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Conserved domains on  [gi|308193616|gb|ADO16339|]
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phosphate ABC transporter, partial [Enterococcus faecium]

Protein Classification

type 2 periplasmic-binding domain-containing protein( domain architecture ID 229383)

type 2 periplasmic-binding protein (PBP2) is typically comprised of two globular subdomains connected by a flexible hinge; it binds its ligand in the cleft between these domains in a manner resembling a Venus flytrap; similar to the ligand-binding domains found in solute binding proteins that serve as initial receptors in the transport, signal transduction and channel gating

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Periplasmic_Binding_Protein_Type_2 super family cl21456
Type 2 periplasmic binding fold superfamily; This evolutionary model and hierarchy represent ...
 3-188 4.72e-73

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.


The actual alignment was detected with superfamily member TIGR02136:

Pssm-ID: 473866 [Multi-domain]  Cd Length: 287  Bit Score: 221.93  E-value: 4.72e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308193616    3 VFAEE--RDGVDASKLVDHKVAVVGMAPIVN-KDTDVKDITKQELIDIFTGKITNWKEVGG--KDQKINVVNRANGSGTR 77
Cdd:TIGR02136  94 IKDEElqKDKQKGIKLIEHKVAVDGLAVVVNkKNVPVDDLTVEQLKKIYSGEITNWKEVGGdlPNKPIVVVGRNAGSGTR 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308193616   78 ATFEKWGLDGATPVQSQ-EQDSSGTVRQLVSQTPGAISYLAFSYLDDSTQALSIDGVEPKEENVADNSWGIWSYEHMYTN 156
Cdd:TIGR02136 174 DTFEEEVMGKAKIKPGKnEQESNGAVVSIVSSNPGAIGYLGLGYVDDSVKTLKVNGVEPSKENIANGSYPLSRPLFMYVN 253

                         170       180       190
                  ....*....|....*....|....*....|....
gi 308193616  157 GKPS--PEVQKFLDYMMTEEIQEGPVKELGYLPI 188
Cdd:TIGR02136 254 GKPKkpELVAEFIDFVLSDDGGERIVEELGYVPL 287
 
Name Accession Description Interval E-value
ptsS_2 TIGR02136
phosphate binding protein; Members of this family are phosphate-binding proteins. Most are ...
 3-188 4.72e-73

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: 221.93  E-value: 4.72e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308193616    3 VFAEE--RDGVDASKLVDHKVAVVGMAPIVN-KDTDVKDITKQELIDIFTGKITNWKEVGG--KDQKINVVNRANGSGTR 77
Cdd:TIGR02136  94 IKDEElqKDKQKGIKLIEHKVAVDGLAVVVNkKNVPVDDLTVEQLKKIYSGEITNWKEVGGdlPNKPIVVVGRNAGSGTR 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308193616   78 ATFEKWGLDGATPVQSQ-EQDSSGTVRQLVSQTPGAISYLAFSYLDDSTQALSIDGVEPKEENVADNSWGIWSYEHMYTN 156
Cdd:TIGR02136 174 DTFEEEVMGKAKIKPGKnEQESNGAVVSIVSSNPGAIGYLGLGYVDDSVKTLKVNGVEPSKENIANGSYPLSRPLFMYVN 253

                         170       180       190
                  ....*....|....*....|....*....|....
gi 308193616  157 GKPS--PEVQKFLDYMMTEEIQEGPVKELGYLPI 188
Cdd:TIGR02136 254 GKPKkpELVAEFIDFVLSDDGGERIVEELGYVPL 287
PBP2_phosphate_like_1 cd13653
Substrate binding domain of putative ABC-type phosphate transporter, a member of the type 2 ...
 5-177 3.68e-68

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: 207.81  E-value: 3.68e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308193616   5 AEERDgvDASKLVDHKVAVVGMAPIVNKDTDVKDITKQELIDIFTGKITNWKEVGGKDQKINVVNRANGSGTRATFEKWG 84
Cdd:cd13653   62 AEEKA--AASGLVEHVIALDGIAIIVNPDNPVKNLTLEQLRDIFSGKITNWKEVGGPDGPIVVISREEGSGTRETFEELV 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308193616  85 LDGATPV-QSQEQDSSGTVRQLVSQTPGAISYLAFSYLDDST-QALSIDGVEPKEENVADNSWGIWSYEHMYTNGKPSPE 162
Cdd:cd13653  140 LGKKDFAkNAVVVPSNGAVVQAVAKNPNAIGYVSLGYVDDSKvKALSVDGVAPTPENIKSGKYPLSRPLYLYTKGEPSGL 219

