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Conserved domains on  [gi|1085662500|emb|SDH69087|]
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multiple sugar transport system substrate-binding protein [Leifsonia sp. 197AMF]

Protein Classification

ABC transporter substrate-binding protein( domain architecture ID 10201045)

ABC transporter substrate-binding protein with similarity to glycerol-3-phosphate (3GP) ABC transporter substrate-binding protein, which serves as the primary receptor for the uptake of 3GP and 3GP esters

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PBP2_UgpB cd14748
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ...
 47-415 1.29e-83

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: 261.46  E-value: 1.29e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500  47 TISFWNGWTGGAAPVLVpKLIDKFNSEHKNIVVKDVPMEWADIAR-KMPLAVKAGKGPDVAVGHGDDIATYAAQGLVLKA 125
Cdd:cd14748     1 EITFWHGMSGPDGKALE-ELVDEFNKSHPDIKVKAVYQGSYDDTLtKLLAALAAGTAPDVAQVDASWVAQLADSGALEPL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 126 DSIVKSLGYKADDFPEGLLDAGKYNGSQYAVPWSITPLGLYVNKDVLQAAGVDPNSIPQDKDSYLAALEKLKAAGVQGEw 205
Cdd:cd14748    80 DDYIDKDGVDDDDFYPAALDAGTYDGKLYGLPFDTSTPVLYYNKDLFEEAGLDPEKPPKTWDELEEAAKKLKDKGGKTG- 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 206 VDGYVFTGTF---EFESLLWQYGGDLFNKDVSKATFNSDAGVKALTWMTDLIKKGYSPADVAQDGNINALIAGKTAFNWN 282
Cdd:cd14748   159 RYGFALPPGDggwTFQALLWQNGGDLLDEDGGKVTFNSPEGVEALEFLVDLVGKDGVSPLNDWGDAQDAFISGKVAMTIN 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 283 GVWQTTN--TAFDKLKWQAVAVPQIGDEK-AVWSSSthWMFMNNKGQDKNKtAAAATFVKWM--NDNSADWPK-TGELPA 356
Cdd:cd14748   239 GTWSLAGirDKGAGFEYGVAPLPAGKGKKgATPAGG--ASLVIPKGSSKKK-EAAWEFIKFLtsPENQAKWAKaTGYLPV 315

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1085662500 357 KNSVRDDPK-LVQTYPNLKPFLDELPYAHYE-PIAPGITTVEATITVAVNEAITGKKDPKQ 415
Cdd:cd14748   316 RKSAAEDPEeFLAENPNYKVAVDQLDYAKPWgPPVPNGAEIRDELNEALEAALLGKKTPEE 376
 
Name Accession Description Interval E-value
PBP2_UgpB cd14748
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ...
 47-415 1.29e-83

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: 261.46  E-value: 1.29e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500  47 TISFWNGWTGGAAPVLVpKLIDKFNSEHKNIVVKDVPMEWADIAR-KMPLAVKAGKGPDVAVGHGDDIATYAAQGLVLKA 125
Cdd:cd14748     1 EITFWHGMSGPDGKALE-ELVDEFNKSHPDIKVKAVYQGSYDDTLtKLLAALAAGTAPDVAQVDASWVAQLADSGALEPL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 126 DSIVKSLGYKADDFPEGLLDAGKYNGSQYAVPWSITPLGLYVNKDVLQAAGVDPNSIPQDKDSYLAALEKLKAAGVQGEw 205
Cdd:cd14748    80 DDYIDKDGVDDDDFYPAALDAGTYDGKLYGLPFDTSTPVLYYNKDLFEEAGLDPEKPPKTWDELEEAAKKLKDKGGKTG- 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 206 VDGYVFTGTF---EFESLLWQYGGDLFNKDVSKATFNSDAGVKALTWMTDLIKKGYSPADVAQDGNINALIAGKTAFNWN 282
Cdd:cd14748   159 RYGFALPPGDggwTFQALLWQNGGDLLDEDGGKVTFNSPEGVEALEFLVDLVGKDGVSPLNDWGDAQDAFISGKVAMTIN 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 283 GVWQTTN--TAFDKLKWQAVAVPQIGDEK-AVWSSSthWMFMNNKGQDKNKtAAAATFVKWM--NDNSADWPK-TGELPA 356
Cdd:cd14748   239 GTWSLAGirDKGAGFEYGVAPLPAGKGKKgATPAGG--ASLVIPKGSSKKK-EAAWEFIKFLtsPENQAKWAKaTGYLPV 315

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1085662500 357 KNSVRDDPK-LVQTYPNLKPFLDELPYAHYE-PIAPGITTVEATITVAVNEAITGKKDPKQ 415
Cdd:cd14748   316 RKSAAEDPEeFLAENPNYKVAVDQLDYAKPWgPPVPNGAEIRDELNEALEAALLGKKTPEE 376
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
 8-341 8.72e-68

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


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 219.92  E-value: 8.72e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500   8 RAIAVAVTAGLGLALTACGSSSSGGGGDvssadytGPKVTISFWngWTGGAAPVLVPKLIDKFNSEHKNIVVKDVPMEWA 87
Cdd:COG1653     2 RRLALALAAALALALAACGGGGSGAAAA-------AGKVTLTVW--HTGGGEAAALEALIKEFEAEHPGIKVEVESVPYD 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500  88 DIARKMPLAVKAGKGPDVAVGHGDDIATYAAQGLVLKADSIVKSLGYKADDFPEGLLDAGKYNGSQYAVPWSITPLGLYV 167
Cdd:COG1653    73 DYRTKLLTALAAGNAPDVVQVDSGWLAEFAAAGALVPLDDLLDDDGLDKDDFLPGALDAGTYDGKLYGVPFNTDTLGLYY 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 168 NKDVLQAAGVDPnsiPQDKDSYLAALEKLKAAGvqGEWvdGYVFTGT--FEFESLLWQYGGDLFNKDvSKATFNSDAGVK 245
Cdd:COG1653   153 NKDLFEKAGLDP---PKTWDELLAAAKKLKAKD--GVY--GFALGGKdgAAWLDLLLSAGGDLYDED-GKPAFDSPEAVE 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 246 ALTWMTDLIKKGYSPADVAQ---DGNINALIAGKTAFNWNGVWQTTN--TAFDKLKWQAVAVPQI--GDEKAVWSSSTHW 318
Cdd:COG1653   225 ALEFLKDLVKDGYVPPGALGtdwDDARAAFASGKAAMMINGSWALGAlkDAAPDFDVGVAPLPGGpgGKKPASVLGGSGL 304

