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Conserved domains on  [gi|1016943462|ref|WP_063144949|]
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MULTISPECIES: phosphonate ABC transporter substrate-binding protein [Enterobacter]

Protein Classification

phosphonate ABC transporter substrate-binding protein( domain architecture ID 10194387)

phosphonate ABC transporter substrate-binding protein is a phosphonate binding protein that is part of the phosphonate uptake system; functions as the initial receptor of the ABC-type transport system

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PBP2_PnhD cd13575
Substrate binding domain of ABC-type phosphonate uptake system; contains the type 2 ...
28-284 1.43e-166

Substrate binding domain of ABC-type phosphonate uptake system; contains the type 2 periplasmic binding fold; This subfamily includes the Escherichia coli PhnD (EcPhnD) which exhibits high affinity for the environmentally abundant 2-aminoethylphosphonate (2-AEP), a precursor in the biosynthesis of phosphonolipids, phosphonoproteins, and phosphonoglycans. The Escherichia coli phn operon encodes 14 genes involved in binding, uptake and metabolism of phosphonate, and is activated under phophophate-limiting conditions. PhnD belongs 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. The PBP2 have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. PhnD is the periplasmic binding component of an ABC-type phosphonate uptake system (PhnCDE) that recognizes and binds phosphonate.


:

Pssm-ID: 270293 [Multi-domain]  Cd Length: 259  Bit Score: 464.25  E-value: 1.43e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016943462  28 EQEKALNFGIISTESQQNLKPQWEPFLKDMETKLGIKVNAFFAPDYAGIIQGMRFNKVDIAWYGNLSAMEAVDRANGQVF 107
Cdd:cd13575     1 EDEKALNFGIISTESQQNLRAQWEPFLAAMEKKLGVKVNAFFAPDYAGIIEGMRFNKVQIAWYGNKSAMEAVDRANGEVF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016943462 108 AQTVAADGSPGYWSVLIVNKDSPINNLNDMLAKRKELTFGNGDPNSTSGYLVPGYYVFAKNN-ASASDFKRTVNASHETN 186
Cdd:cd13575    81 AQTVAADGSPGYYSHLIVNKDSPINSLNDVLAKAKDLTFGNGDPNSTSGFLVPGYYVFAKNGiDPKKFFKRTVNANHETN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016943462 187 ALAVANKQVDVATNNTENLDKLKTSAPDKLKEIKVIWKSPLIPGDPIVWRKNLSESTKDKVYDFFMTYGKTPEEKAVL-A 265
Cdd:cd13575   161 ALAVANKQVDVATNNTENLDRLKERAPEKLKQLRIIWTSPLIPGDPLVWRKDLPEAVKKKIADFFFGYGQTAEEKSVLkE 240
                         250
                  ....*....|....*....
gi 1016943462 266 RLGWAPFRPSSDLQLVPIR 284
Cdd:cd13575   241 RLDWSPFKPSSDGQLVPIR 259
 
Name Accession Description Interval E-value
PBP2_PnhD cd13575
Substrate binding domain of ABC-type phosphonate uptake system; contains the type 2 ...
28-284 1.43e-166

Substrate binding domain of ABC-type phosphonate uptake system; contains the type 2 periplasmic binding fold; This subfamily includes the Escherichia coli PhnD (EcPhnD) which exhibits high affinity for the environmentally abundant 2-aminoethylphosphonate (2-AEP), a precursor in the biosynthesis of phosphonolipids, phosphonoproteins, and phosphonoglycans. The Escherichia coli phn operon encodes 14 genes involved in binding, uptake and metabolism of phosphonate, and is activated under phophophate-limiting conditions. PhnD belongs 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. The PBP2 have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. PhnD is the periplasmic binding component of an ABC-type phosphonate uptake system (PhnCDE) that recognizes and binds phosphonate.


Pssm-ID: 270293 [Multi-domain]  Cd Length: 259  Bit Score: 464.25  E-value: 1.43e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016943462  28 EQEKALNFGIISTESQQNLKPQWEPFLKDMETKLGIKVNAFFAPDYAGIIQGMRFNKVDIAWYGNLSAMEAVDRANGQVF 107
Cdd:cd13575     1 EDEKALNFGIISTESQQNLRAQWEPFLAAMEKKLGVKVNAFFAPDYAGIIEGMRFNKVQIAWYGNKSAMEAVDRANGEVF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016943462 108 AQTVAADGSPGYWSVLIVNKDSPINNLNDMLAKRKELTFGNGDPNSTSGYLVPGYYVFAKNN-ASASDFKRTVNASHETN 186
Cdd:cd13575    81 AQTVAADGSPGYYSHLIVNKDSPINSLNDVLAKAKDLTFGNGDPNSTSGFLVPGYYVFAKNGiDPKKFFKRTVNANHETN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016943462 187 ALAVANKQVDVATNNTENLDKLKTSAPDKLKEIKVIWKSPLIPGDPIVWRKNLSESTKDKVYDFFMTYGKTPEEKAVL-A 265
Cdd:cd13575   161 ALAVANKQVDVATNNTENLDRLKERAPEKLKQLRIIWTSPLIPGDPLVWRKDLPEAVKKKIADFFFGYGQTAEEKSVLkE 240
                         250
                  ....*....|....*....
gi 1016943462 266 RLGWAPFRPSSDLQLVPIR 284
Cdd:cd13575   241 RLDWSPFKPSSDGQLVPIR 259
PhnD TIGR03431
phosphonate ABC transporter, periplasmic phosphonate binding protein; This model is a subset ...
1-291 8.65e-138