                        170
                 ....*....|....*
gi 308193616 163 VQKFLDYMMTEEIQE 177
Cdd:cd13653  220 VKAFIDFALSPEGQA 234
PstS COG0226
ABC-type phosphate transport system, periplasmic component [Inorganic ion transport and ...
 15-189 1.26e-60

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


Pssm-ID: 439996 [Multi-domain]  Cd Length: 275  Bit Score: 189.71  E-value: 1.26e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308193616  15 KLVDHKVAVVGMAPIVNKDTDVKDITKQELIDIFTGKITNWKEVGGK--DQKINVVNRANGSGTRATFEKWGLDGATPV- 91
Cdd:COG0226   76 ELVEIPVAIDGIAVVVNPDNPVKNLTGEQLADIFSGKITNWNDIGGKlpDEPITVVGRSDGSGTTDYFTEYLLGVGAEVr 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308193616  92 -QSQEQDSSGTVRQLVSQTPGAISYLAFSYLDDST-QALSID-----GVEPKEENVADNSWGIWSYEHMYTNGKP---SP 161
Cdd:COG0226  156 eGVEGAEGNEGVVQAVAQTPGAIGYVGLSYAEQNKlKALAIDnkagkFVEPTAENIAAGSYPLSRPLYIYVKKEPdakAP 235

                        170       180
                 ....*....|....*....|....*...
gi 308193616 162 EVQKFLDYMMTEEIQEgPVKELGYLPIT 189
Cdd:COG0226  236 AVKAFLDFVLSDGGQK-IVEKLGYVPLP 262
PBP_like_2 pfam12849
PBP superfamily domain; This domain belongs to the periplasmic binding protein superfamily.
 1-174 1.95e-21

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


Pssm-ID: 432831 [Multi-domain]  Cd Length: 267  Bit Score: 88.37  E-value: 1.95e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308193616    1 SDVFAEERDGVDASK----LVDHKVAVVGMAPIVNKDTDVKDITKQELIDIFTGKITNWKEvGGKDQKINVVNRANGSGT 76
Cdd:pfam12849  65 SRPLTEEEFEAFGANgaggLVEVPVAYDGIAIVVNKDNPANILTVEALKKIFSGKITNWND-GGPDGPIKFVSRGDNSGT 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308193616   77 RATFEKWGLDGATPVQSQEQDSSGTVRQLVSQTPGAISYLAFSYLDDST-------------------QALSIDG----V 133
Cdd:pfam12849 144 TELFSTHLKEKGPWGAAGIGAAGSPGVASVVAGPGAIGYVEVSYALANLgytladvaggtylsfakalKVAKINPgaglV 223

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 308193616  134 EPKEENVADNSWGIWSYEHMYTNGK---PSPEVQKFLDYMMTEE 174
Cdd:pfam12849 224 IPLEEAIADGDYPLSRPYYVIVKNPpkgPAPLAKAFLDFLLSDE 267
PRK10918 PRK10918
phosphate ABC transporter substrate-binding protein PstS;
46-149 2.57e-06

phosphate ABC transporter substrate-binding protein PstS;


Pssm-ID: 182837  Cd Length: 346  Bit Score: 46.74  E-value: 2.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308193616  46 DIFTGKITNWKE---------VGGKDQKINVVNRANGSGTRATFEKWgLDGATPVQSQEQDSSGTVR------------- 103
Cdd:PRK10918 127 DIYLGKIKKWNDeaiaklnpgVKLPSQNIAVVRRADGSGTSFVFTSY-LAKVNEEWKSKVGAGSTVNwptglggkgndgi 205

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 308193616 104 -QLVSQTPGAISYLAFSYLDDS----TQALSIDG--VEPKEENVADNSWGI-WS 149
Cdd:PRK10918 206 aAFVQRLPGAIGYVEYAYAKQNnlayTKLISADGkpVSPTEESFSNAAKGAdWS 259
 
Name Accession Description Interval E-value
ptsS_2 TIGR02136
phosphate binding protein; Members of this family are phosphate-binding proteins. Most are ...
 3-188 4.72e-73