                         330       340
                  ....*....|....*....|...
gi 1085662500 319 MFMNNKgqdKNKtAAAATFVKWM 341
Cdd:COG1653   305 AIPKGS---KNP-EAAWKFLKFL 323
SBP_bac_8 pfam13416
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 65-373 5.71e-25

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


Pssm-ID: 433189 [Multi-domain]  Cd Length: 281  Bit Score: 103.64  E-value: 5.71e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500  65 KLIDKFNSEHkNIVVKDVPMEWADIARKMPLAVKAGKGPDVAV--GHGDDIATYAAQGLVLKADSIVKSlgykaDDFPEg 142
Cdd:pfam13416   1 ALAKAFEKKT-GVTVEVEPQASNDLQAKLLAAAAAGNAPDLDVvwIAADQLATLAEAGLLADLSDVDNL-----DDLPD- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 143 LLDAGKYNGSQYAVPWSI-TPLGLYVNKDVLQAAGVDPNSIpqdkDSYLAALEKLKAAGVQGEWVDGYVFTGtfefeslL 221
Cdd:pfam13416  74 ALDAAGYDGKLYGVPYAAsTPTVLYYNKDLLKKAGEDPKTW----DELLAAAAKLKGKTGLTDPATGWLLWA-------L 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 222 WQYGGDLFNKDVSKatfnsDAGVKALTWMTDLIKKGYSPAdvAQDGNINALIAGKTAFNWNGVWQTTNTAFDKLKWQAVa 301
Cdd:pfam13416 143 LADGVDLTDDGKGV-----EALDEALAYLKKLKDNGKVYN--TGADAVQLFANGEVAMTVNGTWAAAAAKKAGKKLGAV- 214

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1085662500 302 VPQIGdekAVWSSSTHWMFmnnkGQDKNKTAAAATFVKWMN--DNSADWPK-TGELPAKNSVRDDPKlVQTYPNL 373
Cdd:pfam13416 215 VPKDG---SFLGGKGLVVP----AGAKDPRLAALDFIKFLTspENQAALAEdTGYIPANKSAALSDE-VKADPAL 281
malE PRK09474
maltose/maltodextrin ABC transporter substrate-binding protein MalE;
92-289 1.65e-06

maltose/maltodextrin ABC transporter substrate-binding protein MalE;


Pssm-ID: 236533 [Multi-domain]  Cd Length: 396  Bit Score: 50.01  E-value: 1.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500  92 KMPLAVKAGKGPDVAVGHGDDIATYAAQGLV--LKADSIVKSlgyKADDFPeglLDAGKYNGSQYAVPWSITPLGLYVNK 169
Cdd:PRK09474   72 KFPQVAATGDGPDIIFWAHDRFGGYAQSGLLaeVTPSKAFKD---KLVPFT---WDAVRYNGKLIGYPIAVEALSLIYNK 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 170 DVLQAAgvdpnsiPQDKDSYLAALEKLKAAGVQG-EW-VDGYVFTGtfefeSLLWQYGGDLFNK-----DVSKATFNSDA 242
Cdd:PRK09474  146 DLVPTP-------PKTWEEIPALDKELKAKGKSAiMWnLQEPYFTW-----PLIAADGGYAFKFenggyDVKDVGVNNAG 213

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1085662500 243 GVKALTWMTDLIKKGYSPADVAQDGNINALIAGKTAFNWNGVWQTTN 289
Cdd:PRK09474  214 AKAGLQFLVDLVKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSN 260
 
Name Accession Description Interval E-value
PBP2_UgpB cd14748
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ...
 47-415 1.29e-83

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: 261.46  E-value: 1.29e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500  47 TISFWNGWTGGAAPVLVpKLIDKFNSEHKNIVVKDVPMEWADIAR-KMPLAVKAGKGPDVAVGHGDDIATYAAQGLVLKA 125
Cdd:cd14748     1 EITFWHGMSGPDGKALE-ELVDEFNKSHPDIKVKAVYQGSYDDTLtKLLAALAAGTAPDVAQVDASWVAQLADSGALEPL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 126 DSIVKSLGYKADDFPEGLLDAGKYNGSQYAVPWSITPLGLYVNKDVLQAAGVDPNSIPQDKDSYLAALEKLKAAGVQGEw 205
Cdd:cd14748    80 DDYIDKDGVDDDDFYPAALDAGTYDGKLYGLPFDTSTPVLYYNKDLFEEAGLDPEKPPKTWDELEEAAKKLKDKGGKTG- 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 206 VDGYVFTGTF---EFESLLWQYGGDLFNKDVSKATFNSDAGVKALTWMTDLIKKGYSPADVAQDGNINALIAGKTAFNWN 282
Cdd:cd14748   159 RYGFALPPGDggwTFQALLWQNGGDLLDEDGGKVTFNSPEGVEALEFLVDLVGKDGVSPLNDWGDAQDAFISGKVAMTIN 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 283 GVWQTTN--TAFDKLKWQAVAVPQIGDEK-AVWSSSthWMFMNNKGQDKNKtAAAATFVKWM--NDNSADWPK-TGELPA 356
Cdd:cd14748   239 GTWSLAGirDKGAGFEYGVAPLPAGKGKKgATPAGG--ASLVIPKGSSKKK-EAAWEFIKFLtsPENQAKWAKaTGYLPV 315

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1085662500 357 KNSVRDDPK-LVQTYPNLKPFLDELPYAHYE-PIAPGITTVEATITVAVNEAITGKKDPKQ 415
Cdd:cd14748   316 RKSAAEDPEeFLAENPNYKVAVDQLDYAKPWgPPVPNGAEIRDELNEALEAALLGKKTPEE 376
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
 8-341 8.72e-68

