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Conserved domains on  [gi|491533412|ref|WP_005391035|]
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MULTISPECIES: phosphate ABC transporter substrate-binding protein [Vibrio]

Protein Classification

phosphate ABC transporter substrate-binding protein( domain architecture ID 10194586)

phosphate ABC transporter substrate-binding protein similar to Bacillus subtilis phosphate-binding protein PstS, part of the ABC transporter complex PstSACB that is involved in phosphate import

CATH:  3.40.190.10
Gene Ontology:  GO:0140359|GO:0042626|GO:0055052|GO:0006817
PubMed:  26517916|24638992|25750732
TCDB:  3.A.1

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PBP2_phosphate_like_1 cd13653
Substrate binding domain of putative ABC-type phosphate transporter, a member of the type 2 ...
 20-265 1.21e-88

Substrate binding domain of putative ABC-type phosphate transporter, a member of the type 2 periplasmic binding fold superfamily; This subfamily contains uncharacterized phosphate binding domains found in PstS proteins that serve as initial receptors in the ABC transport of phosphate in eubacteria and archaea. After binding the ligand, PstS 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 PstS 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: 270371 [Multi-domain]  Cd Length: 240  Bit Score: 263.28  E-value: 1.21e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491533412  20 AKEINISGSTSVARVMDVLAEEYNKTHPDDYIAVQGIGSSAGITMVNKGVAEIGMSSRYLTESEKGE--DLNVYPIAYDG 97
Cdd:cd13653    1 SGTITISGSTTVAPLAEALAEAFMEKHPGVRIEVQGGGSGTGIKALIEGTADIGMASRPLKAEEKAAasGLVEHVIALDG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491533412  98 LAVVVNRTNSVKNLSQQQLFDIYKGKIKNWKEVGGADQPIAVVTREASSGSRYSFESLLGLTKivndrlvsDISPNNLVV 177
Cdd:cd13653   81 IAIIVNPDNPVKNLTLEQLRDIFSGKITNWKEVGGPDGPIVVISREEGSGTRETFEELVLGKK--------DFAKNAVVV 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491533412 178 NSNSMVKTIVNHNTRAIGFISVGSVD-RSIKAIQLDGIDPTSANISNHKYKLARPFLVLYKvNKISEPGKGFVTFLRSEQ 256
Cdd:cd13653  153 PSNGAVVQAVAKNPNAIGYVSLGYVDdSKVKALSVDGVAPTPENIKSGKYPLSRPLYLYTK-GEPSGLVKAFIDFALSPE 231


                 ....*....
gi 491533412 257 GQKAIADYG 265
Cdd:cd13653  232 GQAIVEKLG 240
 
Name Accession Description Interval E-value
PBP2_phosphate_like_1 cd13653
Substrate binding domain of putative ABC-type phosphate transporter, a member of the type 2 ...
 20-265 1.21e-88

Substrate binding domain of putative ABC-type phosphate transporter, a member of the type 2 periplasmic binding fold superfamily; This subfamily contains uncharacterized phosphate binding domains found in PstS proteins that serve as initial receptors in the ABC transport of phosphate in eubacteria and archaea. After binding the ligand, PstS 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 PstS 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: 270371 [Multi-domain]  Cd Length: 240  Bit Score: 263.28  E-value: 1.21e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491533412  20 AKEINISGSTSVARVMDVLAEEYNKTHPDDYIAVQGIGSSAGITMVNKGVAEIGMSSRYLTESEKGE--DLNVYPIAYDG 97
Cdd:cd13653    1 SGTITISGSTTVAPLAEALAEAFMEKHPGVRIEVQGGGSGTGIKALIEGTADIGMASRPLKAEEKAAasGLVEHVIALDG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491533412  98 LAVVVNRTNSVKNLSQQQLFDIYKGKIKNWKEVGGADQPIAVVTREASSGSRYSFESLLGLTKivndrlvsDISPNNLVV 177
Cdd:cd13653   81 IAIIVNPDNPVKNLTLEQLRDIFSGKITNWKEVGGPDGPIVVISREEGSGTRETFEELVLGKK--------DFAKNAVVV 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491533412 178 NSNSMVKTIVNHNTRAIGFISVGSVD-RSIKAIQLDGIDPTSANISNHKYKLARPFLVLYKvNKISEPGKGFVTFLRSEQ 256
Cdd:cd13653  153 PSNGAVVQAVAKNPNAIGYVSLGYVDdSKVKALSVDGVAPTPENIKSGKYPLSRPLYLYTK-GEPSGLVKAFIDFALSPE 231


                 ....*....
gi 491533412 257 GQKAIADYG 265
Cdd:cd13653  232 GQAIVEKLG 240
PstS COG0226
ABC-type phosphate transport system, periplasmic component [Inorganic ion transport and ...
 18-270 3.42e-76