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: 221.93  E-value: 4.72e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308193616    3 VFAEE--RDGVDASKLVDHKVAVVGMAPIVN-KDTDVKDITKQELIDIFTGKITNWKEVGG--KDQKINVVNRANGSGTR 77
Cdd:TIGR02136  94 IKDEElqKDKQKGIKLIEHKVAVDGLAVVVNkKNVPVDDLTVEQLKKIYSGEITNWKEVGGdlPNKPIVVVGRNAGSGTR 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308193616   78 ATFEKWGLDGATPVQSQ-EQDSSGTVRQLVSQTPGAISYLAFSYLDDSTQALSIDGVEPKEENVADNSWGIWSYEHMYTN 156
Cdd:TIGR02136 174 DTFEEEVMGKAKIKPGKnEQESNGAVVSIVSSNPGAIGYLGLGYVDDSVKTLKVNGVEPSKENIANGSYPLSRPLFMYVN 253

                         170       180       190
                  ....*....|....*....|....*....|....
gi 308193616  157 GKPS--PEVQKFLDYMMTEEIQEGPVKELGYLPI 188
Cdd:TIGR02136 254 GKPKkpELVAEFIDFVLSDDGGERIVEELGYVPL 287
PBP2_phosphate_like_1 cd13653
Substrate binding domain of putative ABC-type phosphate transporter, a member of the type 2 ...
 5-177 3.68e-68

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: 207.81  E-value: 3.68e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308193616   5 AEERDgvDASKLVDHKVAVVGMAPIVNKDTDVKDITKQELIDIFTGKITNWKEVGGKDQKINVVNRANGSGTRATFEKWG 84
Cdd:cd13653   62 AEEKA--AASGLVEHVIALDGIAIIVNPDNPVKNLTLEQLRDIFSGKITNWKEVGGPDGPIVVISREEGSGTRETFEELV 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308193616  85 LDGATPV-QSQEQDSSGTVRQLVSQTPGAISYLAFSYLDDST-QALSIDGVEPKEENVADNSWGIWSYEHMYTNGKPSPE 162
Cdd:cd13653  140 LGKKDFAkNAVVVPSNGAVVQAVAKNPNAIGYVSLGYVDDSKvKALSVDGVAPTPENIKSGKYPLSRPLYLYTKGEPSGL 219

                        170
                 ....*....|....*
gi 308193616 163 VQKFLDYMMTEEIQE 177
Cdd:cd13653  220 VKAFIDFALSPEGQA 234
PstS COG0226
ABC-type phosphate transport system, periplasmic component [Inorganic ion transport and ...
 15-189 1.26e-60

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


Pssm-ID: 439996 [Multi-domain]  Cd Length: 275  Bit Score: 189.71  E-value: 1.26e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308193616  15 KLVDHKVAVVGMAPIVNKDTDVKDITKQELIDIFTGKITNWKEVGGK--DQKINVVNRANGSGTRATFEKWGLDGATPV- 91
Cdd:COG0226   76 ELVEIPVAIDGIAVVVNPDNPVKNLTGEQLADIFSGKITNWNDIGGKlpDEPITVVGRSDGSGTTDYFTEYLLGVGAEVr 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308193616  92 -QSQEQDSSGTVRQLVSQTPGAISYLAFSYLDDST-QALSID-----GVEPKEENVADNSWGIWSYEHMYTNGKP---SP 161
Cdd:COG0226  156 eGVEGAEGNEGVVQAVAQTPGAIGYVGLSYAEQNKlKALAIDnkagkFVEPTAENIAAGSYPLSRPLYIYVKKEPdakAP 235

                        170       180
                 ....*....|....*....|....*...
gi 308193616 162 EVQKFLDYMMTEEIQEgPVKELGYLPIT 189
Cdd:COG0226  236 AVKAFLDFVLSDGGQK-IVEKLGYVPLP 262
PBP2_phosphate cd13566
Substrate binding domain of putative ABC-type phosphate transporter, a member of the type 2 ...
 14-177 3.03e-60

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: 187.79  E-value: 3.03e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308193616  14 SKLVDHKVAVVGMAPIVNKDTDVKDITKQELIDIFTGKITNWKEVGGKDQKINVVNRANGSGTRATFEKW-GLDGATPVQ 92
Cdd:cd13566   73 IELVEFVIAYDGIAVIVNPDNPVASLTLEQLRDIFTGKITNWSEVGGPDEPIVVYGRDEGSGTRDYFEELvLGKGEFIRN 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308193616  93 SQEQDSSGTVRQLVSQTPGAISYLAFSYLDDSTQ--ALSIDGVEPKEENVADNSWGIWSYEHMYTNGKPSPEVQKFLDYM 170
Cdd:cd13566  153 AVVAPSNGALVQAVAGDPNAIGYVGLGYVDENKKvkALKVDGVAPTVENIKSGKYPLSRPLFLYTKGEPSPAVKAFIDFA 232