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


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 219.92  E-value: 8.72e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500   8 RAIAVAVTAGLGLALTACGSSSSGGGGDvssadytGPKVTISFWngWTGGAAPVLVPKLIDKFNSEHKNIVVKDVPMEWA 87
Cdd:COG1653     2 RRLALALAAALALALAACGGGGSGAAAA-------AGKVTLTVW--HTGGGEAAALEALIKEFEAEHPGIKVEVESVPYD 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500  88 DIARKMPLAVKAGKGPDVAVGHGDDIATYAAQGLVLKADSIVKSLGYKADDFPEGLLDAGKYNGSQYAVPWSITPLGLYV 167
Cdd:COG1653    73 DYRTKLLTALAAGNAPDVVQVDSGWLAEFAAAGALVPLDDLLDDDGLDKDDFLPGALDAGTYDGKLYGVPFNTDTLGLYY 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 168 NKDVLQAAGVDPnsiPQDKDSYLAALEKLKAAGvqGEWvdGYVFTGT--FEFESLLWQYGGDLFNKDvSKATFNSDAGVK 245
Cdd:COG1653   153 NKDLFEKAGLDP---PKTWDELLAAAKKLKAKD--GVY--GFALGGKdgAAWLDLLLSAGGDLYDED-GKPAFDSPEAVE 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 246 ALTWMTDLIKKGYSPADVAQ---DGNINALIAGKTAFNWNGVWQTTN--TAFDKLKWQAVAVPQI--GDEKAVWSSSTHW 318
Cdd:COG1653   225 ALEFLKDLVKDGYVPPGALGtdwDDARAAFASGKAAMMINGSWALGAlkDAAPDFDVGVAPLPGGpgGKKPASVLGGSGL 304

                         330       340
                  ....*....|....*....|...
gi 1085662500 319 MFMNNKgqdKNKtAAAATFVKWM 341
Cdd:COG1653   305 AIPKGS---KNP-EAAWKFLKFL 323
MalE COG2182
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
1-415 1.37e-62

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


Pssm-ID: 441785 [Multi-domain]  Cd Length: 410  Bit Score: 207.88  E-value: 1.37e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500   1 MKKRFAAraiAVAVTAGLGLALTACGSSSSGGGGDVSSADytGPKVTIsfwngWTGGAAPVLVPKLIDKFNSEHkNIVVK 80
Cdd:COG2182     1 MKRRLLA---ALALALALALALAACGSGSSSSGSSSAAGA--GGTLTV-----WVDDDEAEALEEAAAAFEEEP-GIKVK 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500  81 DVPMEWADIARKMPLAVKAGKGPDVAVGHGDDIATYAAQGLVLKADSIVKSlgykADDFPEGLLDAGKYNGSQYAVPWSI 160
Cdd:COG2182    70 VVEVPWDDLREKLTTAAPAGKGPDVFVGAHDWLGELAEAGLLAPLDDDLAD----KDDFLPAALDAVTYDGKLYGVPYAV 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 161 TPLGLYVNKDVLqaagvdPNSIPQDKDSYLAALEKLKAAGVQGEWVDgyvFTGTFEFESLLWQYGGDLFNK---DVSKAT 237
Cdd:COG2182   146 ETLALYYNKDLV------KAEPPKTWDELIAAAKKLTAAGKYGLAYD---AGDAYYFYPFLAAFGGYLFGKdgdDPKDVG 216

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 238 FNSDAGVKALTWMTDLIKKGYSPADVAQDGNINALIAGKTAFNWNGVWQTTN-TAFDKLKWQAVAVPQI--GDEKAVWSS 314
Cdd:COG2182   217 LNSPGAVAALEYLKDLIKDGVLPADADYDAADALFAEGKAAMIINGPWAAADlKKALGIDYGVAPLPTLagGKPAKPFVG 296

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 315 STHWMFMNNKgqdKNKTAAAAtFVKWMNDNSAD---WPKTGELPAKNSVRDDPKlVQTYPNLKPFLDELPYAHYEPIAPG 391
Cdd:COG2182   297 VKGFGVSAYS---KNKEAAQE-FAEYLTSPEAQkalFEATGRIPANKAAAEDAE-VKADPLIAAFAEQAEYAVPMPNIPE 371

                         410       420
                  ....*....|....*....|....
gi 1085662500 392 ITTVEATITVAVNEAITGKKDPKQ 415
Cdd:COG2182   372 MGAVWTPLGTALQAIASGKADPAE 395
PBP2_TMBP_like cd13585
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ...
 47-415 1.10e-60

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: 202.25  E-value: 1.10e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500  47 TISFWNGWTGGAAPVLvPKLIDKFNSEHKNIVVKDVPMEWADIARKMPLAVKAGKGPDVAVGHGDDIATYAAQGLVLKAD 126
Cdd:cd13585     1 TLTFWDWGQPAETAAL-KKLIDAFEKENPGVKVEVVPVPYDDYWTKLTTAAAAGTAPDVFYVDGPWVPEFASNGALLDLD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 127 SIVKSLGYKaDDFPEGLLDAGKYNGSQYAVPWSITPLGLYVNKDVLQAAGVDPnSIPQDKDSYLAALEKLKAAGVQgewV 206
Cdd:cd13585    80 DYIEKDGLD-DDFPPGLLDAGTYDGKLYGLPFDADTLVLFYNKDLFDKAGPGP-KPPWTWDELLEAAKKLTDKKGG---Q 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 207 DGYVFTG----TFEFESLLWQYGGDLFNKDVSKATFNSDAGVKALTWMTDLIKKGYSPADVAQDGN--INALIAGKTAFN 280
Cdd:cd13585   155 YGFALRGgsggQTQWYPFLWSNGGDLLDEDDGKATLNSPEAVEALQFYVDLYKDGVAPSSATTGGDeaVDLFASGKVAMM 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 281 WNGVWQ--TTNTAFDKLKWQAVAVPQIGDEKAVWSSSTHWMFMNNKGQDKnktAAAATFVKWM----NDNSADWPKTGEL 354
Cdd:cd13585   235 IDGPWAlgTLKDSKVKFKWGVAPLPAGPGGKRASVLGGWGLAISKNSKHP---EAAWKFIKFLtskeNQLKLGGAAGPAA 311