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


Pssm-ID: 439996 [Multi-domain]  Cd Length: 275  Bit Score: 232.85  E-value: 3.42e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491533412  18 AIAKEINISGSTSVARVMDVLAEEYNKTHPDDYIAVQGIGSSAGITMVNKGVAEIGMSSRYLTESEK------GEDLNVY 91
Cdd:COG0226    1 AASGTITIAGSSTVYPLAEAWAEAFQKANPGVTINVQSGGSGGGIKQFIAGTVDIGNSSRPLKDEELeaakenGVELVEI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491533412  92 PIAYDGLAVVVNRTNSVKNLSQQQLFDIYKGKIKNWKEVGGA--DQPIAVVTREASSGSRYSFESLLGLTKivndrlvSD 169
Cdd:COG0226   81 PVAIDGIAVVVNPDNPVKNLTGEQLADIFSGKITNWNDIGGKlpDEPITVVGRSDGSGTTDYFTEYLLGVG-------AE 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491533412 170 ISPNNLVVNSNSMVKTIVNHNTRAIGFISVGSVD-RSIKAIQLD-----GIDPTSANISNHKYKLARPFLVLYKVNKISE 243
Cdd:COG0226  154 VREGVEGAEGNEGVVQAVAQTPGAIGYVGLSYAEqNKLKALAIDnkagkFVEPTAENIAAGSYPLSRPLYIYVKKEPDAK 233

                        250       260
                 ....*....|....*....|....*....
gi 491533412 244 PG--KGFVTFLRSEQGQKAIADYGYTPVK 270
Cdd:COG0226  234 APavKAFLDFVLSDGGQKIVEKLGYVPLP 262
ptsS_2 TIGR02136
phosphate binding protein; Members of this family are phosphate-binding proteins. Most are ...
 21-269 9.46e-67

phosphate binding protein; Members of this family are phosphate-binding proteins. Most are found in phosphate ABC-transporter operons, but some are found in phosphate regulatory operons. This model separates members of the current family from the phosphate ABC transporter phosphate binding protein described by TIGRFAMs model TIGR00975. [Transport and binding proteins, Anions]


Pssm-ID: 273991 [Multi-domain]  Cd Length: 287  Bit Score: 209.22  E-value: 9.46e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491533412   21 KEINISGSTSVARVMDVLAEEYNKTHPDDYIAVQGIGSSAGITMVNKGVAEIGMSSRYLTESE------KGEDLNVYPIA 94
Cdd:TIGR02136  36 STITIDGSTTVAPLAEAAAEEFQKIHPGVSVTVQGAGSGTGIKALINGTVDIGNSSRPIKDEElqkdkqKGIKLIEHKVA 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491533412   95 YDGLAVVVNRTNS-VKNLSQQQLFDIYKGKIKNWKEVGGA--DQPIAVVTREASSGSRYSFEsllglTKIVNDRlvsDIS 171
Cdd:TIGR02136 116 VDGLAVVVNKKNVpVDDLTVEQLKKIYSGEITNWKEVGGDlpNKPIVVVGRNAGSGTRDTFE-----EEVMGKA---KIK 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491533412  172 PNNLVVNSNSMVKTIVNHNTRAIGFISVGSVDRSIKAIQLDGIDPTSANISNHKYKLARP-FLVLYKVNKISEPGKGFVT 250
Cdd:TIGR02136 188 PGKNEQESNGAVVSIVSSNPGAIGYLGLGYVDDSVKTLKVNGVEPSKENIANGSYPLSRPlFMYVNGKPKKPELVAEFID 267

                         250       260
                  ....*....|....*....|
gi 491533412  251 FLRS-EQGQKAIADYGYTPV 269
Cdd:TIGR02136 268 FVLSdDGGERIVEELGYVPL 287
PBP_like_2 pfam12849
PBP superfamily domain; This domain belongs to the periplasmic binding protein superfamily.
 13-256 5.09e-34

PBP superfamily domain; This domain belongs to the periplasmic binding protein superfamily.


Pssm-ID: 432831 [Multi-domain]  Cd Length: 267  Bit Score: 124.20  E-value: 5.09e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491533412   13 AVSLPAIAKEINISGSTSVARVMDVLAEEYNKTHPDDYIAVQGIGSSAGITMVNKGVAEIGMSSRYLTESEKGE------ 86
Cdd:pfam12849   2 AAASAPTVGTILIAGSSTQAPGLLDLAEAFEKKYPGAKVKVTSVGSGEGIKALLNGDVDVALVSRPLTEEEFEAfganga 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491533412   87 -DLNVYPIAYDGLAVVVNRTNSVKNLSQQQLFDIYKGKIKNWKEvGGADQPIAVVTREASSGSRYSFESLLGLTKIVNDR 165
Cdd:pfam12849  82 gGLVEVPVAYDGIAIVVNKDNPANILTVEALKKIFSGKITNWND-GGPDGPIKFVSRGDNSGTTELFSTHLKEKGPWGAA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491533412  166 lvsdispnNLVVNSNSMVKTIVNHNTrAIGFISVGS----------------VDRSIKAIQLDGI-------DPTSANIS 222
Cdd:pfam12849 161 --------GIGAAGSPGVASVVAGPG-AIGYVEVSYalanlgytladvaggtYLSFAKALKVAKInpgaglvIPLEEAIA 231

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 491533412  223 NHKYKLARP-FLVLYKVNKISEPG-KGFVTFLRSEQ 256
Cdd:pfam12849 232 DGDYPLSRPyYVIVKNPPKGPAPLaKAFLDFLLSDE 267
PRK10918 PRK10918
phosphate ABC transporter substrate-binding protein PstS;
1-223 1.57e-12

phosphate ABC transporter substrate-binding protein PstS;


