0687   94 AGLLQplDKSKLPNLANLDPRFKdppFDPGNVYGVPYTWGTTGIAYNTDKVKEPptswadlwdpeykgkvallddprevl 173

                        170       180       190
                 ....*....|....*....|....*....|.
gi 291417114 214 -------GIDPKSITgPESMKKAFETLDSKK 237
Cdd:COG0687  174 gaallylGYDPNSTD-PADLDAAFELLIELK 203
malE PRK09474
maltose/maltodextrin ABC transporter substrate-binding protein MalE;
108-219 3.84e-07

maltose/maltodextrin ABC transporter substrate-binding protein MalE;


Pssm-ID: 236533 [Multi-domain]  Cd Length: 396  Bit Score: 52.32  E-value: 3.84e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 108 LKELAAKYEEETGVKVNIESMGGginiqgtLKGYYQ----AGNMPDIFVNGADpDFENWCGQDLLEDLSDQPWVSD---- 179
Cdd:PRK09474  46 LAEVGKKFEKDTGIKVTVEHPDK-------LEEKFPqvaaTGDGPDIIFWAHD-RFGGYAQSGLLAEVTPSKAFKDklvp 117

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 291417114 180 -TDAAYKYkDGKIYGFPYTVEAIGLAYNADILEKAgidPKS 219
Cdd:PRK09474 118 fTWDAVRY-NGKLIGYPIAVEALSLIYNKDLVPTP---PKT 154
PBP2_MBP cd13656
The periplasmic binding component of ABC tansport system specific for maltose; possess the ...
 108-210 1.64e-06

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: 50.29  E-value: 1.64e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 108 LKELAAKYEEETGVKVNIESMGGginIQGTLKGYYQAGNMPDIFVNGADpDFENWCGQDLLEDLSDQPWVSD-----TDA 182
Cdd:cd13656   16 LAEVGKKFEKDTGIKVTVEHPDK---LEEKFPQVAATGDGPDIIFWAHD-RFGGYAQSGLLAEITPDKAFQDklypfTWD 91

                         90       100
                 ....*....|....*....|....*...
gi 291417114 183 AYKYkDGKIYGFPYTVEAIGLAYNADIL 210
Cdd:cd13656   92 AVRY-NGKLIAYPIAVEALSLIYNKDLL 118
PBP2_ABC_oligosaccharides cd13522
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
 107-415 1.30e-05

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: 47.41  E-value: 1.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 107 ALKELAAKYEEET-GVKVNIESmGGGINIQGTLKGYYQAGNMPDIFVNGADpdfenWCGQ----DLLEDLS-----DQPW 176
Cdd:cd13522   15 AVNELIAKFEKAYpGITVEVTY-QDTEARRQFFSTAAAGGKGPDVVFGPSD-----SLGPfaaaGLLAPLDeyvskSGKY 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 177 VSDTDAAYKYkDGKIYGFPYTVEAIGLAYNADILekagidpksitgPESMKKAFETLDSKKSELGLDAVIGYCAEATNLY 256
Cdd:cd13522   89 APNTIAAMKL-NGKLYGVPVSVGAHLMYYNKKLV------------PKNPPKTWQELIALAQGLKAKNVWGLVYNQNEPY 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 257 WSTGnhLFGVYEDEGLKRDDSKYFDLLKDGGKLDSdrfekYAEMVGLFNKYsdpNLLVSGTYDQQI-LNFSSGKYAFVTQ 335
Cdd:cd13522  156 FFAA--WIGGFGGQVFKANNGKNNPTLDTPGAVEA-----LQFLVDLKSKY---KIMPPETDYSIAdALFKAGKAAMIIN 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 336 GSWigatmttdDKDAYEKAGKFKVGMIPY-AFEEGQDTILTNSPSWWSVFKN-DNAEEAKKFLNWVAGEKGQDILVNKAG 413
Cdd:cd13522  226 GPW--------DLGDYRQALKINLGVAPLpTFSGTKHAAPFVGGKGFGINKEsQNKAAAVEFVKYLTSYQAQLVLFDDAG 297