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1085662500 355 PAKNSVRDDPKLVQTYPNLKPFLDELPYAHYEPIAPGITTVEATITVAVNEAITGK--KDPKQ 415
Cdd:cd13585   312 LAAAAASAAAPDAKPALALAAAADALAAAVPPPVPPPWPEVYPILSEALQEALLGAlgKSPEE 374
PBP2_XBP1_like cd14749
The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; ...
 47-415 3.74e-53

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: 182.58  E-value: 3.74e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500  47 TISFWNGWTGGAAPVLVPKLIDKFNSEHKNIVVKDVPMEWADIARKMPLAVKAGKGPDVA-VGHGDDIATYAAQGLVLKA 125
Cdd:cd14749     1 TITYWQYFTGDTKKKYMDELIADFEKENPNIKVKVVVFPYDNYKTKLKTAVAAGEGPDVFnLWPGGWLAEFVKAGLLLPL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 126 DSIVKSLGYKaDDFPEGLLDAGKYNGSQYAVPWSITPLGLYVNKDVLQAAGvdPNSIPQDKDSYLAALEKLKAA--GVQG 203
Cdd:cd14749    81 TDYLDPNGVD-KRFLPGLADAVTFNGKVYGIPFAARALALFYNKDLFEEAG--GVKPPKTWDELIEAAKKDKFKakGQTG 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 204 EWVDGYVFTGTFEFESLLWQYGGDLFNKDVS-KATFNSDAGVKALTWMTDLIKKGYSPADVAQ---DGNINALIAGKTAF 279
Cdd:cd14749   158 FGLLLGAQGGHWYFQYLVRQAGGGPLSDDGSgKATFNDPAFVQALQKLQDLVKAGAFQEGFEGidyDDAGQAFAQGKAAM 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 280 NWNGVWQTTN--TAFDKLKWQAVAVPQIGdEKAVWSSS--THWMFMNNKGQDknKTAAAATFVKWMNDNSAD---WPKTG 352
Cdd:cd14749   238 NIGGSWDLGAikAGEPGGKIGVFPFPTVG-KGAQTSTIggSDWAIAISANGK--KKEAAVKFLKYLTSPEVMkqyLEDVG 314

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1085662500 353 ELPAKNSVRDDPKLVQtYPNLKPFLDELPYAHYEPIA-PGITTVEATITVAVNEAITGKKDPKQ 415
Cdd:cd14749   315 LLPAKEVVAKDEDPDP-VAILGPFADVLNAAGSTPFLdEYWPAAAQVHKDAVQKLLTGKIDPEQ 377
PBP2_MalE cd14747
Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes ...
 47-415 9.48e-48

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: 167.88  E-value: 9.48e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500  47 TISFWNGWtGGAAPVLVPKLIDKFNSEHKNIVVKDVPMEWADIARKMPLAVKAGKGPDVAVGHGDDIATYAAQGlVLKAD 126
Cdd:cd14747     1 TLTVWAMG-NSAEAELLKELADEFEKENPGIEVKVQVLPWGDAHTKITTAAASGDGPDVVQLGNTWVAEFAAMG-ALEDL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 127 SIVKSLGYKADDFPEGLLDAGKYNGSQYAVPWSITPLGLYVNKDVLQAAGvdPNSIPQDKDSYLAALEKLKAagvQGEWV 206
Cdd:cd14747    79 TPYLEDLGGDKDLFPGLVDTGTVDGKYYGVPWYADTRALFYRTDLLKKAG--GDEAPKTWDELEAAAKKIKA---DGPDV 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 207 DGYVFTGT----FEFESLLWQYGGDLFNKDVSKATFNSDAGVKALTWMTDLIKKGYSPADVAQDG-NINALIA-GKTAFN 280
Cdd:cd14747   154 SGFAIPGKndvwHNALPFVWGAGGDLATKDKWKATLDSPEAVAGLEFYTSLYQKGLSPKSTLENSaDVEQAFAnGKVAMI 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 281 WNGVWQ----TTNTAFDKLKWQAVAVP-QIGDEKAVWSSSTHWMFMNNKgqdKNKTAAAAtFVKWM--NDNSADWPK-TG 352
Cdd:cd14747   234 ISGPWEigaiREAGPDLAGKWGVAPLPgGPGGGSPSFAGGSNLAVFKGS---KNKDLAWK-FIEFLssPENQAAYAKaTG 309

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1085662500 353 ELPAKNSVRDDPKLVQTyPNLKPFLDELPYAHYEPIAPGITTVEATITVAVNEAITG-KKDPKQ 415
Cdd:cd14747   310 MLPANTSAWDDPSLAND-PLLAVFAEQLKTGKATPATPEWGEIEAELVLVLEEVWIGvGADVED 372
PBP2_TMBP cd14750
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; ...
 65-415 1.74e-44

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: 159.38  E-value: 1.74e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500  65 KLIDKFNSEHKNIVVKDVPMEW-ADIARKMPLAVKAGKGPDVAVGHGDDI--ATYAAQGLVLKADSIVKSLGYkaDDFPE 141
Cdd:cd14750    18 KAIAAFEKKHPDIKVEIEELPAsSDDQRQQLVTALAAGSSAPDVLGLDVIwiPEFAEAGWLLPLTEYLKEEED--DDFLP 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 142 GLLDAGKYNGSQYAVPWSITPLGLYVNKDVLQAAGVDPnsiPQDKDSYLAALEKLKAagvQGEWVDGYVFTG-TFE---- 216
Cdd:cd14750    96 ATVEANTYDGKLYALPWFTDAGLLYYRKDLLEKYGPEP---PKTWDELLEAAKKRKA---GEPGIWGYVFQGkQYEglvc 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 217 -FESLLWQYGGDLFNKDVSKATFNSDAGVKALTWMTDLIKKGYSPADV---AQDGNINALIAGKTAF--NWNGVWQTTNT 290
Cdd:cd14750   170 nFLELLWSNGGDIFDDDSGKVTVDSPEALEALQFLRDLIGEGISPKGVltyGEEEARAAFQAGKAAFmrNWPYAYALLQG 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 291 AFDKL--KWQAVAVPQIGDEKAVwSSSTHWMFMNNKgQDKNKtAAAATFVKWMNdnSADWPKT-----GELPAKNSVRDD 363
Cdd:cd14750   250 PESAVagKVGVAPLPAGPGGGSA-STLGGWNLAISA-NSKHK-EAAWEFVKFLT--SPEVQKRraingGLPPTRRALYDD 324