Pssm-ID: 182837  Cd Length: 346  Bit Score: 66.39  E-value: 1.57e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491533412   1 MLRFTVATLLAIAVSLPAI----AKEINISGSTSVARVMDVLAEEYNKtHPDDYIAVQGIGSSAGITMVNKGVAEIGMSS 76
Cdd:PRK10918   3 VMRTTVATVVAATLSMSAFsafaAASLTGAGATFPAPVYAKWADTYQK-ETGNKVNYQGIGSSGGVKQIIANTVDFGASD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491533412  77 RYLTESEKGED-LNVYPIAYDGLAVVVNrTNSVKN----LSQQQLFDIYKGKIKNWKE---------VGGADQPIAVVTR 142
Cdd:PRK10918  82 APLSDEKLAQEgLFQFPTVIGGVVLAVN-IPGLKSgelvLDGKTLGDIYLGKIKKWNDeaiaklnpgVKLPSQNIAVVRR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491533412 143 EASSGSRYSFESLLGLtkiVNDRLVSDIS-------PNNLVVNSNSMVKTIVNHNTRAIGFISVGSVDRS----IKAIQL 211
Cdd:PRK10918 161 ADGSGTSFVFTSYLAK---VNEEWKSKVGagstvnwPTGLGGKGNDGIAAFVQRLPGAIGYVEYAYAKQNnlayTKLISA 237

                        250
                 ....*....|....
gi 491533412 212 DG--IDPTSANISN 223
Cdd:PRK10918 238 DGkpVSPTEESFSN 251
 
Name Accession Description Interval E-value
PBP2_phosphate_like_1 cd13653
Substrate binding domain of putative ABC-type phosphate transporter, a member of the type 2 ...
 20-265 1.21e-88

Substrate binding domain of putative ABC-type phosphate transporter, a member of the type 2 periplasmic binding fold superfamily; This subfamily contains uncharacterized phosphate binding domains found in PstS proteins that serve as initial receptors in the ABC transport of phosphate in eubacteria and archaea. After binding the ligand, PstS 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 PstS 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: 270371 [Multi-domain]  Cd Length: 240  Bit Score: 263.28  E-value: 1.21e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491533412  20 AKEINISGSTSVARVMDVLAEEYNKTHPDDYIAVQGIGSSAGITMVNKGVAEIGMSSRYLTESEKGE--DLNVYPIAYDG 97
Cdd:cd13653    1 SGTITISGSTTVAPLAEALAEAFMEKHPGVRIEVQGGGSGTGIKALIEGTADIGMASRPLKAEEKAAasGLVEHVIALDG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491533412  98 LAVVVNRTNSVKNLSQQQLFDIYKGKIKNWKEVGGADQPIAVVTREASSGSRYSFESLLGLTKivndrlvsDISPNNLVV 177
Cdd:cd13653   81 IAIIVNPDNPVKNLTLEQLRDIFSGKITNWKEVGGPDGPIVVISREEGSGTRETFEELVLGKK--------DFAKNAVVV 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491533412 178 NSNSMVKTIVNHNTRAIGFISVGSVD-RSIKAIQLDGIDPTSANISNHKYKLARPFLVLYKvNKISEPGKGFVTFLRSEQ 256
Cdd:cd13653  153 PSNGAVVQAVAKNPNAIGYVSLGYVDdSKVKALSVDGVAPTPENIKSGKYPLSRPLYLYTK-GEPSGLVKAFIDFALSPE 231


                 ....*....
gi 491533412 257 GQKAIADYG 265
Cdd:cd13653  232 GQAIVEKLG 240
PBP2_phosphate cd13566
Substrate binding domain of putative ABC-type phosphate transporter, a member of the type 2 ...
 20-265 2.01e-82

Substrate binding domain of putative ABC-type phosphate transporter, a member of the type 2 periplasmic binding fold superfamily; This subfamily contains uncharacterized phosphate binding domains found in PstS proteins that serve as initial receptors in the ABC transport of phosphate in eubacteria and archaea. After binding the ligand, PstS 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 PstS proteins belong to the PBPII 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: 270284 [Multi-domain]  Cd Length: 245  Bit Score: 247.50  E-value: 2.01e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491533412  20 AKEINISGSTSVARVMDVLAEEYNKTHPDDYIAVQGIGSSAGITMVNKGVAEIGMSSRYLTESEK------GEDLNVYPI 93
Cdd:cd13566    1 SGTITIAGSSTVAPLAEALAEEFMKKHPGVRVTVQGGGSGAGIKALIAGTADIAMASRPLKDEEKaaaeanGIELVEFVI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491533412  94 AYDGLAVVVNRTNSVKNLSQQQLFDIYKGKIKNWKEVGGADQPIAVVTREASSGSRYSFESLLGLTKivndrlvsDISPN 173
Cdd:cd13566   81 AYDGIAVIVNPDNPVASLTLEQLRDIFTGKITNWSEVGGPDEPIVVYGRDEGSGTRDYFEELVLGKG--------EFIRN 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491533412 174 NLVVNSNSMVKTIVNHNTRAIGFISVGSVDRS--IKAIQLDGIDPTSANISNHKYKLARPFLVLYKvNKISEPGKGFVTF 251
Cdd:cd13566  153 AVVAPSNGALVQAVAGDPNAIGYVGLGYVDENkkVKALKVDGVAPTVENIKSGKYPLSRPLFLYTK-GEPSPAVKAFIDF 231