phosphonate ABC transporter, periplasmic phosphonate binding protein; This model is a subset of the broader subfamily of phosphate/phosphonate binding protein ABC transporter components, TIGR01098. In this model all members of the seed have support from genomic context for association with pathways for the metabolims of phosphonates, particularly the C-P lyase system, GenProp0232. This model includes the characterized phnD gene from E. coli. Note that this model does not identify all phnD-subfamily genes with evident phosphonate context, but all sequences above the trusted context may be inferred to bind phosphonate compounds even in the absence of such context. Furthermore, there is ample evidence to suggest that many other members of the TIGR01098 subfamily have a different primary function.


Pssm-ID: 132472 [Multi-domain]  Cd Length: 288  Bit Score: 392.49  E-value: 8.65e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016943462   1 MSYKAVAALAFTSMFSLStllsPAYAEEQEKALNFGIISTESQQNLKPQWEPFLKDMETKLGIKVNAFFAPDYAGIIQGM 80
Cdd:TIGR03431   1 MLRRLILSLVAAFMLISS----NAQAEDWPKELNFGIIPTENASDLKQRWEPLADYLSKKLGVKVKLFFATDYAGVIEGM 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016943462  81 RFNKVDIAWYGNLSAMEAVDRANGQVFAQTVAADGSPGYWSVLIVNKDSPINNLNDMlakrKELTFGNGDPNSTSGYLVP 160
Cdd:TIGR03431  77 RFGKVDIAWYGPSSYAEAYQKANAEAFAIEVNADGSTGYYSVLIVKKDSPIKSLEDL----KGKTFGFVDPNSTSGFLVP 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016943462 161 GYYVFAKNNASASD-FKRTVNA-SHETNALAVANKQVDVATNNTENLDKLKT-SAPDKLKEIKVIWKSPLIPGDPIVWRK 237
Cdd:TIGR03431 153 SYYLFKKNGIKPKEyFKKVTFSgSHEAAILAVANGTVDAATTNDENLDRMIRkGQPDAMEDLRIIWKSPLIPNGPIVYRK 232
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1016943462 238 NLSESTKDKVYDFFMTYGKTPEEKAVLARLGW-APFRPSSDLQLVPIRQLALFKE 291
Cdd:TIGR03431 233 DLPADLKAKIRKAFLNYHKTDKACFEKIAGGDlKGFVAASDKDYDPIRDLKKAKI 287
Phosphonate-bd pfam12974
ABC transporter, phosphonate, periplasmic substrate-binding protein; This is a family of ...
35-277 3.36e-92

ABC transporter, phosphonate, periplasmic substrate-binding protein; This is a family of periplasmic proteins which are part of the transport system for alkylphosphonate uptake.


Pssm-ID: 432911 [Multi-domain]  Cd Length: 243  Bit Score: 274.91  E-value: 3.36e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016943462  35 FGIISTESQQNLKPQWEPFLKDMETKLGIKVNAFFAPDYAGIIQGMRFNKVDIAWYGNLSAMEAVDRANGQVFAQTVAAD 114
Cdd:pfam12974   1 FGVLPDESPDELKARYQPLADYLSEELGVPVELVVATDYAAVVEALRAGQVDIAYFGPLAYVQAVDRAGAEPLATPVEPD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016943462 115 GSPGYWSVLIVNKDSPINNLNDMlakrKELTFGNGDPNSTSGYLVPGYYVFAKNN-ASASDFKRTVNASHETNALAVANK 193
Cdd:pfam12974  81 GSAGYRSVIIVRKDSPIQSLEDL----KGKTVAFGDPSSTSGYLVPLALLFAEAGlDPEDDFKPVFSGSHDAVALAVLNG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016943462 194 QVDVATNNTENLDKLKTSAPDKLKEIKVIWKSPLIPGDPIVWRKNLSESTKDKVYDFFMTYGKTPEEKAVLARLGWAPFR 273
Cdd:pfam12974 157 DADAGAVNSEVLERLVAEGPIDRDQLRVIAESPPIPNDPLVARPDLPPELKEKIRDALLALDETPEGRKVLEALGIDGFV 236

                  ....
gi 1016943462 274 PSSD 277
Cdd:pfam12974 237 PADD 240
PhnD COG3221
ABC-type phosphate/phosphonate transport system, periplasmic component [Inorganic ion ...
37-287 1.66e-83

ABC-type phosphate/phosphonate transport system, periplasmic component [Inorganic ion transport and metabolism];