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1085662500 364 PKLVQTYPNLKPFLDELPYAHYEPIAPGITTVEATITVAVNEAITGKKDPKQ 415
Cdd:cd14750   325 PEVLEAYPFLPALLEALENAVPRPVTPKYPEVSTAIQIALSAALSGQATPEE 376
PBP2_GacH cd14751
The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; ...
 47-415 6.20e-36

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: 135.97  E-value: 6.20e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500  47 TISFWNGwTGGAAPVLVPKLIDKFNSEHKNIVVKDVPMEWADIARKMPLAVKAGKGPDVAVGHGDDIATYAAQGLVLKAD 126
Cdd:cd14751     1 TITFWHT-SSDEEKVLYEKLIPAFEKEYPKIKVKAVRVPFDGLHNQIKTAAAGGQAPDVMRADIAWVPEFAKLGYLQPLD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 127 SIVksLGYKADDFPEGLLDAGKYNGSQYAVPWSITPLGLYVNKDVLQAAGVDPnsiPQDKDSYLAALEK-LKAAGVQGEW 205
Cdd:cd14751    80 GTP--AFDDIVDYLPGPMETNRYNGHYYGVPQVTNTLALFYNKRLLEEAGTEV---PKTMDELVAAAKAiKKKKGRYGLY 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 206 VDGyvfTGTFEFESLLWQYGGDLFNKDVSKATFNSDAGVKALTWMTDLIKKGYS--PADVAQDGNINALIAGKTAFNWNG 283
Cdd:cd14751   155 ISG---DGPYWLLPFLWSFGGDLTDEKKATGYLNSPESVRALETIVDLYDEGAItpCASGGYPNMQDGFKSGRYAMIVNG 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 284 VWQTTN-----TAFDKLKWQAVAVPQ--------IGDEKAVwsssthwMFMNNKGQDknktaAAATFVKWMNDNSADWPK 350
Cdd:cd14751   232 PWAYADilggkEFKDPDNLGIAPVPAgpggsgspVGGEDLV-------IFKGSKNKD-----AAWKFVKFMSSAEAQALT 299

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1085662500 351 TGE---LPAKNSVRDDPKLVQTyPNLKPFLDELPYAHYEPIAPGITTVEATITVAVNEAITGKKDPKQ 415
Cdd:cd14751   300 AAKlglLPTRTSAYESPEVANN-PMVAAFKPALETAVPRPPIPEWGELFEPLTLAFAKVLRGEKSPRE 366
PBP2_Maltodextrin cd13657
The periplasmic binding component of ABC transport system specific for maltodextrin; This ...
 47-415 8.67e-30

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: 119.02  E-value: 8.67e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500  47 TISFWNGWTGGAAPVLVpKLIDKFNSEHKNIVVKDVPMEWADIARKMPLAVKAGKGPDVAVGHGDDIATYAAQGLVLKAD 126
Cdd:cd13657     1 TITIWHALTGAEEDALQ-QIIDEFEAKYPVPNVKVPFEKKPDLQNKLLTAIPAGEGPDLFIWAHDWIGQFAEAGLLVPIS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 127 SIVKSLgyKADDFPEGLLDAGKYNGSQYAVPWSITPLGLYVNKDVLQAAgvdpnsiPQDKDSYLAALEKLKAAGVQGEwv 206
Cdd:cd13657    80 DYLSED--DFENYLPTAVEAVTYKGKVYGLPEAYETVALIYNKALVDQP-------PETTDELLAIMKDHTDPAAGSY-- 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 207 dGYVFT-GTFEFESLLWQ-YGGDLFNKDVSKATFNSDAGVKALTWMTDLIKKgYSPADVAQDGNINALIAGKTAFNWNGV 284
Cdd:cd13657   149 -GLAYQvSDAYFVSAWIFgFGGYYFDDETDKPGLDTPETIKGIQFLKDFSWP-YMPSDPSYNTQTSLFNEGKAAMIINGP 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 285 WQTTNTAFDKLKWQAVAVPQIGDEKAVWSSSTHWMFMNNKGQDKNKTAAAATFVKWMNDNS-----ADwpKTGELPAKNS 359
Cdd:cd13657   227 WFIGGIKAAGIDLGVAPLPTVDGTNPPRPYSGVEGIYVTKYAERKNKEAALDFAKFFTTAEaskilAD--ENGYVPAATN 304

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1085662500 360 VRDDPKlVQTYPNLKPFLDELPYAHYEPIAPGITTVEATITVAVNEAITGKKDPKQ 415
Cdd:cd13657   305 AYDDAE-VAADPVIAAFKAQAEHGVPMPNSPEMASVWGPVTLALAAVYQGGQDPQE 359
PBP2_Maltose_binding_like cd13586
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
 47-415 1.08e-29