                 ....*..
gi 308193616 171 MTEEIQE 177
Cdd:cd13566  233 LSPEGQK 239
PBP_like_2 pfam12849
PBP superfamily domain; This domain belongs to the periplasmic binding protein superfamily.
 1-174 1.95e-21

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


Pssm-ID: 432831 [Multi-domain]  Cd Length: 267  Bit Score: 88.37  E-value: 1.95e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308193616    1 SDVFAEERDGVDASK----LVDHKVAVVGMAPIVNKDTDVKDITKQELIDIFTGKITNWKEvGGKDQKINVVNRANGSGT 76
Cdd:pfam12849  65 SRPLTEEEFEAFGANgaggLVEVPVAYDGIAIVVNKDNPANILTVEALKKIFSGKITNWND-GGPDGPIKFVSRGDNSGT 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308193616   77 RATFEKWGLDGATPVQSQEQDSSGTVRQLVSQTPGAISYLAFSYLDDST-------------------QALSIDG----V 133
Cdd:pfam12849 144 TELFSTHLKEKGPWGAAGIGAAGSPGVASVVAGPGAIGYVEVSYALANLgytladvaggtylsfakalKVAKINPgaglV 223

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 308193616  134 EPKEENVADNSWGIWSYEHMYTNGK---PSPEVQKFLDYMMTEE 174
Cdd:pfam12849 224 IPLEEAIADGDYPLSRPYYVIVKNPpkgPAPLAKAFLDFLLSDE 267
PBP2_phosphate_like_2 cd13654
Substrate binding domain of putative ABC-type phosphate transporter, a member of the type 2 ...
 20-174 3.80e-13

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: 65.74  E-value: 3.80e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308193616  20 KVAVVGMAPIVNKDTD-VKDITKQELIDI--FTGKITNWKEVGGK--DQKINVVNRANGSGTRATFEKWGLDGATPVQS- 93
Cdd:cd13654   79 PVAYDGLTVVVNPANDwAKCLTELELKSIwaAESPITTWSDVRPSwpDEPIELYGPGTDSGTFDYFTEAIVGEGGSIREd 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308193616  94 ---QEQDSsgTVRQLVSQTPGAISYLAFSYLD---DSTQALSIDG----VEPKEENVADN-----SWGIWSY---EHMYT 155
Cdd:cd13654  159 ytaSEDDN--VLVQGVAGDKNALGFFGYAYYEengDKLKAVKIDGgegtVAPSAETTISGgyyplSRPLFIYvkkASLAE 236

                        170
                 ....*....|....*....
gi 308193616 156 NgkpsPEVQKFLDYMMTEE 174
Cdd:cd13654  237 K----PAVAAFVKFYLENA 251
PBP2_PstS cd13565
Substrate binding domain of ABC-type phosphate transporter, a member of the type 2 ...
 23-177 8.77e-12

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: 61.86  E-value: 8.77e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308193616  23 VVGM-APIVNKD--TDVKDITKQELIDIFTGKITNWKEVGGK---------DQKINVVNRANGSGT-------------- 76
Cdd:cd13565   78 VIGAvVVAYNLPgvKGLLLLSGEVLADIFLGKITKWNDPAIAalnpgvnlpDTPITVVHRSDGSGTtfiftdylsavspe 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308193616  77 -RATFEKWGLDgATPVQSQEQDSSGtVRQLVSQTPGAISYLAFSYLDDstQALSIDGVEPkeenvadnsWGIWSYEHMYT 155
Cdd:cd13565  158 wKDKVGAGKSV-AWPVGLGGKGNEG-VAAAVKQTPGSIGYVELSYALQ--NGLPAAALYP---------IVGFTYILVKK 224

                        170       180
                 ....*....|....*....|....*
gi 308193616 156 NGKPSP---EVQKFLDYMMTEEIQE 177
Cdd:cd13565  225 DYKDAEkakAVKKFLKWALTEGQKF 249
PBP2_phosphate_binding cd01006
Substrate binding domain of ABC-type phosphate transporter, a member of the type 2 ...
 1-173 1.04e-11

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: 61.51  E-value: 1.04e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308193616   1 SDVFAEERDgVDASKLVDHKVAVVGMAPIVNKDTDVKDIT--KQELIDIFTGKITNWKEVG---------GKDQKINVVN 69
Cdd:cd01006   56 SDAYLSESE-AANKGLHTFTLAIDGLAIVVNQPGPVTNLTlnGKQLYGIYKGQIKNWDDVGiaalnpgvnLPDQKIAVVT 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308193616  70 RANGSGTRATF---------EKWGLDG-----ATPVQSQEQDSSGTVrQLVSQTPGAISYLAFSYLDDSTQAlsidgvep 135
Cdd:cd01006  135 REDGSGTRFSFtsylgktktEKDGKGTtevsdVAPTALGVNGNSG*K-TLVNHNPGAVGYISIGSVDQSSLK-------- 205