Pssm-ID: 442454 [Multi-domain]  Cd Length: 250  Bit Score: 252.92  E-value: 1.66e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016943462  37 IISTESQQNLKPQWEPFLKDMETKLGIKVNAFFAPDYAGIIQGMRFNKVDIAWYGNLSAMEAVDRANGQVFAQTVaADGS 116
Cdd:COG3221     1 VLPSESPADLLARWQPLADYLEEELGVPVELVPATDYAALIEALRAGQVDLAFLGPLPYVLARDRAGAEPLATPV-RDGS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016943462 117 PGYWSVLIVNKDSPINNLNDMlakrKELTFGNGDPNSTSGYLVPGYYVFAKNNASASDFKRTVNA-SHETNALAVANKQV 195
Cdd:COG3221    80 PGYRSVIIVRADSPIKSLEDL----KGKRFAFGDPDSTSGYLVPRALLAEAGLDPERDFSEVVFSgSHDAVILAVANGQA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016943462 196 DVATNNTENLDKLKTSAPDKlKEIKVIWKSPLIPGDPIVWRKNLSESTKDKVYDFFMTYGKTPEEKAVLARLGWAPFRPS 275
Cdd:COG3221   156 DAGAVDSGVLERLVEEGPDA-DQLRVIWESPPIPNDPFVARPDLPPELREKIREALLSLDEDPEGKAILEALGLEGFVPA 234
                         250
                  ....*....|..
gi 1016943462 276 SDLQLVPIRQLA 287
Cdd:COG3221   235 DDADYDPIRELL 246
 
Name Accession Description Interval E-value
PBP2_PnhD cd13575
Substrate binding domain of ABC-type phosphonate uptake system; contains the type 2 ...
28-284 1.43e-166

Substrate binding domain of ABC-type phosphonate uptake system; contains the type 2 periplasmic binding fold; This subfamily includes the Escherichia coli PhnD (EcPhnD) which exhibits high affinity for the environmentally abundant 2-aminoethylphosphonate (2-AEP), a precursor in the biosynthesis of phosphonolipids, phosphonoproteins, and phosphonoglycans. The Escherichia coli phn operon encodes 14 genes involved in binding, uptake and metabolism of phosphonate, and is activated under phophophate-limiting conditions. PhnD belongs 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. The PBP2 have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. PhnD is the periplasmic binding component of an ABC-type phosphonate uptake system (PhnCDE) that recognizes and binds phosphonate.


Pssm-ID: 270293 [Multi-domain]  Cd Length: 259  Bit Score: 464.25  E-value: 1.43e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016943462  28 EQEKALNFGIISTESQQNLKPQWEPFLKDMETKLGIKVNAFFAPDYAGIIQGMRFNKVDIAWYGNLSAMEAVDRANGQVF 107
Cdd:cd13575     1 EDEKALNFGIISTESQQNLRAQWEPFLAAMEKKLGVKVNAFFAPDYAGIIEGMRFNKVQIAWYGNKSAMEAVDRANGEVF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016943462 108 AQTVAADGSPGYWSVLIVNKDSPINNLNDMLAKRKELTFGNGDPNSTSGYLVPGYYVFAKNN-ASASDFKRTVNASHETN 186
Cdd:cd13575    81 AQTVAADGSPGYYSHLIVNKDSPINSLNDVLAKAKDLTFGNGDPNSTSGFLVPGYYVFAKNGiDPKKFFKRTVNANHETN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016943462 187 ALAVANKQVDVATNNTENLDKLKTSAPDKLKEIKVIWKSPLIPGDPIVWRKNLSESTKDKVYDFFMTYGKTPEEKAVL-A 265
Cdd:cd13575   161 ALAVANKQVDVATNNTENLDRLKERAPEKLKQLRIIWTSPLIPGDPLVWRKDLPEAVKKKIADFFFGYGQTAEEKSVLkE 240
                         250
                  ....*....|....*....
gi 1016943462 266 RLGWAPFRPSSDLQLVPIR 284
Cdd:cd13575   241 RLDWSPFKPSSDGQLVPIR 259
PhnD TIGR03431
phosphonate ABC transporter, periplasmic phosphonate binding protein; This model is a subset ...
1-291 8.65e-138

phosphonate ABC transporter, periplasmic phosphonate binding protein; This model is a subset of the broader subfamily of phosphate/phosphonate binding protein ABC transporter components, TIGR01098. In this model all members of the seed have support from genomic context for association with pathways for the metabolims of phosphonates, particularly the C-P lyase system, GenProp0232. This model includes the characterized phnD gene from E. coli. Note that this model does not identify all phnD-subfamily genes with evident phosphonate context, but all sequences above the trusted context may be inferred to bind phosphonate compounds even in the absence of such context. Furthermore, there is ample evidence to suggest that many other members of the TIGR01098 subfamily have a different primary function.


Pssm-ID: 132472 [Multi-domain]  Cd Length: 288  Bit Score: 392.49  E-value: 8.65e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016943462   1 MSYKAVAALAFTSMFSLStllsPAYAEEQEKALNFGIISTESQQNLKPQWEPFLKDMETKLGIKVNAFFAPDYAGIIQGM 80
Cdd:TIGR03431   1 MLRRLILSLVAAFMLISS----NAQAEDWPKELNFGIIPTENASDLKQRWEPLADYLSKKLGVKVKLFFATDYAGVIEGM 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016943462  81 RFNKVDIAWYGNLSAMEAVDRANGQVFAQTVAADGSPGYWSVLIVNKDSPINNLNDMlakrKELTFGNGDPNSTSGYLVP 160
Cdd:TIGR03431  77 RFGKVDIAWYGPSSYAEAYQKANAEAFAIEVNADGSTGYYSVLIVKKDSPIKSLEDL----KGKTFGFVDPNSTSGFLVP 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016943462 161 GYYVFAKNNASASD-FKRTVNA-SHETNALAVANKQVDVATNNTENLDKLKT-SAPDKLKEIKVIWKSPLIPGDPIVWRK 237
Cdd:TIGR03431 153 SYYLFKKNGIKPKEyFKKVTFSgSHEAAILAVANGTVDAATTNDENLDRMIRkGQPDAMEDLRIIWKSPLIPNGPIVYRK 232
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1016943462 238 NLSESTKDKVYDFFMTYGKTPEEKAVLARLGW-APFRPSSDLQLVPIRQLALFKE 291
Cdd:TIGR03431 233 DLPADLKAKIRKAFLNYHKTDKACFEKIAGGDlKGFVAASDKDYDPIRDLKKAKI 287
3A0109s03R TIGR01098
phosphate/phosphite/phosphonate ABC transporter, periplasmic binding protein; Phosphonates are ...
4-254 5.37e-107