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: 118.55  E-value: 1.08e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500  47 TISFWNGWTGGAAPVlvPKLIDKFNSEHkNIVVKDVPMEWADIARKMPLAVKAGKGPDVAVGHGDDIATYAAQGLVLKAD 126
Cdd:cd13586     1 TITVWTDEDGELEYL--KELAEEFEKKY-GIKVEVVYVDSGDTREKFITAGPAGKGPDVFFGPHDWLGELAAAGLLAPIP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 127 SIVKslgyKADDFPEGLLDAGKYNGSQYAVPWSITPLGLYVNKDVLqaagVDPnsiPQDKDSYLAALEK--LKAAGVQG- 203
Cdd:cd13586    78 EYLA----VKIKNLPVALAAVTYNGKLYGVPVSVETIALFYNKDLV----PEP---PKTWEELIALAKKfnDKAGGKYGf 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 204 --EWVDGYVFTGtfefesLLWQYGGDLF---NKDVSKATFNSDAGVKALTWMTDLIKK-GYSPADVAQDGNINALIAGKT 277
Cdd:cd13586   147 ayDQTNPYFSYP------FLAAFGGYVFgenGGDPTDIGLNNEGAVKGLKFIKDLKKKyKVLPPDLDYDIADALFKEGKA 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 278 AFNWNGVWQTTNTAFDKLKWQAVAVPQIgdEKAVWS---SSTHWMFMNNKGQDKnktAAAATFVKWMNDNSAD---WPKT 351
Cdd:cd13586   221 AMIINGPWDLADYKDAGINFGVAPLPTL--PGGKQAapfVGVQGAFVSAYSKNK---EAAVEFAEYLTSDEAQlllFEKT 295

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1085662500 352 GELPAKNSVRDDPkLVQTYPNLKPFLDELPYAHYEPIAPGITTVEATITVAVNEAITGKKDPKQ 415
Cdd:cd13586   296 GRIPALKDALNDA-AVKNDPLVKAFAEQAQYGVPMPNIPEMAAVWDAMGNALNLVASGKATPEE 358
PBP2_ABC_oligosaccharides cd13522
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
 47-415 1.55e-26

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: 109.81  E-value: 1.55e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500  47 TISFWNgWTGGAAPVLVPKLIDKFNSEHKNIVVKDVPMEWADIARKMPLAVKAGKGPDVAVGHGDDIATYAAQGLVLKAD 126
Cdd:cd13522     1 TITVWH-QYDTGENQAVNELIAKFEKAYPGITVEVTYQDTEARRQFFSTAAAGGKGPDVVFGPSDSLGPFAAAGLLAPLD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 127 SIVKSLGYKADDFpeglLDAGKYNGSQYAVPWSITPLGLYVNKDVLqaagvdPNSIPQDKDSYLAALEKLKAAGVqgeWv 206
Cdd:cd13522    80 EYVSKSGKYAPNT----IAAMKLNGKLYGVPVSVGAHLMYYNKKLV------PKNPPKTWQELIALAQGLKAKNV---W- 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 207 dGYVFTGT--FEFESLLWQYGGDLF--NKDVSKATFNSDAGVKALTWMTDLIKK-GYSPADVAQDGNINALIAGKTAFNW 281
Cdd:cd13522   146 -GLVYNQNepYFFAAWIGGFGGQVFkaNNGKNNPTLDTPGAVEALQFLVDLKSKyKIMPPETDYSIADALFKAGKAAMII 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 282 NGVWqTTNTAFDKLKWQAVAVPQIGDEKAVWSS----STHWMfMNNKGQDKnktAAAATFVKWMNDNSAD---WPKTGEL 354
Cdd:cd13522   225 NGPW-DLGDYRQALKINLGVAPLPTFSGTKHAApfvgGKGFG-INKESQNK---AAAVEFVKYLTSYQAQlvlFDDAGDI 299

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1085662500 355 PAKNSVRDDPkLVQTYPNLKPFLDELPYAHYEPIAPGITTVEATITVAVNEAITGKKDPKQ 415
Cdd:cd13522   300 PANLQAYESP-AVQNKPAQKASAEQAAYGVPMPNIPEMRAVWDAFRIAVNSVLAGKVTPEA 359
SBP_bac_8 pfam13416
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 65-373 5.71e-25

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


Pssm-ID: 433189 [Multi-domain]  Cd Length: 281  Bit Score: 103.64  E-value: 5.71e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500  65 KLIDKFNSEHkNIVVKDVPMEWADIARKMPLAVKAGKGPDVAV--GHGDDIATYAAQGLVLKADSIVKSlgykaDDFPEg 142
Cdd:pfam13416   1 ALAKAFEKKT-GVTVEVEPQASNDLQAKLLAAAAAGNAPDLDVvwIAADQLATLAEAGLLADLSDVDNL-----DDLPD- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 143 LLDAGKYNGSQYAVPWSI-TPLGLYVNKDVLQAAGVDPNSIpqdkDSYLAALEKLKAAGVQGEWVDGYVFTGtfefeslL 221
Cdd:pfam13416  74 ALDAAGYDGKLYGVPYAAsTPTVLYYNKDLLKKAGEDPKTW----DELLAAAAKLKGKTGLTDPATGWLLWA-------L 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 222 WQYGGDLFNKDVSKatfnsDAGVKALTWMTDLIKKGYSPAdvAQDGNINALIAGKTAFNWNGVWQTTNTAFDKLKWQAVa 301
Cdd:pfam13416 143 LADGVDLTDDGKGV-----EALDEALAYLKKLKDNGKVYN--TGADAVQLFANGEVAMTVNGTWAAAAAKKAGKKLGAV- 214

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1085662500 302 VPQIGdekAVWSSSTHWMFmnnkGQDKNKTAAAATFVKWMN--DNSADWPK-TGELPAKNSVRDDPKlVQTYPNL 373
Cdd:pfam13416 215 VPKDG---SFLGGKGLVVP----AGAKDPRLAALDFIKFLTspENQAALAEdTGYIPANKSAALSDE-VKADPAL 281
PBP2_CMBP cd13658
The periplasmic binding component of ABC transport systems specific for cyclo/maltodextrin; ...
 65-415 2.25e-20