                        250
                 ....*....|....
gi 491533412 252 LRSEQGQKAIADYG 265
Cdd:cd13566  232 ALSPEGQKIIEEVG 245
PstS COG0226
ABC-type phosphate transport system, periplasmic component [Inorganic ion transport and ...
 18-270 3.42e-76

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


Pssm-ID: 439996 [Multi-domain]  Cd Length: 275  Bit Score: 232.85  E-value: 3.42e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491533412  18 AIAKEINISGSTSVARVMDVLAEEYNKTHPDDYIAVQGIGSSAGITMVNKGVAEIGMSSRYLTESEK------GEDLNVY 91
Cdd:COG0226    1 AASGTITIAGSSTVYPLAEAWAEAFQKANPGVTINVQSGGSGGGIKQFIAGTVDIGNSSRPLKDEELeaakenGVELVEI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491533412  92 PIAYDGLAVVVNRTNSVKNLSQQQLFDIYKGKIKNWKEVGGA--DQPIAVVTREASSGSRYSFESLLGLTKivndrlvSD 169
Cdd:COG0226   81 PVAIDGIAVVVNPDNPVKNLTGEQLADIFSGKITNWNDIGGKlpDEPITVVGRSDGSGTTDYFTEYLLGVG-------AE 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491533412 170 ISPNNLVVNSNSMVKTIVNHNTRAIGFISVGSVD-RSIKAIQLD-----GIDPTSANISNHKYKLARPFLVLYKVNKISE 243
Cdd:COG0226  154 VREGVEGAEGNEGVVQAVAQTPGAIGYVGLSYAEqNKLKALAIDnkagkFVEPTAENIAAGSYPLSRPLYIYVKKEPDAK 233

                        250       260
                 ....*....|....*....|....*....
gi 491533412 244 PG--KGFVTFLRSEQGQKAIADYGYTPVK 270
Cdd:COG0226  234 APavKAFLDFVLSDGGQKIVEKLGYVPLP 262
PBP2_phosphate_binding cd01006
Substrate binding domain of ABC-type phosphate transporter, a member of the type 2 ...
 20-265 4.59e-68

Substrate binding domain of ABC-type phosphate transporter, a member of the type 2 periplasmic-binding fold superfamily; This phosphate-binding domain shows significant homology to the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. 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: 270227 [Multi-domain]  Cd Length: 253  Bit Score: 211.35  E-value: 4.59e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491533412  20 AKEINISGSTSVARVMDVLAEEYNKTHPDDYIAVQGIGSSAGITMVNKGVAEIGMSSRYLTESE-KGEDLNVYPIAYDGL 98
Cdd:cd01006    1 ASELTISGSTSVAPI*DVWAEKYNQQHPETYVAVQGVGSTAGISQLKAGTVDIGASDAYLSESEaANKGLHTFTLAIDGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491533412  99 AVVVNRTNSVKNL--SQQQLFDIYKGKIKNWKEVGGA---------DQPIAVVTREASSGSRYSFESLLGLTKIVND--- 164
Cdd:cd01006   81 AIVVNQPGPVTNLtlNGKQLYGIYKGQIKNWDDVGIAalnpgvnlpDQKIAVVTREDGSGTRFSFTSYLGKTKTEKDgkg 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491533412 165 -RLVSDISPNNLVVNSNSMVKTIVNHNTRAIGFISVGSVDRS-IKAIQLdgidptsanisnhkYKLARPFLVL-YKVNKI 241
Cdd:cd01006  161 tTEVSDVAPTALGVNGNSG*KTLVNHNPGAVGYISIGSVDQSsLKAIQL--------------YPISRPFLILhYSDQKD 226

                        250       260
                 ....*....|....*....|....*..
gi 491533412 242 SEPG---KGFVTFLRSEQGQKAIADYG 265
Cdd:cd01006  227 AATDeqtKEFIAWAKSEGAAKLIVEYG 253
ptsS_2 TIGR02136
phosphate binding protein; Members of this family are phosphate-binding proteins. Most are ...
 21-269 9.46e-67

phosphate binding protein; Members of this family are phosphate-binding proteins. Most are found in phosphate ABC-transporter operons, but some are found in phosphate regulatory operons. This model separates members of the current family from the phosphate ABC transporter phosphate binding protein described by TIGRFAMs model TIGR00975. [Transport and binding proteins, Anions]


Pssm-ID: 273991 [Multi-domain]  Cd Length: 287  Bit Score: 209.22  E-value: 9.46e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491533412   21 KEINISGSTSVARVMDVLAEEYNKTHPDDYIAVQGIGSSAGITMVNKGVAEIGMSSRYLTESE------KGEDLNVYPIA 94
Cdd:TIGR02136  36 STITIDGSTTVAPLAEAAAEEFQKIHPGVSVTVQGAGSGTGIKALINGTVDIGNSSRPIKDEElqkdkqKGIKLIEHKVA 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491533412   95 YDGLAVVVNRTNS-VKNLSQQQLFDIYKGKIKNWKEVGGA--DQPIAVVTREASSGSRYSFEsllglTKIVNDRlvsDIS 171
Cdd:TIGR02136 116 VDGLAVVVNKKNVpVDDLTVEQLKKIYSGEITNWKEVGGDlpNKPIVVVGRNAGSGTRDTFE-----EEVMGKA---KIK 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491533412  172 PNNLVVNSNSMVKTIVNHNTRAIGFISVGSVDRSIKAIQLDGIDPTSANISNHKYKLARP-FLVLYKVNKISEPGKGFVT 250
Cdd:TIGR02136 188 PGKNEQESNGAVVSIVSSNPGAIGYLGLGYVDDSVKTLKVNGVEPSKENIANGSYPLSRPlFMYVNGKPKKPELVAEFID 267

