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Conserved domains on  [gi|15599354|ref|NP_252848|]
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iron-enterobactin transporter periplasmic binding protein [Pseudomonas aeruginosa PAO1]

Protein Classification

Fe2+-enterobactin ABC transporter substrate-binding protein( domain architecture ID 11485126)

Fe2+-enterobactin ABC transporter substrate-binding protein similar to Escherichia coli ferric enterobactin binding protein FepB that plays a key role in transporting the catecholate siderophore ferric enterobactin from the outer to the inner membrane in Gram-negative bacteria

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
PRK10957 PRK10957
iron-enterobactin transporter periplasmic binding protein; Provisional
27-301 1.83e-154

iron-enterobactin transporter periplasmic binding protein; Provisional


:

Pssm-ID: 236806 [Multi-domain]  Cd Length: 317  Bit Score: 434.40  E-value: 1.83e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599354   27 EPKPARIVSTTPSVTGILLAMDAPLVASAATTP-SRLTDAKGFFSQWAKVADQRGVEVLYrNLRFDIEAVIAQDPDLLVA 105
Cdd:PRK10957  41 ESKPQRIVSTSVTLTGTLLAIDAPVIASGATTPnTRVADDQGFFRQWSDVAKERGVEVLY-IGEPDAEAVAAQMPDLIVI 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599354  106 SATGADSAAPYRAELEAQGvPTLVVDYSKHSWQELATELGRHTGLERQAQAAIQRFDAYTAEVAAAIAPPQGPVSVVGYN 185
Cdd:PRK10957 120 SATGGDSALALYDQLSAIA-PTLVIDYDDKSWQELATQLGEATGLEKQAAAVIAQFDAQLAEVKAKITLPPQPVSALVYN 198
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599354  186 IAG-SYSIGRQASPQARLLEALGFQVAELPEALAGKVT--RASDFQFISRENLPAAIAGDSVFLLGASDDDVQAFLADPV 262
Cdd:PRK10957 199 GAGhSANLWTPESAQGQLLEQLGFTLAELPAGLQASTSqgKRHDIIQLGGENLAAGLNGETLFLFAGDDKDADAFLADPL 278
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 15599354  263 LANLSAVREKRVYALGPSSFRIDYYSGRQMIDNVARHFR 301
Cdd:PRK10957 279 LANLPAVQNKQVYALGTDTFRLDYYSATQLLDRLAALFG 317
 
Name Accession Description Interval E-value
PRK10957 PRK10957
iron-enterobactin transporter periplasmic binding protein; Provisional
27-301 1.83e-154

iron-enterobactin transporter periplasmic binding protein; Provisional


Pssm-ID: 236806 [Multi-domain]  Cd Length: 317  Bit Score: 434.40  E-value: 1.83e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599354   27 EPKPARIVSTTPSVTGILLAMDAPLVASAATTP-SRLTDAKGFFSQWAKVADQRGVEVLYrNLRFDIEAVIAQDPDLLVA 105
Cdd:PRK10957  41 ESKPQRIVSTSVTLTGTLLAIDAPVIASGATTPnTRVADDQGFFRQWSDVAKERGVEVLY-IGEPDAEAVAAQMPDLIVI 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599354  106 SATGADSAAPYRAELEAQGvPTLVVDYSKHSWQELATELGRHTGLERQAQAAIQRFDAYTAEVAAAIAPPQGPVSVVGYN 185
Cdd:PRK10957 120 SATGGDSALALYDQLSAIA-PTLVIDYDDKSWQELATQLGEATGLEKQAAAVIAQFDAQLAEVKAKITLPPQPVSALVYN 198
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599354  186 IAG-SYSIGRQASPQARLLEALGFQVAELPEALAGKVT--RASDFQFISRENLPAAIAGDSVFLLGASDDDVQAFLADPV 262
Cdd:PRK10957 199 GAGhSANLWTPESAQGQLLEQLGFTLAELPAGLQASTSqgKRHDIIQLGGENLAAGLNGETLFLFAGDDKDADAFLADPL 278
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 15599354  263 LANLSAVREKRVYALGPSSFRIDYYSGRQMIDNVARHFR 301
Cdd:PRK10957 279 LANLPAVQNKQVYALGTDTFRLDYYSATQLLDRLAALFG 317
FepB COG4592
ABC-type Fe2+-enterobactin transport system, periplasmic component [Inorganic ion transport ...
27-301 2.74e-123