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: 92.16  E-value: 2.25e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500  65 KLIDKFNSEHkNIVVKDVPMEWADIARKMPLAVKAGKGPDVAVGHGDDIATYAAQGLVLKadsiVKSLGYKADDFPEGLL 144
Cdd:cd13658    17 KIAKQYTKKT-GVKVKLVEVDQLDQLEKLSLDGPAGKGPDVMVAPHDRIGSAVLQGLLSP----IKLSKDKKKGFTDQAL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 145 DAGKYNGSQYAVPWSITPLGLYVNKDVLQAAgvdPNSIpQDKDSYLAAL--EKLKAAGVQGEWVDGYVFTGtfefesLLW 222
Cdd:cd13658    92 KALTYDGKLYGLPAAVETLALYYNKDLVKNA---PKTF-DELEALAKDLtkEKGKQYGFLADATNFYYSYG------LLA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 223 QYGGDLFNK-----DVSKATFNSDAGVKALTWMTDLIKKGYSPADVAQDGNINALIAGKTAFNWNGVWQTTNTAFDKLKW 297
Cdd:cd13658   162 GNGGYIFKKngsdlDINDIGLNSPGAVKAVKFLKKWYTEGYLPKGMTGDVIQGLFKEGKAAAVIDGPWAIQEYQEAGVNY 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 298 QAVAVPQIGDEKAVWSssthwmFMNNKG-----QDKNKtAAAATFVKWMN--DNSAD-WPKTGELPAKNSVRDDPkLVQT 369
Cdd:cd13658   242 GVAPLPTLPNGKPMAP------FLGVKGwylsaYSKHK-EWAQKFMEFLTskENLKKrYDETNEIPPRKDVRSDP-EIKN 313

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1085662500 370 YPNLKPFldELPYAHYEPIaPGITTVEATITVAVN---EAITGKKDPKQ 415
Cdd:cd13658   314 NPLTSAF--AKQASRAVPM-PNIPEMGAVWEPANNalfFILSGKKTPKQ 359
SBP_bac_1 pfam01547
Bacterial extracellular solute-binding protein; This family also includes the bacterial ...
 64-346 1.19e-16

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: 80.15  E-value: 1.19e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500  64 PKLIDKFNSEHKNIVVKDVPMEWADIARKMPLAVKAGKGP-DVAVGHGDDIATYAAQGLVLKADSIVKSlgykaddfpeg 142
Cdd:pfam01547  11 QALVKEFEKEHPGIKVEVESVGSGSLAQKLTTAIAAGDGPaDVFASDNDWIAELAKAGLLLPLDDYVAN----------- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 143 llDAGKYNGSQYAVPWSITPLGLYVNKDVLQAAGVDPnsiPQDKDSYLAALEKLKAAGVQGEWVDGYVFTGTFE--FESL 220
Cdd:pfam01547  80 --YLVLGVPKLYGVPLAAETLGLIYNKDLFKKAGLDP---PKTWDELLEAAKKLKEKGKSPGGAGGGDASGTLGyfTLAL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 221 LWQYGGDLFNKDVskATFNSDAGVKALTWMTDLI--------KKGYSPADVAQDGNINALIAGKTAFNWNGVWQTTNTAF 292
Cdd:pfam01547 155 LASLGGPLFDKDG--GGLDNPEAVDAITYYVDLYakvlllkkLKNPGVAGADGREALALFEQGKAAMGIVGPWAALAANK 232

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1085662500 293 DKLKwQAVAVPQIGDEKAV----------WSSSTHWMFMNNKGQDKnktAAAATFVKWMNDNSA 346
Cdd:pfam01547 233 VKLK-VAFAAPAPDPKGDVgyaplpagkgGKGGGYGLAIPKGSKNK---EAAKKFLDFLTSPEA 292
PBP2_MBP cd13656
The periplasmic binding component of ABC tansport system specific for maltose; possess the ...
 88-305 1.82e-10

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: 62.23  E-value: 1.82e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500  88 DIARKMPLAVKAGKGPDVAVGHGDDIATYAAQGLVlkadSIVKSLGYKADDFPEGLLDAGKYNGSQYAVPWSITPLGLYV 167
Cdd:cd13656    38 KLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLL----AEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIY 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 168 NKDVLqaagvdPNSiPQDKDSYLAALEKLKAAGVQGEWVDgyvFTGTFEFESLLWQYGGDLFNKDVSKaTFNSDAGV--- 244
Cdd:cd13656   114 NKDLL------PNP-PKTWEEIPALDKELKAKGKSALMFN---LQEPYFTWPLIAADGGYAFKYENGK-YDIKDVGVdna 182

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1085662500 245 ---KALTWMTDLIKKGYSPADVAQDGNINALIAGKTAFNWNGVWQTTNTAFDKLKWQAVAVPQI 305
Cdd:cd13656   183 gakAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKVNYGVTVLPTF 246
PBP2_AlgQ_like_1 cd13580
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 44-386 8.69e-08

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: 54.26  E-value: 8.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500  44 PKVTISFWNGWTGGAAP-----VLVPKLIDKFNSEHKNIVVKDVpmEWADiarKMPLAVKAGKGPDVAVGHGDD-IATYA 117
Cdd:cd13580     1 EPVTITIVANLGGNPKPdpddnPYTKYLEEKTNIDVKVKWVPDS--SYDE---KLNLALASGDLPDIVVVNDPQlSITLV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 118 AQGLVLKADSIVKSLG--YKADDFPEGLlDAGKYNGSQYAVPWS---ITPLGLYVNKDVLQAAGVDPnsiPQDKDSYLAA 192
Cdd:cd13580    76 KQGALWDLTDYLDKYYpnLKKIIEQEGW-DSASVDGKIYGIPRKrplIGRNGLWIRKDWLDKLGLEV---PKTLDELYEV 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 193 LEKLKAAGVQGEWV-DGYVFTGTFE-----FESLLWQYGG--DLFNKDVS---KATFNSDAGVKALTWMTDLIKKGYSPA 261
Cdd:cd13580   152 AKAFTEKDPDGNGKkDTYGLTDTKDligsgFTGLFGAFGAppNNWWKDEDgklVPGSIQPEMKEALKFLKKLYKEGLIDP 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 262 DVA--QDGNINALI-AGKTAF---NWNGVWQTTNTAFDKL---KWQAVAVPQIGD-EKAVWSSSTHW-MFMNNKGQDKNK 330
Cdd:cd13580   232 EFAvnDGTKANEKFiSGKAGIfvgNWWDPAWPQASLKKNDpdaEWVAVPIPSGPDgKYGVWAESGVNgFFVIPKKSKKPE 311