                         250       260
                  ....*....|....*....|
gi 491533412  251 FLRS-EQGQKAIADYGYTPV 269
Cdd:TIGR02136 268 FVLSdDGGERIVEELGYVPL 287
PBP_like_2 pfam12849
PBP superfamily domain; This domain belongs to the periplasmic binding protein superfamily.
 13-256 5.09e-34

PBP superfamily domain; This domain belongs to the periplasmic binding protein superfamily.


Pssm-ID: 432831 [Multi-domain]  Cd Length: 267  Bit Score: 124.20  E-value: 5.09e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491533412   13 AVSLPAIAKEINISGSTSVARVMDVLAEEYNKTHPDDYIAVQGIGSSAGITMVNKGVAEIGMSSRYLTESEKGE------ 86
Cdd:pfam12849   2 AAASAPTVGTILIAGSSTQAPGLLDLAEAFEKKYPGAKVKVTSVGSGEGIKALLNGDVDVALVSRPLTEEEFEAfganga 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491533412   87 -DLNVYPIAYDGLAVVVNRTNSVKNLSQQQLFDIYKGKIKNWKEvGGADQPIAVVTREASSGSRYSFESLLGLTKIVNDR 165
Cdd:pfam12849  82 gGLVEVPVAYDGIAIVVNKDNPANILTVEALKKIFSGKITNWND-GGPDGPIKFVSRGDNSGTTELFSTHLKEKGPWGAA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491533412  166 lvsdispnNLVVNSNSMVKTIVNHNTrAIGFISVGS----------------VDRSIKAIQLDGI-------DPTSANIS 222
Cdd:pfam12849 161 --------GIGAAGSPGVASVVAGPG-AIGYVEVSYalanlgytladvaggtYLSFAKALKVAKInpgaglvIPLEEAIA 231

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 491533412  223 NHKYKLARP-FLVLYKVNKISEPG-KGFVTFLRSEQ 256
Cdd:pfam12849 232 DGDYPLSRPyYVIVKNPPKGPAPLaKAFLDFLLSDE 267
PBP_like pfam12727
PBP superfamily domain; This family belongs to the periplasmic binding domain superfamily. It ...
 39-210 8.87e-31

PBP superfamily domain; This family belongs to the periplasmic binding domain superfamily. It is often associated with a helix-turn-helix domain.


Pssm-ID: 463683 [Multi-domain]  Cd Length: 192  Bit Score: 113.44  E-value: 8.87e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491533412   39 AEEYNKTHPDDYIAVQGIGSSAGITMVNKGVAEIGMSSRYLTESEkGEDLNVYPIAYDGLAVVVnrtnsVKNLSQQQLFD 118
Cdd:pfam12727   1 AEELARKHPGVRLAVAYVGSLGGLAALRRGEAHIAGIHLLDPETG-EYNLPFLRRLLPGIPVVL-----INLAYREQGLV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491533412  119 IYKG---KIKNWKEVggADQPIAVVTREASSGSRYSFESLLGLTKIVNdrlvSDISPNNLVVNSNSMVKTIVNHNTRAIG 195
Cdd:pfam12727  75 VAPGnpkGITGWEDL--ARPGLRFVNRQRGSGTRVLLDELLRKAGIDP----SDINGYDREERSHLAVAAAVASGRADAG 148

                         170
                  ....*....|....*
gi 491533412  196 FiSVGSVDRSIKAIQ 210
Cdd:pfam12727 149 L-GIEAAARALGGLD 162
PBP2_phosphate_like_2 cd13654
Substrate binding domain of putative ABC-type phosphate transporter, a member of the type 2 ...
 22-265 1.67e-29

Substrate binding domain of putative ABC-type phosphate transporter, a member of the type 2 periplasmic binding fold superfamily; This subfamily contains uncharacterized phosphate binding domains found in PstS proteins that serve as initial receptors in the ABC transport of phosphate in eubacteria and archaea. After binding the ligand, PstS 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 PstS 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: 270372  Cd Length: 259  Bit Score: 111.96  E-value: 1.67e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491533412  22 EINISGSTSVARVMDVLAEEYNKTHPDDYIAVQGIGSSAGITMVNKGVAEIGMSSRYLTESE------KGEDLNVYPIAY 95
Cdd:cd13654    3 QIRIDGSSTVYPITEAVAEEFGKSGPGVTVTVGSSGTGGGFKKFCAGETDISNASRPIKDSEaelceaNGIEYIELPVAY 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491533412  96 DGLAVVVNRTN-SVKNLSQQQLFDI--YKGKIKNWKEVGGA--DQPIAVVTREASSGSRYSF-ESLLGLTKivndRLVSD 169
Cdd:cd13654   83 DGLTVVVNPANdWAKCLTELELKSIwaAESPITTWSDVRPSwpDEPIELYGPGTDSGTFDYFtEAIVGEGG----SIRED 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491533412 170 ISPNNlvvNSNSMVKTIVNhNTRAIGFISVGSVDR---SIKAIQLDGIDPTSA-----NISNHKYKLARPfLVLYkVNKI 241
Cdd:cd13654  159 YTASE---DDNVLVQGVAG-DKNALGFFGYAYYEEngdKLKAVKIDGGEGTVApsaetTISGGYYPLSRP-LFIY-VKKA 232