phosphate/phosphite/phosphonate ABC transporter, periplasmic binding protein; Phosphonates are a varied class of phosphorus-containing organic compound in which a direct C-P bond is found, rather than a C-O-P linkage of the phosphorus through an oxygen atom. They may be toxic but also may be used as sources of phosphorus and energy by various bacteria. Phosphonate utilization systems typically are encoded in 14 or more genes, including a three gene ABC transporter. This family includes the periplasmic binding protein component of ABC transporters for phosphonates as well as other, related binding components for closely related substances such as phosphate and phosphite. A number of members of this family are found in genomic contexts with components of selenium metabolic processes suggestive of a role in selenate or other selenium-compound transport. A subset of this model in which nearly all members exhibit genomic context with elements of phosphonate metabolism, particularly the C-P lyase system (GenProp0232) has been built (TIGR03431) as an equivalog. Nevertheless, there are members of this subfamily (TIGR01098) which show up sporadically on a phylogenetic tree that also show phosphonate context and are most likely competent to transport phosphonates. [Transport and binding proteins, Anions]


Pssm-ID: 273442 [Multi-domain]  Cd Length: 254  Bit Score: 313.13  E-value: 5.37e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016943462   4 KAVAALAFTSMFSLSTLLSPAYAE--EQEKALNFGIISTESQQNLKPQWEPFLKDMETKLGIKVNAFFAPDYAGIIQGMR 81
Cdd:TIGR01098   3 RLLALLAALLGASLAAACSKKAAEaaAVPKELNFGILPGENASNLTRRWEPLADYLEKKLGIKVQLFVATDYSAVIEAMR 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016943462  82 FNKVDIAWYGNLSAMEAVDRANGQVFAQT-VAADGSPGYWSVLIVNKDSPINNLNDmlakRKELTFGNGDPNSTSGYLVP 160
Cdd:TIGR01098  83 FGRVDIAWFGPSSYVLAHYRANAEVFALTaVSTDGSPGYYSVIIVKADSPIKSLKD----LKGKTFAFGDPASTSGYLVP 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016943462 161 GYYVFAKNNASAS-DFKRTVNA-SHETNALAVANKQVDVATNNTENLDKLKTSAPDKLKEIKVIWKSPLIPGDPIVWRKN 238
Cdd:TIGR01098 159 RYQLKKEGGLDADgFFSEVVFSgSHDASALAVANGKVDAATNNSSAIGRLKKRGPSDMKKVRVIWKSPLIPNDPIAVRKD 238
                         250
                  ....*....|....*.
gi 1016943462 239 LSESTKDKVYDFFMTY 254
Cdd:TIGR01098 239 LPPELKEKIRDAFLTL 254
PBP2_PhnD_like cd01071
Substrate binding domain of phosphonate uptake system-like, a member of the type 2 ...
28-284 2.68e-93

Substrate binding domain of phosphonate uptake system-like, a member of the type 2 periplasmic-binding fold superfamily; This family includes alkylphosphonate binding domain PhnD. These domains are found in PhnD-like proteins that are predicted to function as initial receptors in hypophosphite, phosphonate, or phosphate ABC transport in archaea and eubacteria. PhnD is the periplasmic binding component of an ABC-type phosphonate uptake system (PhnCDE) that recognizes and binds phosphonate. PhnD belongs 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. The PBP2 have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270232 [Multi-domain]  Cd Length: 253  Bit Score: 277.99  E-value: 2.68e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016943462  28 EQEKALNFGIISTESQQNLKPQWEPFLKDMETKLGIKVNAFFAPDYAGIIQGMRFNKVDIAWYGNLSAMEAVDRANGQVF 107
Cdd:cd01071     1 AAPKELRFGLVPAEDADELKKEFEPLADYLEEELGVPVELVVATSYAAVVEAMRNGKVDIAWLGPASYVLAHDRAGAEAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016943462 108 AqTVAADGSPGYWSVLIVNKDSPINNLNDMLAKRkeltFGNGDPNSTSGYLVPGYYVFAKNNASASDFKRTV-NASHETN 186
Cdd:cd01071    81 A-TEVRDGSPGYYSVIIVRKDSPIKSLEDLKGKT----VAFVDPSSTSGYLFPRAMLKDAGIDPPDFFFEVVfAGSHDSA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016943462 187 ALAVANKQVDVATNNTENLDKLKTSAPDKLKEIKVIWKSPLIPGDPIVWRKNLSESTKDKVYDFFMTYGKTPEEKAVLAR 266
Cdd:cd01071   156 LLAVANGDVDAAATYDSTLERAAAAGPIDPDDLRVIWRSPPIPNDPLVVRKDLPPALKAKIRDALLDLDETDEGQKLLAG 235
                         250
                  ....*....|....*...
gi 1016943462 267 LGWAPFRPSSDLQLVPIR 284
Cdd:cd01071   236 LGLTGFVPATDDDYDPIR 253
Phosphonate-bd pfam12974
ABC transporter, phosphonate, periplasmic substrate-binding protein; This is a family of ...
35-277 3.36e-92

ABC transporter, phosphonate, periplasmic substrate-binding protein; This is a family of periplasmic proteins which are part of the transport system for alkylphosphonate uptake.