                 ..
gi 291417114 414 FI 415
Cdd:cd13522  298 DI 299
PBP2_AlgQ_like_4 cd13583
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 98-405 2.37e-05

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: 46.58  E-value: 2.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114  98 VNGKIEVDaalKELAAKYEEETGVKVNIE--SMGGGINIQGTLKGyyqAGNMPDIFVNGADPDFENWCGQDLLEDLSD-- 173
Cdd:cd13583   12 PNYPVKDD---WLIWKEIEEKTNVKFKRTpiPSSDYETKRSLLIA---SGDAPDIIPVLYPGEENEFVASGALLPISDyl 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 174 ----------QPW-VSDTDAAYKYKDGKIYGFPYTVEAIG----LAYNADILEKAGIDPKSITGP--ESMKKAFE-TLDS 235
Cdd:cd13583   86 dympnykkyvEKWgLGKELATGRQSDGKYYSLPGLHEDPGvqysFLYRKDIFEKAGIKIPTTWDEfyAALKKLKEkYPDS 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 236 -------KKSELGLDAVIGYCAEA------TNLYWSTGNHLFGVYEDEglkrddskyfdllkdggkldsdrfekYAEMVG 302
Cdd:cd13583  166 ypysdrwNSNALLLIAAPAFGTTAgwgfsnYTYDPDTDKFVYGATTDE--------------------------YKDMLQ 219

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 303 LFNKYSDPNLL----VSGTYDQQILNFSSGKYAFVTQGSWIGATMTTDDKDAYEkaGKFKVGMIP---------YAFEEG 369
Cdd:cd13583  220 YFNKLYAEGLLdpesFTQTDDQAKAKFLNGKSFVITTNPQTVDELQRNLRAADG--GNYEVVSITppagpagkaINGSRL 297

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 291417114 370 QDTILTNSpswwSVFKNDNAEEAKKFLNWVAGEKGQ 405
Cdd:cd13583  298 ENGFMISS----KAKDSKNFEALLQFLDWLYSDEGQ 329
PBP2_AlgQ_like_3 cd13582
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 111-410 6.35e-05

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: 270300 [Multi-domain]  Cd Length: 504  Bit Score: 45.39  E-value: 6.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 111 LAAKYEEETGVKVNIESMGGGINIQGTLkgYYQAGNMPD-IFVNGADPDFENWCGQDLLEDLSDQ------PWVSDTDA- 182
Cdd:cd13582   22 VAKKITELTGVTLEIEYLVGGEKQKIGL--MIASGDLPDlIYAKGDTDKLIEAGALVPLDDLIEKygpnikKWYGDYLLk 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 183 AYKYKDGKIYGFPYTVEAI-------GLAYNADILEKAGIdPKSITgPESMKKAFETLDSKKSELGLDAVIGY--CAEAT 253
Cdd:cd13582  100 KLRSEDGHIYYLPNYRVEDapwypngGFWLQHDVLKELGY-PKIKT-LDDYENLIKDYKKKYPTINGQPTIGFtaLTDDW 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 254 NLYWSTGNHLFGV-YEDEG-LKRDDSKYFDLLKDGGKLDSDRFEKYAEM--VGLFNKYSdpnllVSGTYDQQILNFSSGK 329
Cdd:cd13582  178 RFLISVTNPAFLAgYPNDGeVYVDPKTLKAKFHYTRPYYKEYYKWLNELwnEGLLDKES-----FTQKYDQYLAKIASGR 252

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 330 -YAFVTQGSWIGATMTTDDKDAYEKAgkfKVGMIPYAFEEG-QDTILTNSPS--WWSVF---KNDNAEEAKKFLNWVAGE 402
Cdd:cd13582  253 vLGFYDAGWDIGNAITALKAKGKDER---LYAYYPVAVGVDdKDYNYGDPGYlgGDGIAitkSCKDPERAFKFLDWLASE 329


                 ....*...
gi 291417114 403 KGQdILVN 410
Cdd:cd13582  330 EAQ-KLIN 336
PBP2_Fbp_like_1 cd13544
Substrate binding domain of a putative ferric iron transporter, a member of the type 2 ...
 105-408 1.23e-04