                        250       260
                 ....*....|....*....|....*...
gi 491533412 242 S---EPG-KGFVTFLRSEQgQKAIADYG 265
Cdd:cd13654  233 SlaeKPAvAAFVKFYLENA-QEAAGEVG 259
PBP2_PstS cd13565
Substrate binding domain of ABC-type phosphate transporter, a member of the type 2 ...
 20-265 2.35e-26

Substrate binding domain of ABC-type phosphate transporter, a member of the type 2 periplasmic-binding fold superfamily; This subfamily contians phosphate binding domain found in PstS proteins that serve as initial receptors in the ABC transport of phosphate in eubacteria and archaea. After binding the ligand, PstS 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 PstS proteins belong to the PBPII 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: 270283 [Multi-domain]  Cd Length: 254  Bit Score: 103.46  E-value: 2.35e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491533412  20 AKEINISGSTSVARVMDVLAEEYNKTHPDDYIAVQGIGSSAGITMVNKGVAEIGMSSRYLTESE-KGEDLNVY--PIAYD 96
Cdd:cd13565    1 AVTLTGAGATFPAPLYQKWIDEYKKAHPGVKINYQSIGSGAGIKQFIAGTVDFGASDAPLSDAElAKAGGGLLqiPTVIG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491533412  97 GLAVVVNRT--NSVKNLSQQQLFDIYKGKIKNWKEVGGA---------DQPIAVVTREASSGSRYSFESLLGL------T 159
Cdd:cd13565   81 AVVVAYNLPgvKGLLLLSGEVLADIFLGKITKWNDPAIAalnpgvnlpDTPITVVHRSDGSGTTFIFTDYLSAvspewkD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491533412 160 KIVNDRLVSdiSPNNLVVNSNSMVKTIVNHNTRAIGFISVG-SVDRSIKAIQLdgidptsanisnhkYKLARP-FLVLYK 237
Cdd:cd13565  161 KVGAGKSVA--WPVGLGGKGNEGVAAAVKQTPGSIGYVELSyALQNGLPAAAL--------------YPIVGFtYILVKK 224

                        250       260       270
                 ....*....|....*....|....*....|.
gi 491533412 238 VNKISEPG---KGFVTFLRSEqGQKAIADYG 265
Cdd:cd13565  225 DYKDAEKAkavKKFLKWALTE-GQKFAADLG 254
3a0107s03 TIGR00975
phosphate ABC transporter, phosphate-binding protein; This family represents one type of ...
 26-156 8.76e-15

phosphate ABC transporter, phosphate-binding protein; This family represents one type of (periplasmic, in Gram-negative bacteria) phosphate-binding protein found in phosphate ABC (ATP-binding cassette) transporters. This protein is accompanied, generally in the same operon, by an ATP binding protein and (usually) two permease proteins. [Transport and binding proteins, Anions]


Pssm-ID: 273374 [Multi-domain]  Cd Length: 313  Bit Score: 72.86  E-value: 8.76e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491533412   26 SGSTSVARVMDVLAEEYNKTHPDDYIAVQGIGSSAGITMVNKGVAEIGMSSRYLTESE---KGEDLNVYPIAYDGLAVVV 102
Cdd:TIGR00975   4 AGSTFPAPLYTKWFPDFQKSNPGVTINYQGIGSGAGIAQFAAGTVDFGASDAPLSEADlaaAGSGLLNFPTVIGAIVVTY 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491533412  103 NrTNSVK---NLSQQQLFDIYKGKIKNW---------KEVGGADQPIAVVTREASSGSRYSFESLL 156
Cdd:TIGR00975  84 N-LPGVSeklKLDGPVLAKIFLGKIKQWndpaiaalnPGVKLPGTAITVVHRSDGSGTTFNFTNYL 148
PRK10918 PRK10918
phosphate ABC transporter substrate-binding protein PstS;
1-223 1.57e-12

phosphate ABC transporter substrate-binding protein PstS;


Pssm-ID: 182837  Cd Length: 346  Bit Score: 66.39  E-value: 1.57e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491533412   1 MLRFTVATLLAIAVSLPAI----AKEINISGSTSVARVMDVLAEEYNKtHPDDYIAVQGIGSSAGITMVNKGVAEIGMSS 76
Cdd:PRK10918   3 VMRTTVATVVAATLSMSAFsafaAASLTGAGATFPAPVYAKWADTYQK-ETGNKVNYQGIGSSGGVKQIIANTVDFGASD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491533412  77 RYLTESEKGED-LNVYPIAYDGLAVVVNrTNSVKN----LSQQQLFDIYKGKIKNWKE---------VGGADQPIAVVTR 142
Cdd:PRK10918  82 APLSDEKLAQEgLFQFPTVIGGVVLAVN-IPGLKSgelvLDGKTLGDIYLGKIKKWNDeaiaklnpgVKLPSQNIAVVRR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491533412 143 EASSGSRYSFESLLGLtkiVNDRLVSDIS-------PNNLVVNSNSMVKTIVNHNTRAIGFISVGSVDRS----IKAIQL 211
Cdd:PRK10918 161 ADGSGTSFVFTSYLAK---VNEEWKSKVGagstvnwPTGLGGKGNDGIAAFVQRLPGAIGYVEYAYAKQNnlayTKLISA 237