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1085662500 331 taAAATFVKWMNDNSADWPKTGELPAKNSVRDDPKLVQTYPNLKPFLDELPYAHYE 386
Cdd:cd13580   312 --AILKLLDFLSDPEVQKLLDYGIEGVHYTVKDGGPVNIIPPDKQEVGDATLDYFQ 365
malE PRK09474
maltose/maltodextrin ABC transporter substrate-binding protein MalE;
92-289 1.65e-06

maltose/maltodextrin ABC transporter substrate-binding protein MalE;


Pssm-ID: 236533 [Multi-domain]  Cd Length: 396  Bit Score: 50.01  E-value: 1.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500  92 KMPLAVKAGKGPDVAVGHGDDIATYAAQGLV--LKADSIVKSlgyKADDFPeglLDAGKYNGSQYAVPWSITPLGLYVNK 169
Cdd:PRK09474   72 KFPQVAATGDGPDIIFWAHDRFGGYAQSGLLaeVTPSKAFKD---KLVPFT---WDAVRYNGKLIGYPIAVEALSLIYNK 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 170 DVLQAAgvdpnsiPQDKDSYLAALEKLKAAGVQG-EW-VDGYVFTGtfefeSLLWQYGGDLFNK-----DVSKATFNSDA 242
Cdd:PRK09474  146 DLVPTP-------PKTWEEIPALDKELKAKGKSAiMWnLQEPYFTW-----PLIAADGGYAFKFenggyDVKDVGVNNAG 213

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1085662500 243 GVKALTWMTDLIKKGYSPADVAQDGNINALIAGKTAFNWNGVWQTTN 289
Cdd:PRK09474  214 AKAGLQFLVDLVKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSN 260
PBP2_oligosaccharide_1 cd13655
The periplasmic binding component of ABC tansport system specific for an unknown ...
 62-275 2.32e-05

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


Pssm-ID: 270373 [Multi-domain]  Cd Length: 363  Bit Score: 46.18  E-value: 2.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500  62 LVPKLIDKFNSEHK--NIVVKDVPMEWADIARKmpLAVKAGKGPDVAVGHGDDIATYAAQGLVL----KADSIVKSlgyk 135
Cdd:cd13655    13 WLKEMVDAFKEKHPewKITITIGVVGEADAKDE--VLKDPSAAADVFAFANDQLGELVDAGAIYpltgSAVDKIKN---- 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 136 adDFPEGLLDAGKYNGSQYAVPWSITPLGLYVNKDVLQAAGVdpnsipQDKDSYLAALEKLKAAgVQGEWVDGYVFTGTF 215
Cdd:cd13655    87 --TNSEATVDAVTYNGKLYGYPFTANTWFMYYDKSKLTEDDV------KSLDTMLAKAPDAKGK-VSFDLSNSWYLYAFF 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 216 efesllWQYGGDLF---NKDVSKATFNSDAGVKALTWMTDLI--KKGYSPAD-----VAQDGNINALIAG 275
Cdd:cd13655   158 ------FGAGCKLFgnnGGDTAGCDFNNEKGVAVTNYLVDLVanPKFVNDADgdaisGLKDGTLGAGVSG 221
PRK10974 PRK10974
sn-glycerol-3-phosphate ABC transporter substrate-binding protein UgpB;
5-257 5.71e-05

sn-glycerol-3-phosphate ABC transporter substrate-binding protein UgpB;


Pssm-ID: 182876 [Multi-domain]  Cd Length: 438  Bit Score: 45.18  E-value: 5.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500   5 FAARAIAVAVTAGLGLALTACGSsssggggdvssadytgpkVTISFWNGWTGgAAPVLVPKLIDKFNSEHKNivVKDVPM 84
Cdd:PRK10974    3 KSLRSTALGLALGLALSGNAQAV------------------TEIPFWHSMEG-ELGKEVDSLAQRFNASQPD--YKIVPV 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500  85 EWADIARKMPL---AVKAGKGPDVAVGHGDDIATYAAQGLVLKADSIVKSLGYKADDFPEGLLDAGKY----NGSQYAVP 157
Cdd:PRK10974   62 YKGNYEQSLAAgiaAFRSGNAPAILQVYEVGTATMMASKAIKPVYDVFKDAGIPFDESQFVPTVAGYYsdakTGHLLSQP 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500 158 W-SITPLgLYVNKDVLQAAGVDPNSIPQDKDSYLAALEKLKAAGVQGEWVDGYvfTGTFEFESLLWQYG------GDLFN 230
Cdd:PRK10974  142 FnSSTPV-LYYNKDAFKKAGLDPEQPPKTWQDLAAYAAKLRAAGMKCGYASGW--QGWIQLENFSAWHGlpfaskNNGFD 218

                         250       260
                  ....*....|....*....|....*..
gi 1085662500 231 KDVSKATFNSDAGVKALTWMTDLIKKG 257
Cdd:PRK10974  219 GTDAVLEFNKPEQVKHIALLEEMNKKG 245
PotD COG0687
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism];
1-199 5.08e-03

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


Pssm-ID: 440451 [Multi-domain]  Cd Length: 348  Bit Score: 38.74  E-value: 5.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500   1 MKKRFAARAIAVAVTAGLGLALTAcgssssggggdvsSADytGPKVTISFWngwtGGAAPvlvPKLIDKFNSEHKNIVVK 80
Cdd:COG0687     1 MSRRSLLGLAAAALAAALAGGAPA-------------AAA--EGTLNVYNW----GGYID---PDVLEPFEKETGIKVVY 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085662500  81 DVPMEWADIARKMplavKAGKGP-DVAVGHGDDIATYAAQGLVLKAD-SIVKSLGYKADDFPEGLLDAGKyngsQYAVPW 158
Cdd:COG0687    59 DTYDSNEEMLAKL----RAGGSGyDVVVPSDYFVARLIKAGLLQPLDkSKLPNLANLDPRFKDPPFDPGN----VYGVPY 130

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1085662500 159 SITPLGLYVNKDV---------------------------------LQAAGVDPNSIpqDKDSYLAALEKLKAA 199
Cdd:COG0687   131 TWGTTGIAYNTDKvkepptswadlwdpeykgkvallddprevlgaaLLYLGYDPNST--DPADLDAAFELLIEL 202
 
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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