Pssm-ID: 432911 [Multi-domain]  Cd Length: 243  Bit Score: 274.91  E-value: 3.36e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016943462  35 FGIISTESQQNLKPQWEPFLKDMETKLGIKVNAFFAPDYAGIIQGMRFNKVDIAWYGNLSAMEAVDRANGQVFAQTVAAD 114
Cdd:pfam12974   1 FGVLPDESPDELKARYQPLADYLSEELGVPVELVVATDYAAVVEALRAGQVDIAYFGPLAYVQAVDRAGAEPLATPVEPD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016943462 115 GSPGYWSVLIVNKDSPINNLNDMlakrKELTFGNGDPNSTSGYLVPGYYVFAKNN-ASASDFKRTVNASHETNALAVANK 193
Cdd:pfam12974  81 GSAGYRSVIIVRKDSPIQSLEDL----KGKTVAFGDPSSTSGYLVPLALLFAEAGlDPEDDFKPVFSGSHDAVALAVLNG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016943462 194 QVDVATNNTENLDKLKTSAPDKLKEIKVIWKSPLIPGDPIVWRKNLSESTKDKVYDFFMTYGKTPEEKAVLARLGWAPFR 273
Cdd:pfam12974 157 DADAGAVNSEVLERLVAEGPIDRDQLRVIAESPPIPNDPLVARPDLPPELKEKIRDALLALDETPEGRKVLEALGIDGFV 236

                  ....
gi 1016943462 274 PSSD 277
Cdd:pfam12974 237 PADD 240
PhnD COG3221
ABC-type phosphate/phosphonate transport system, periplasmic component [Inorganic ion ...
37-287 1.66e-83

ABC-type phosphate/phosphonate transport system, periplasmic component [Inorganic ion transport and metabolism];


Pssm-ID: 442454 [Multi-domain]  Cd Length: 250  Bit Score: 252.92  E-value: 1.66e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016943462  37 IISTESQQNLKPQWEPFLKDMETKLGIKVNAFFAPDYAGIIQGMRFNKVDIAWYGNLSAMEAVDRANGQVFAQTVaADGS 116
Cdd:COG3221     1 VLPSESPADLLARWQPLADYLEEELGVPVELVPATDYAALIEALRAGQVDLAFLGPLPYVLARDRAGAEPLATPV-RDGS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016943462 117 PGYWSVLIVNKDSPINNLNDMlakrKELTFGNGDPNSTSGYLVPGYYVFAKNNASASDFKRTVNA-SHETNALAVANKQV 195
Cdd:COG3221    80 PGYRSVIIVRADSPIKSLEDL----KGKRFAFGDPDSTSGYLVPRALLAEAGLDPERDFSEVVFSgSHDAVILAVANGQA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016943462 196 DVATNNTENLDKLKTSAPDKlKEIKVIWKSPLIPGDPIVWRKNLSESTKDKVYDFFMTYGKTPEEKAVLARLGWAPFRPS 275
Cdd:COG3221   156 DAGAVDSGVLERLVEEGPDA-DQLRVIWESPPIPNDPFVARPDLPPELREKIREALLSLDEDPEGKAILEALGLEGFVPA 234
                         250
                  ....*....|..
gi 1016943462 276 SDLQLVPIRQLA 287
Cdd:COG3221   235 DDADYDPIRELL 246
PBP2_PnhD_2 cd13572
Substrate binding domain of uncharacterized ABC-type phosphonate-like transporter; contains ...
29-284 1.19e-46

Substrate binding domain of uncharacterized ABC-type phosphonate-like transporter; contains the type 2 periplasmic binding fold; This subfamily includes putative periplasmic binding component of an ABC transport system similar to alkylphosphonate binding domain PnhD. These domains are found in PnhD-like proteins that are predicted to function as initial receptors in hypophosphite, phosphonate, or phosphate ABC transport in archaea and eubacteria. They 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: 270290 [Multi-domain]  Cd Length: 249  Bit Score: 158.25  E-value: 1.19e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016943462  29 QEKALNFGIISTESQQNLKPQWEPFLKDMETKLGIKVNAFFAPDYAGIIQGMRFNKVDIAWYGNLSAMEAVDRANGQVFA 108
Cdd:cd13572     2 APETLKVGAIPDENPTTLIRLNDPLADYLEKELGVEVELVVVTDYAAMVEAMRNGQLDLAYFGGLTYVQARLKPGAEPIA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016943462 109 QtVAADGSPGYWSVLIVNKDSPINNLNDmlAKRKELTFgnGDPNSTSGYLVPGYYVFAKNNASASDFKR-TVNASHETNA 187
Cdd:cd13572    82 Q-LLRDGDPTFHSVFIANTDSGINSLAD--LKGKRFAF--GDPASTSGHLMPRYFLLEAGVLPDGDFYRvGFSGAHDATA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016943462 188 LAVANKQVDVATNNTENLDKLKTSAPDKLKEIKVIWKSPLIPGDPIVWRKNLSESTKDKVYDFFMTYgktpEEKAVLARL 267
Cdd:cd13572   157 LAVANGKVDAGALNEAIWESLVEEGKIDGEKVKVIWRTPPYPDYPWTVRPNLGPELKEKVRNAFLSL----DDPEVLDIF 232
                         250
                  ....*....|....*..
gi 1016943462 268 GWAPFRPSSDLQLVPIR 284
Cdd:cd13572   233 GASGFIPASDDDYDPIE 249
PBP2_PnhD_1 cd13571
Substrate binding domain of uncharacterized ABC-type phosphonate-like transporter; contains ...
28-284 1.99e-46