Substrate binding domain of a putative ferric iron transporter, a member of the type 2 periplasmic binding fold superfamily; The substrate domain of this group shows a high homology to the periplasmic component of ferric iron transporter (Fbp), but its biochemical characterization has not been performed. 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. After binding iron with high affinity, Fbp 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 ferric iron-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: 270262 [Multi-domain]  Cd Length: 292  Bit Score: 43.74  E-value: 1.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 105 DAALKELAAKYEEETGVKVNIESMGGGI---NIQgtlkgyYQAGN-MPDIFVNGADPDFENWCGQDLLEDLsDQPWVSDT 180
Cdd:cd13544   10 EEEAKAILEAFKKDTGIKVEFVRLSTGEalaRLE------AEKGNpQADVWFGGTADAHIQAKKEGLLEPY-KSPNADKI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 181 DAAYKYKDGKIYGFpyTVEAIGLAYNADILEKAGIDPksitgPESMKkafETLDSK-KSELGL-DAVI---GYCAEATNL 255
Cdd:cd13544   83 PAKFKDPDGYWTGI--YLGPLGFGVNTDELKEKGLPV-----PKSWE---DLLNPEyKGEIVMpNPASsgtAYTFLASLI 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 256 ywstgnHLFGvyEDEGlkrddskyFDLLKdggKLDSDrfekyaemVGLFNKysdpnllvSGTYDQQILnfSSGKYAfvtq 335
Cdd:cd13544  153 ------QLMG--EDEA--------WEYLK---KLNKN--------VGQYTK--------SGSAPAKLV--ASGEAA---- 191

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 291417114 336 gswIGATMTTDdkDAYEKAGKFKVGMIpyAFEEGQdtiltnspSWW----SVFKN-DNAEEAKKFLNWVAGEKGQDIL 408
Cdd:cd13544  192 ---IGISFLHD--ALKLKEQGYPIKII--FPKEGT--------GYEieavAIIKGaKNPEAAKAFIDWALSKEAQELL 254
ModA COG0725
ABC-type molybdate transport system, periplasmic Mo-binding protein ModA [Inorganic ion ...
 270-417 2.04e-04

ABC-type molybdate transport system, periplasmic Mo-binding protein ModA [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, periplasmic Mo-binding protein ModA is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 440489 [Multi-domain]  Cd Length: 253  Bit Score: 42.93  E-value: 2.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 270 EGLKRDDSKYFDLLKDGGKL-----DSDRFEKYAEMV----GLFNKYSDPnlLVSGTYDQQILNF-SSGKY-AFVTQGSw 338
Cdd:COG0725  114 KGNPADISSLEDLAKPGVRIaigdpKTVPYGKYAKEAlekaGLWDALKPK--LVLGENVRQVLAYvESGEAdAGIVYLS- 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 339 igatmttddkDAYEKAGKFKVGMIPYAFEEGQD---TILTNSPswwsvfkndNAEEAKKFLNWVAGEKGQDILVnKAGFI 415
Cdd:COG0725  191 ----------DALAAKGVLVVVELPAELYAPIVypaAVLKGAK---------NPEAAKAFLDFLLSPEAQAILE-KYGFE 250


                 ..
gi 291417114 416 SP 417
Cdd:COG0725  251 PP 252
PBP2_AlgQ1_2 cd13584
Periplasmic-binding component of alginate-specific ABC uptake system; contains the type 2 ...
 179-407 2.30e-04

Periplasmic-binding component of alginate-specific ABC uptake system; contains the type 2 periplasmic binding fold; This group represents the periplasmic-binding component of high molecular weight (HMW) alginate uptake system found in gram-negative soil bacteria such as Sphingomonas sp. A1. 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 includes 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: 270302 [Multi-domain]  Cd Length: 481  Bit Score: 43.58  E-value: 2.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 179 DTDAAYKYKDGKIYGFPY------TVEAIGLAYNADILEKAGID-PKSITGPESMKKAFETLDSKKSELGLDAVIgycae 251
Cdd:cd13584  105 DVKKAITTDDGNIYGFPYlpdgdvAKEARGYFIRKDWLDKLGLKtPSTIDEWYTVLKAFKERDPNGNGKADEVPL----- 179