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 308193616 136 keenvADNSWGIWSYE---HMYTNGKPSP--EVQKFLDYMMTE 173
Cdd:cd01006  206 -----AIQLYPISRPFlilHYSDQKDAATdeQTKEFIAWAKSE 243
3a0107s03 TIGR00975
phosphate ABC transporter, phosphate-binding protein; This family represents one type of ...
 44-188 2.65e-09

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: 55.14  E-value: 2.65e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308193616   44 LIDIFTGKITNW---------KEVGGKDQKINVVNRANGSGTRATFEK--------WGLD---GAT---PVQSQEQDSSG 100
Cdd:TIGR00975  99 LAKIFLGKIKQWndpaiaalnPGVKLPGTAITVVHRSDGSGTTFNFTNylskvspeWGKKvgaGKTvqwPAGVGGKGNDG 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308193616  101 TVrQLVSQTPGAISYLAFSYL--------------------DDSTQALSIDGV---EPKEENV------ADNSWGIWSYE 151
Cdd:TIGR00975 179 VV-AGVKQTPGAIGYVEWSFAkqnklsfaalknsagkfvlpDAESIKAAAAGAkisTPKNDAIsmtdppGPGAYPIVSYT 257

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 308193616  152 HMYTNGK-PSPE----VQKFLDYMMTEEIQEgpVKELGYLPI 188
Cdd:TIGR00975 258 YLIVYKKqKDPAkakaLKAFLTWAITNGQSF--LDDLGYIPL 297
PRK10918 PRK10918
phosphate ABC transporter substrate-binding protein PstS;
46-149 2.57e-06

phosphate ABC transporter substrate-binding protein PstS;


Pssm-ID: 182837  Cd Length: 346  Bit Score: 46.74  E-value: 2.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308193616  46 DIFTGKITNWKE---------VGGKDQKINVVNRANGSGTRATFEKWgLDGATPVQSQEQDSSGTVR------------- 103
Cdd:PRK10918 127 DIYLGKIKKWNDeaiaklnpgVKLPSQNIAVVRRADGSGTSFVFTSY-LAKVNEEWKSKVGAGSTVNwptglggkgndgi 205

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 308193616 104 -QLVSQTPGAISYLAFSYLDDS----TQALSIDG--VEPKEENVADNSWGI-WS 149
Cdd:PRK10918 206 aAFVQRLPGAIGYVEYAYAKQNnlayTKLISADGkpVSPTEESFSNAAKGAdWS 259
PBP_like pfam12727
PBP superfamily domain; This family belongs to the periplasmic binding domain superfamily. It ...
 51-170 1.63e-05

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: 43.33  E-value: 1.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308193616   51 KITNWKEVGgkDQKINVVNRANGSGTRATFEKW----GLDGAT-PVQSQEQDSSGTVRQLVSQTPGAIsylafsylddst 125
Cdd:pfam12727  82 GITGWEDLA--RPGLRFVNRQRGSGTRVLLDELlrkaGIDPSDiNGYDREERSHLAVAAAVASGRADA------------ 147

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 308193616  126 qALSIDGVEPKEENVADNSWGIWSYEHMYT-NGKPSPEVQKFLDYM 170
Cdd:pfam12727 148 -GLGIEAAARALGGLDFIPLARERYDLVIPkEALDDPAVQALLEVL 192
SBP_bac_11 pfam13531
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 51-177 7.70e-03

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


Pssm-ID: 463911 [Multi-domain]  Cd Length: 225  Bit Score: 36.09  E-value: 7.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308193616   51 KITNWKEVGGKDQKINVVN-RANGSG--TRATFEKWGLDGAtpVQSQEQDSSGTVRQLVS-----QTPGAISYLafSYLD 122
Cdd:pfam13531  91 DISGLADLLKPGVRLAVADpKTAPSGraALELLEKAGLLKA--LEKKVVVLGENVRQALTavasgEADAGIVYL--SEAL 166

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 308193616  123 DSTQALSIDGVEPKEE--NVADNSWGIWsyehmyTNGKPSPEVQKFLDYMMTEEIQE 177
Cdd:pfam13531 167 FPENGPGLEVVPLPEDlnLPLDYPAAVL------KKAAHPEAARAFLDFLLSPEAQA 217
 
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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