Substrate binding domain of uncharacterized ABC-type phosphonate-like transporter; contains the type 2 periplasmic binding fold; This subfamily includes putative periplasmic binding components of an ABC transport system similar to alkylphosphonate binding domain PnhD. These domains are found in PnhD-like proteins that are predicted to function as initial receptors in hypophosphite, phosphonate, or phosphate ABC transport in archaea and eubacteria. They 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: 270289 [Multi-domain]  Cd Length: 253  Bit Score: 157.81  E-value: 1.99e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016943462  28 EQEKALNFGIISTESQQNLKPQWEPFLKDMETKLGIKVNAFFAPDYAGIIQGMRFNKVDIAWYGNLSAMEAVDRANGQVF 107
Cdd:cd13571     1 ASSPPLRIGLASVLSPRETLALYDPLAEYLERKLGRPVEFVQRRTYAEINELLKNGKVDLAFVCSGAYVQARDKAGLELL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016943462 108 AQTVAaDGSPGYWSVLIVNKDSPINNLNDMLAKRkeltFGNGDPNSTSGYLVPGYYVFAKNNASASDFKRTVNA-SHETN 186
Cdd:cd13571    81 AVPEI-NGQPTYRSYIIVPADSPAKSLEDLKGKR----FAFTDPLSNSGFLVPMYLLAELGLDPERFFSRVFFTgSHDKS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016943462 187 ALAVANKQVDVATNNTENLDKLKTSAPDKLKEIKVIWKSPLIPGDPIVWRKNLSESTKDKVYDFFMTYGKTPEEKAVLAR 266
Cdd:cd13571   156 IQAVANGLVDGAAVDSLVYEYAVEKGPELAANVRIIWRSEPIGNPPVVARPGLDPELKAALQEAFLSMHEDPEGRAALEG 235
                         250
                  ....*....|....*...
gi 1016943462 267 LGWAPFRPSSDLQLVPIR 284
Cdd:cd13571   236 LGIDRFVPADDSLYDPIR 253
PBP2_PnhD_4 cd13574
Substrate binding domain of uncharacterized ABC-type phosphonate-like transporter; contains ...
28-284 8.66e-28

Substrate binding domain of uncharacterized ABC-type phosphonate-like transporter; contains the type 2 periplasmic binding fold; This subfamily includes putative periplasmic binding component of an ABC transport system similar to alkylphosphonate binding domain PnhD. These domains are found in PnhD-like proteins that are predicted to function as initial receptors in hypophosphite, phosphonate, or phosphate ABC transport in archaea and eubacteria. They 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: 270292 [Multi-domain]  Cd Length: 250  Bit Score: 108.94  E-value: 8.66e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016943462  28 EQEKALNFGIISTESQQNLKPQWEPFLKDMETKLGIKVNAFFAPDYAGIIQGMRFNKVDIAWYGNLSAMEAVDRANG-QV 106
Cdd:cd13574     1 AAEPPLRFGVHPYLSPTELVKRFQPLLDYLEEELGRPVEIKVSKDYQEHVDRLGSGKIDIAYLGPAPYVQAKDRRYGiKP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016943462 107 FAQTVAADGSPGYWSVLIVNKDSPINNLNDMLAKRkeltFGNGDPNSTSGYLVPGYYVfAKNNASASDFKRTVN-ASHET 185
Cdd:cd13574    81 LLALLETDGKPTYNGVIVVRADSPIKSLADLAGKS----FAFGDPLSTMGHLVPRAML-RQAGITSLDLAGYDYlGRHDN 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016943462 186 NALAVANKQVDVATNNTENLDKLKTSAPdklkeiKVIWKSPLIPGDPIVWRKNLSESTKDKVYDFFMTYGKTPEEKAVLA 265
Cdd:cd13574   156 VALAVLAGEFDAGALKEEVYRKYKGRGL------RVLATSPPLPGHALVARATLPEELVKALRRALLELDSTGAGLAILT 229
                         250       260
                  ....*....|....*....|....
gi 1016943462 266 -----RLGwapFRPSSDLQLVPIR 284
Cdd:cd13574   230 wieelRHG---FVPVTDEDYDLLR 250
ABC_peri_selen TIGR04553
putative selenate ABC transporter periplasmic binding protein; Members of this family ABC ...
33-287 1.24e-27

putative selenate ABC transporter periplasmic binding protein; Members of this family ABC transporter periplasmic binding proteins and represent one clade within a larger family that includes phosphate, phosphite, and phosphonate transporters. All members of the seed alignment occur near a gene for SelD, the selenium-activating protein needed to make selenocysteine or selenouridine. Context therefore suggests members should be able to transport selenate, although transporting other substrates as well (e.g. phosphonates) is possible. This model has no overlap with TIGR03431, whose members are found regularly with phosphonate catabolism operons.