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 252 aTNLYWSTGN-----HLFGVYEDEGLKRDDSKYfdllkdgGKLDsdrfEKYAEMVGLFNK-YS----DPNLLV--SGTYD 319
Cdd:cd13584  180 -ILTKPGYDEtgrliNAWGAYMDFYQENGKVKY-------GPLE----PGFKDFLKTMNQwYKegliDPDFFTrkAKARE 247

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 320 QQILNFSSGkyAFVTQgswIGATMTTDDKDAYEKAGKFKVGMIPYA------FEEGQDTILTNSPSWWSV-FKNDNAEEA 392
Cdd:cd13584  248 QNIMNGNIG--GFTHD---WFASTGTFNLALLKNVPDFKLVAVPPPvlnkgqTPYEEDSRQIAKGDGAAItASNKNPVLA 322

                        250
                 ....*....|....*
gi 291417114 393 KKFLNWVAGEKGQDI 407
Cdd:cd13584  323 IKWLDYAYSEEGRLL 337
SBP_bac_11 pfam13531
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 106-414 1.09e-03

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


Pssm-ID: 463911 [Multi-domain]  Cd Length: 225  Bit Score: 40.71  E-value: 1.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114  106 AALKELAAKYEEETGVKVNIESMGGginiqGTLKGYYQAGNMPDIFVnGADPDFenwcgqdlLEDLSDQPWVSDTDAAyk 185
Cdd:pfam13531  10 AALRELAAAFEAETGVKVVVSYGGS-----GKLAKQIANGAPADVFI-SADSAW--------LDKLAAAGLVVPGSRV-- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114  186 ykdgkiygfPYTVEAIGLAYNADilekagiDPKSITGPESMKKAfetldskkselglDAVIGYCAEATNLYwstgnhlfG 265
Cdd:pfam13531  74 ---------PLAYSPLVIAVPKG-------NPKDISGLADLLKP-------------GVRLAVADPKTAPS--------G 116

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114  266 VYEDEGLKRddskyfdllkdggkldsdrfekyaemVGLFNKYSDpNLLVSGTYDQQILNF-SSGKY-AFVTQGSWIgatm 343
Cdd:pfam13531 117 RAALELLEK--------------------------AGLLKALEK-KVVVLGENVRQALTAvASGEAdAGIVYLSEA---- 165

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 291417114  344 ttddkDAYEKAGKFKV------GMIPYAFeegQDTILTNSPswwsvfkndNAEEAKKFLNWVAGEKGQDILVnKAGF 414
Cdd:pfam13531 166 -----LFPENGPGLEVvplpedLNLPLDY---PAAVLKKAA---------HPEAARAFLDFLLSPEAQAILR-KYGF 224
PBP2_ModA_like_1 cd13538
Substrate binding domain of putative molybdate-binding protein;the type 2 periplasmic binding ...
 349-415 1.49e-03

Substrate binding domain of putative molybdate-binding protein;the type 2 periplasmic binding protein fold; This subfamily contains domains found in ModA proteins of putative ABC-type transporter. Molybdate transport system is comprised of a periplasmic binding protein, an integral membrane protein, and an energizer protein. These three proteins are coded by modA, modB, and modC genes, respectively. ModA proteins serve as initial receptors in the ABC transport of molybdate mostly in eubacteria and archaea. After binding molybdate 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 ModA 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: 270256 [Multi-domain]  Cd Length: 230  Bit Score: 39.98  E-value: 1.49e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 291417114 349 DAYEKAGKFKVGMIPyafEEGQDT------ILTNSPswwsvfkndNAEEAKKFLNWVAGEKGQDILvNKAGFI 415
Cdd:cd13538  171 DAKAASEKLKVITIP---EEYNVTatypiaVLKASK---------NPELARAFVDFLLSEEGQAIL-AEYGFG 230
PBP2_AlgQ_like_2 cd13581
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 105-235 2.00e-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: 270299 [Multi-domain]  Cd Length: 490  Bit Score: 40.77  E-value: 2.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 105 DAALKELAAKYEEETGVKVN---IESMGGGINIQGTLKGyyqaGNMPDIFVNGA--DPDFENWCGQDLLEDLSD-----Q 174
Cdd:cd13581   16 DYNENLFFKRLEEKTGIKIEwetVPEDAWAEKKNLMLAS----GDLPDAFLGAGasDADLMTYGKQGLFLPLEDlidkyA 91