                        250
                 ....*....|....
gi 491533412 212 DG--IDPTSANISN 223
Cdd:PRK10918 238 DGkpVSPTEESFSN 251
ModA COG0725
ABC-type molybdate transport system, periplasmic Mo-binding protein ModA [Inorganic ion ...
 1-270 1.08e-08

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


Pssm-ID: 440489 [Multi-domain]  Cd Length: 253  Bit Score: 54.49  E-value: 1.08e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491533412   1 MLRFTVATLLAIAVSLPAIAKEINISGSTSVARVMDVLAEEYNKTHPDDYIAVQGIGSSAGITMVNKGV-AEIGMSS--- 76
Cdd:COG0725    5 LLALLLLALLLAGASAAAAAAELTVFAAASLKEALEELAAAFEKEHPGVKVELSFGGSGALARQIEQGApADVFISAdek 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491533412  77 --RYLTESEKGEDLNVYPIAYDGLAVVVNRTNsvknlsqqqlfdiyKGKIKNWKEVGGADQPIAVVTREASSGSRYSFES 154
Cdd:COG0725   85 ymDKLAKKGLILAGSRVVFATNRLVLAVPKGN--------------PADISSLEDLAKPGVRIAIGDPKTVPYGKYAKEA 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491533412 155 L--LGLTKIVNDRLVsdispnnlvvnsnsMVKTIvnhnTRAIGFISVGSVD-----RSIkAIQLDGIDPTsANISNHKYK 227
Cdd:COG0725  151 LekAGLWDALKPKLV--------------LGENV----RQVLAYVESGEADagivyLSD-ALAAKGVLVV-VELPAELYA 210

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 491533412 228 LARPFLVLYKVNKISEPGKGFVTFLRSEQGQKAIADYGYTPVK 270
Cdd:COG0725  211 PIVYPAAVLKGAKNPEAAKAFLDFLLSPEAQAILEKYGFEPPK 253
PBP2_CysL_like cd08420
C-terminal substrate binding domain of LysR-type transcriptional regulator CysL, which ...
 22-253 3.26e-07

C-terminal substrate binding domain of LysR-type transcriptional regulator CysL, which activates the transcription of the cysJI operon encoding sulfite reductase, contains the type 2 periplasmic binding fold; CysL, also known as YwfK, is a regular of sulfur metabolism in Bacillus subtilis. Sulfur is required for the synthesis of proteins and essential cofactors in all living organism. Sulfur can be assimilated either from inorganic sources (sulfate and thiosulfate), or from organic sources (sulfate esters, sulfamates, and sulfonates). CysL activates the transcription of the cysJI operon encoding sulfite reductase, which reduces sulfite to sulfide. Both cysL mutant and cysJI mutant are unable to grow using sulfate or sulfite as the sulfur source. Like other LysR-type regulators, CysL also negatively regulates its own transcription. In Escherichia coli, three LysR-type activators are involved in the regulation of sulfur metabolism: CysB, Cbl and MetR. The topology of this substrate-binding domain is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. 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: 176112 [Multi-domain]  Cd Length: 201  Bit Score: 49.41  E-value: 3.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491533412  22 EINISGSTSVARVM--DVLAEeYNKTHPDdyIAVQ-GIGSSAGIT-MVNKGVAEIGmssryLTESE-KGEDLNVYPIAYD 96
Cdd:cd08420    1 TLRIGASTTIGEYLlpRLLAR-FRKRYPE--VRVSlTIGNTEEIAeRVLDGEIDLG-----LVEGPvDHPDLIVEPFAED 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491533412  97 GLAVVVNRTNSVKNLSQQQLFDIykgkiknwkevggADQPIavVTREASSGSRYSFESLLGLTKIVNDRLvsDISpnnLV 176
Cdd:cd08420   73 ELVLVVPPDHPLAGRKEVTAEEL-------------AAEPW--ILREPGSGTREVFERALAEAGLDGLDL--NIV---ME 132

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491533412 177 VNSNSMVKTIVNHNtRAIGFISVGSVDR-----SIKAIQLDGIDPTsanisnhkyklaRPFLVLYkvNKISEPGKGFVTF 251
Cdd:cd08420  133 LGSTEAIKEAVEAG-LGISILSRLAVRKelelgRLVALPVEGLRLT------------RPFSLIY--HKDKYLSPAAEAF 197


                 ..
gi 491533412 252 LR 253
Cdd:cd08420  198 LE 199
SBP_bac_11 pfam13531
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 24-267 4.50e-07