Pssm-ID: 275346 [Multi-domain]  Cd Length: 266  Bit Score: 108.70  E-value: 1.24e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016943462  33 LNFGIISTESQQNLKPQWEPFLKDMETKLGIKVNafFAP--DYAGIIQGMRFNKVDIAWYGNLSAMEAVDRANGQV-FAQ 109
Cdd:TIGR04553   2 FVFTAIPDEDPTELQRRFAPLADYLEEELGVEVR--FVPvtDYAAAVEAFRNNQVQLAWFGGLTGVQARVRVPGSVpLAQ 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016943462 110 TVAadgSPGYWSVLIVNkDSPINNLNDMLAKRKELTFGNGDPNSTSGYLVPGYYVFAKNNASASDFKRT-VNASHETNAL 188
Cdd:TIGR04553  80 RVE---DEAFRSVFIAH-ESTILELADGLPELKGKTFTFGSKSSTSGRLMPRSFLLEAGEAPDDDFKRVgYSGAHDATLA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016943462 189 AVANKQVDVATNNTENLDKLKTSAPDKLKEIKVIWKSP-------LIPGDpivWRKNLSESTKDKVYDFFMTY-GKTPEE 260
Cdd:TIGR04553 156 LVEAGTYDAGALNISVWEKEVADGKVDTDKVRVIWTTPgypdynwTVRGD---VDERFGEGFTDKVTQALLDLdPSTAED 232
                         250       260
                  ....*....|....*....|....*..
gi 1016943462 261 KAVLARLGWAPFRPSSDLQLVPIRQLA 287
Cdd:TIGR04553 233 KEILELFRASRFIPTSNDNYAGIEAAA 259
PBP2_PnhD_3 cd13573
Substrate binding domain of uncharacterized ABC-type phosphonate-like transporter; contains ...
31-262 2.32e-22

Substrate binding domain of uncharacterized ABC-type phosphonate-like transporter; contains the type 2 periplasmic binding fold; This subfamily includes putative periplasmic binding component of an ABC transport system similar to alkylphosphonate binding domain PnhD. These domains are found in PnhD-like proteins that are predicted to function as initial receptors in hypophosphite, phosphonate, or phosphate ABC transport in archaea and eubacteria. They 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: 270291 [Multi-domain]  Cd Length: 253  Bit Score: 94.08  E-value: 2.32e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016943462  31 KALNFGIISTESQQNLKPQWEPFLKDMETKLGIKVNAFFAPDYAGIIQGMRFNKVDIAWYGNLSAMEAVDRANGQVFAQT 110
Cdd:cd13573     4 DTLVFAYTPVEDPAVYQEIWAPFIAHISKVTGKDVQFYPVQSNAAQTEAMRSGRLHIAGFSTGPTPFAVNLAGAVPFAVK 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016943462 111 VAADGSPGYWSVLIVNKDSPINNLNDMLAKRKELTfgngDPNSTSGYLVPGYYVFAKNNASAS-DFKRTVNASHETNALA 189
Cdd:cd13573    84 GYEDGSFGYELEVITRIDSGIQKVKDLKGRKVAHT----SPTSNSGHLAPRALFPAQGGIVPDkDYEVTFSGKHDQSILG 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1016943462 190 VANKQVDVATNNTENLDKLKTSAPDKLKEIKVIWKSPLIPGDPIVWRKNLSESTKDKVYDFFMTYGKTPEEKA 262
Cdd:cd13573   160 VFNGDYDAAPVASDVLERMAERGQVKEEQFRVIYKSFAFPTGPFGYAHNLKPELREKIKEAFFTYDFAGTKLA 232
Periplasmic_Binding_Protein_Type_2 cd00648
Type 2 periplasmic binding fold superfamily; This evolutionary model and hierarchy represent ...
33-237 5.77e-14

Type 2 periplasmic binding fold superfamily; This evolutionary model and hierarchy represent the ligand-binding domains found in solute binding proteins that serve as initial receptors in the transport, signal transduction and channel gating. The PBP2 proteins share the same architecture as periplasmic binding proteins type 1 (PBP1), but have a different topology. They are typically 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 origin of PBP module can be traced across the distant phyla, including eukaryotes, archebacteria, and prokaryotes. The majority of PBP2 proteins are involved in the uptake of a variety of soluble substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. 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. Besides transport proteins, the family includes ionotropic glutamate receptors and unorthodox sensor proteins involved in signal transduction. The substrate binding domain of the LysR transcriptional regulators and the oligopeptide-like transport systems also contain the type 2 periplasmic binding fold and thus they are significantly homologous to that of the PBP2; however, these two families are grouped into a separate hierarchy of the PBP2 superfamily due to the large number of protein sequences.