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 291417114 175 PWVS-------DTDAAYKYKDGKIYGFPYTVEAIGLAY------NADILEKAGID-PKSITGPESMKKAFETLDS 235
Cdd:cd13581   92 PNLKalfdenpDIKAAITAPDGHIYALPSVNECYHCSYgqrmwiNKKWLDKLGLEmPTTTDELYEVLKAFKEQDP 166
PBP2_Fbp_like_5 cd13551
Substrate binding domain of an uncharacterized ferric iron transporter, a member of the type 2 ...
 149-221 3.00e-03

Substrate binding domain of an uncharacterized ferric iron transporter, 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. This periplasmic domain (Fbp) has high affinity for ferric iron and serves as the primary receptor for transport. After binding iron with high affinity, Fbp 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 ferric iron-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: 270269 [Multi-domain]  Cd Length: 267  Bit Score: 39.31  E-value: 3.00e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 291417114 149 DIFVNGADPDFENWCGQDLLEDLSDQpWVSDTDAAYKYKDGkiYGFPYTVEAIGLAYNADILEkAGIDPKSIT 221
Cdd:cd13551   52 DVVFGLNAVSFERLKKQGLLVPYTPS-WAGEIPSALSDGDG--YYYPLVQQPIVLAYNPDTMT-DPDAPKSWT 120
PBP2_PotD_PotF_like cd13590
The periplasmic-binding component of ABC transporters involved in uptake of polyamines; ...
 110-219 4.50e-03

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: 39.14  E-value: 4.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291417114 110 ELAAKYEEETGVKVNI------ESMGGGINiQGTLKGYyqagnmpDIFVnGADPDFENWCGQDLLE--DLSDQPWVSDTD 181
Cdd:cd13590   14 EVLKAFEKETGVKVNYdtydsnEEMLAKLR-AGGGSGY-------DLVV-PSDYMVERLIKQGLLEplDHSKLPNLKNLD 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 291417114 182 AAY---KYKDGKIYGFPYTVEAIGLAYNADileKAGIDPKS 219
Cdd:cd13590   85 PQFlnpPYDPGNRYSVPYQWGTTGIAYNKD---KVKEPPTS 122
PBP2_ModA3_like cd13517
Substrate binding domain of molybdate binding protein-like (ModA3), a member of the type 2 ...
 106-160 5.07e-03

Substrate binding domain of molybdate binding protein-like (ModA3), a member of the type 2 periplasmic binding fold superfamily; This subfamily contains molybdate binding protein-like (ModA3) domain of an ABC-type transporter. Molybdate transport system is comprised of a periplasmic binding protein, an integral membrane protein, and an energizer protein. These three proteins are coded by modA, modB, and modC genes, respectively. ModA proteins serve as initial receptors in the ABC transport of molybdate mostly in eubacteria and archaea. ModA transporters import molybdenum and tungsten from the environment in the form of the oxyanions molybdate (MoO(4) (2-)) and tungstate (WO(4) (2-)). After binding molybdate 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. In contrast to the structure of the two ModA homologs from Escherichia coli and Azotobacter vinelandii, where the oxygen atoms are tetrahedrally arrangted around the metal center, the structure of Pyrococcus furiosus ModA/WtpA (PfModA) has shown that a binding site for molybdate and tungstate where the central metal atom is in a hexacoordinate configuration. The ModA 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: 270235 [Multi-domain]  Cd Length: 223  Bit Score: 38.36  E-value: 5.07e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 291417114 106 AALK----ELAAKYEEETGVKVNIEsmGGGiniQGTLKGYYQAGNMPDIFVNGADPDFE 160
Cdd:cd13517    8 AGLKkpmeEIAKLFEKKTGIKVEVT--YGG---SGQLLSQIETSKKGDVFIPGSEDYME 61
 
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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