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


Pssm-ID: 463911 [Multi-domain]  Cd Length: 225  Bit Score: 49.57  E-value: 4.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491533412   24 NISGSTSVARVMDVLAEEYnKTHPDDYIAVQGIGSSAGITMV-NKGVAEIGMSS-----RYLTESEKGEDLNVYPIAYDG 97
Cdd:pfam13531   1 TVAAAGGLAAALRELAAAF-EAETGVKVVVSYGGSGKLAKQIaNGAPADVFISAdsawlDKLAAAGLVVPGSRVPLAYSP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491533412   98 LAVVVNRTNsvknlsqqqlfdiyKGKIKNWKEVGGADQPIAVVTREASSGSRYSFESL--LGLTKIVNDRLVsdispnNL 175
Cdd:pfam13531  80 LVIAVPKGN--------------PKDISGLADLLKPGVRLAVADPKTAPSGRAALELLekAGLLKALEKKVV------VL 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491533412  176 VVNSNSMVKTIVNhNTRAIGFISVGSVDRSIKAIQLDGIDPTSANISNHKYKLARPflvlyKVNKISEPGKGFVTFLRSE 255
Cdd:pfam13531 140 GENVRQALTAVAS-GEADAGIVYLSEALFPENGPGLEVVPLPEDLNLPLDYPAAVL-----KKAAHPEAARAFLDFLLSP 213

                         250
                  ....*....|..
gi 491533412  256 QGQKAIADYGYT 267
Cdd:pfam13531 214 EAQAILRKYGFR 225
PBP2_ModA_like_1 cd13538
Substrate binding domain of putative molybdate-binding protein;the type 2 periplasmic binding ...
 22-266 1.14e-04

Substrate binding domain of putative molybdate-binding protein;the type 2 periplasmic binding protein fold; This subfamily contains domains found in ModA proteins of putative ABC-type transporter. Molybdate transport system is comprised of a periplasmic binding protein, an integral membrane protein, and an energizer protein. These three proteins are coded by modA, modB, and modC genes, respectively. ModA proteins serve as initial receptors in the ABC transport of molybdate mostly in eubacteria and archaea. After binding molybdate with high affinity, they interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The ModA proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270256 [Multi-domain]  Cd Length: 230  Bit Score: 42.29  E-value: 1.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491533412  22 EINISGSTSVARVMDVLAEEYNKTHPDDYIAVQGIGSSAGITMVNKGV-AEIGMS--SRYLTE-SEKGEDL-NVYPIAYD 96
Cdd:cd13538    1 TLTVFAAASLTDAFTEIGEQFEKSNPGVKVTFNFAGSQALVTQIEQGApADVFASadTANMDAlVKAGLLVdTPTIFATN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491533412  97 GLAVVVNRTNsvknlsqqqlfdiyKGKIKNWKEVGGADQPIAVVTREASSGsRYSFESLLGLTKIVNDRLVSDISPNnlV 176
Cdd:cd13538   81 KLVVIVPKDN--------------PAKITSLADLAKPGVKIVIGAPEVPVG-TYTRRVLDKAGNDYAYGYKEAVLAN--V 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491533412 177 VNSNSMVKTIVnhnTRAI------GFISVGSVDRSIKAIQLDGIdPTSANISNhKYKLArpflvLYKVNKISEPGKGFVT 250
Cdd:cd13538  144 VSEETNVRDVV---TKVAlgeadaGFVYVTDAKAASEKLKVITI-PEEYNVTA-TYPIA-----VLKASKNPELARAFVD 213

                        250
                 ....*....|....*.
gi 491533412 251 FLRSEQGQKAIADYGY 266
Cdd:cd13538  214 FLLSEEGQAILAEYGF 229
PBP2_YvgL_like cd13537
Substrate binding domain of putative molybdate-binding protein YvgL and similar proteins;the ...
 22-267 1.18e-03

Substrate binding domain of putative molybdate-binding protein YvgL and similar proteins;the type 2 periplasmic binding protein fold; This subfamily contains domains found in ModA proteins of putative ABC-type transporter. ModA proteins serve as initial receptors in the ABC transport of molybdate in eubacteria and archaea. Bacteria and archaea import molybdenum and tungsten from the environment in the form of the oxyanions molybdate (MoO(4) (2-)) and tungstate (WO(4) (2-)). After binding molybdate and tungstate with high affinity, they interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The ModA proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270255 [Multi-domain]  Cd Length: 225  Bit Score: 39.19  E-value: 1.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491533412  22 EINISGSTSVARVMDVLAEEYNKTHPDDYIAVQGIGSSAGITMVNKGV-AEIGMSS--RYLTESEKGEDL---NVYPIAY 95
Cdd:cd13537    1 TLTVSAAASLKDALDEIATEYEKENPGVKITFNFGGSGTLQKQIESGApADVFFSAakKQMDALEDKGLIdasTRKNLLK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491533412  96 DGLAVVVNRTNSVKNLSQQQLFDiykgkiknwkevggADQPIAVVTREASSGSRYSFESL--LGLTKIVNDRLVsdisPN 173
Cdd:cd13537   81 NKLVLIVPKDSDSKISSFDLTKD--------------DVKKIAIGEPETVPAGKYAKEALekLGLWDEIESKLV----YG 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491533412 174 NLVVNsnsmVKTIVnhntrAIGFISVGSVDRSIKAIQLDGIDPTSANISNHK---YKLARpflvlYKVNKISEPGKGFVT 250
Cdd:cd13537  143 KDVRQ----VLTYV-----ETGNADAGFVYKTDALINKKVKVVEEAPEDTHTpiiYPIAV-----IKNSENKEEAQKFID 208

                        250
                 ....*....|....*..
gi 491533412 251 FLRSEQGQKAIADYGYT 267
Cdd:cd13537  209 FLKSEEAKKIFEKYGFE 225
 
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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