Pssm-ID: 270214 [Multi-domain]  Cd Length: 196  Bit Score: 69.52  E-value: 5.77e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016943462  33 LNFGIISTESQQnlkPQWEPFLKDMETKLGIKVNAFFAPDYAGIIQGMRFNKVDIAWYGNLSAMEAVDRANgqVFAQTVA 112
Cdd:cd00648     2 LTVASIGPPPYA---GFAEDAAKQLAKETGIKVELVPGSSIGTLIEALAAGDADVAVGPIAPALEAAADKL--APGGLYI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016943462 113 ADGSPGYWSVLIVNKDSPINNlNDMLAKRKELTFGNGDPNSTSGYLvpGYYVFAKNNASASDFKRTVNASHETNALAVAN 192
Cdd:cd00648    77 VPELYVGGYVLVVRKGSSIKG-LLAVADLDGKRVGVGDPGSTAVRQ--ARLALGAYGLKKKDPEVVPVPGTSGALAAVAN 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1016943462 193 KQVDVATNNTENLdklkTSAPDKLKEIKVIWKS--PLIPGDPIVWRK 237
Cdd:cd00648   154 GAVDAAIVWVPAA----ERAQLGNVQLEVLPDDlgPLVTTFGVAVRK 196
TauA COG0715
ABC-type nitrate/sulfonate/bicarbonate transport system, periplasmic component [Inorganic ion ...
60-199 6.72e-08

ABC-type nitrate/sulfonate/bicarbonate transport system, periplasmic component [Inorganic ion transport and metabolism];


Pssm-ID: 440479 [Multi-domain]  Cd Length: 297  Bit Score: 53.09  E-value: 6.72e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016943462  60 KLGIKVNAFFAPDYAGIIQGMRFNKVDIAWYGNLSAMEAvdRANG---QVFAQTVAADGspgywSVLIVNKDSPINNLND 136
Cdd:COG0715    48 KEGLDVELVEFAGGAAALEALAAGQADFGVAGAPPALAA--RAKGapvKAVAALSQSGG-----NALVVRKDSGIKSLAD 120
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1016943462 137 MLAKRkeltFGnGDPNSTSGYLVPgyYVFAKNNASASDFKrTVNASHETNALAVANKQVDVAT 199
Cdd:COG0715   121 LKGKK----VA-VPGGSTSHYLLR--ALLAKAGLDPKDVE-IVNLPPPDAVAALLAGQVDAAV 175
PBP2_NrtA_SsuA_CpmA_like cd01008
Substrate binding domain of ABC-type nitrate/sulfonate/bicarbonate transporters, a member of ...
58-198 2.00e-03

Substrate binding domain of ABC-type nitrate/sulfonate/bicarbonate transporters, a member of the type 2 periplasmic binding fold superfamily; This family represents the periplasmic binding proteins involved in nitrate, alkanesulfonate, and bicarbonate transport. These domains are found in eubacterial perisplamic-binding proteins that serve as initial receptors in the ABC transport of bicarbonate, nitrate, taurine, or a wide range of aliphatic sulfonates. Other closest homologs involved in thiamine (vitamin B1) biosynthetic pathway and desulfurization (DszB) are also included in this family. After binding their ligand with high affinity, they 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. These 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: 270229 [Multi-domain]  Cd Length: 212  Bit Score: 38.81  E-value: 2.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016943462  58 ETKLGIKVNAFFAPDYAGIIQGMRFNKVDIAWYGNLSAMEAvdRANGQVFaQTVAADGSPGYWSVLIVNKDSPINNLNDM 137
Cdd:cd01008    26 KEKEGIDVEWVEFTSGPPALEALAAGSLDFGTGGDTPALLA--AAGGVPV-VLIAALSRSPNGNGIVVRKDSGITSLADL 102
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1016943462 138 LAKRKELTFGngdpnSTSGYLVpgYYVFAKNNASASDFKrTVNASHETNALAVANKQVDVA 198
Cdd:cd01008   103 KGKKIAVTKG-----TTGHFLL--LKALAKAGLSVDDVE-LVNLGPADAAAALASGDVDAW 155
PBP2_SsuA_like_1 cd13556
Substrate binding domain of putative sulfonate binding protein, a member of the type 2 ...
77-196 7.27e-03

Substrate binding domain of putative sulfonate binding protein, a member of the type 2 periplasmic binding fold superfamily; This subfamily includes the periplasmic component of putative ABC-type sulfonate transport system similar to SsuA. These domains are found in eubacterial SsuA proteins that serve as initial receptors in the ABC transport of bicarbonate, nitrate, taurine, or a wide range of aliphatic sulfonates, while other closest homologs are involved in thiamine (vitamin B1) biosynthetic pathway and desulfurization (DszB). After binding the ligand, SsuA interacts 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. The SsuA 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: 270274  Cd Length: 265  Bit Score: 37.45  E-value: 7.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016943462  77 IQGMRFNKVDIAWYGNLSAMEAvdRANGQ------VFaqtvaadgSPGYWSVLIVNKDSPINNLNDMLAKRKELTFGNgD 150
Cdd:cd13556    45 LEFLNSGSVDFGSTAGLAALLA--KANGNpiktvyVY--------SRPEWTALVVRKDSPIRSVADLKGKKVAVTKGT-D 113
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1016943462 151 PnstsgylvpgyYVF---AKNNA--SASDFkRTVNASHETNALAVANKQVD 196
Cdd:cd13556   114 P-----------YIFllrALNTAglSKNDI-EIVNLQHADGRTALEKGDVD 152
 
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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