ABC-type Fe2+-enterobactin transport system, periplasmic component [Inorganic ion transport and metabolism];


Pssm-ID: 443649 [Multi-domain]  Cd Length: 330  Bit Score: 355.79  E-value: 2.74e-123
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599354  27 EPKPARIVSTTPSVTGILLAMDAPLVASAATTPSRLTDAKGFFSQWAKVADQRGVEVLYRNLRFDIEAVIAQDPDLLVAS 106
Cdd:COG4592  54 PAKPQRIVSTSVTLTGSLLAIDAPVVASGATTPNNVTDDQGFFRQWADVAKERGVKRLYIGLEPNAEAIAAAAPDLIIGS 133
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599354 107 ATGADSAAPYRAELEAQgVPTLVVDYSKHSWQELATELGRHTGLERQAQAAIQRFDAYTAEVAAAIAPPQGPVSVVGYNI 186
Cdd:COG4592 134 ATGGDSALDLYDQLSAI-APTLVVNYDDKSWQELATQLGEATGHEAQADAVIAAFDARVAEVKAAITLPPQPVSALVYNE 212
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599354 187 AGSYSIGRQASPQARLLEALGFQVAELPEALAGKVTR--ASDFQFISRENLPAAIAGDSVFLLGASDDDVQAFLADPVLA 264
Cdd:COG4592 213 DGGANLWTPESAQGQLLQALGFTLAPLPAELATSTSQgkRGDIVQLSGENLAAALTGPTLFLFAADDKDVDALKADPLLA 292
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 15599354 265 NLSAVREKRVYALGPSSFRIDYYSGRQMIDNVARHFR 301
Cdd:COG4592 293 HLPAVQAGRVYALGPDSFRLDYYSASNLLDRLEKLFG 329
FhuD cd01146
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ...
29-294 1.17e-52

Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial receptors in ABC transport of Fe3+-siderophores in many eubacterial species. They belong to the TroA-like superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA-like protein is comprised of two globular subdomains connected by a long alpha helix and binds its specific ligands in the cleft between these domains.


Pssm-ID: 238566 [Multi-domain]  Cd Length: 256  Bit Score: 172.86  E-value: 1.17e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599354  29 KPARIVSTTPSVTGILLAMDAPLVASAATtpsrltdakGFFSQWAKVADQRGVEVLYRNLR--FDIEAVIAQDPDLLVAS 106
Cdd:cd01146   2 KPQRIVALDWGALETLLALGVKPVGVADT---------AGYKPWIPEPALPLEGVVDVGTRgqPNLEAIAALKPDLILGS 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599354 107 ATGADsaAPYraELEAQGVPTLVVDYSKH--SWQELATELGRHTGLERQAQAAIQRFDAYTAEVAAAIAPPQG-PVSVVG 183
Cdd:cd01146  73 ASRHD--EIY--DQLSQIAPTVLLDSSPWlaEWKENLRLIAKALGKEEEAEKLLAEYDQRLAELRQKLPDKGPkPVSVVR 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599354 184 YNIAGSYSIGRQASPQARLLEALGFQVAELPEAlagkvTRASDFQFISRENLPAAiAGDSVFLLGASDDD-VQAFLADPV 262
Cdd:cd01146 149 FSDAGSIRLYGPNSFAGSVLEDLGLQNPWAQET-----TNDSGFATISLERLAKA-DADVLFVFTYEDEElAQALQANPL 222
                       250       260       270
                ....*....|....*....|....*....|...
gi 15599354 263 LANLSAVREKRVYALGPS-SFRIDYYSGRQMID 294
Cdd:cd01146 223 WQNLPAVKNGRVYVVDDVwWFFGGGLSAARLLL 255
Peripla_BP_2 pfam01497
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ...
34-280 3.38e-19

Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding proteins, several of which are involved in iron and cobalamin transport. Among its ligands are siderophores bacillibactin, enterobactin and iron(III)-hydroxamates (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1 https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 426291 [Multi-domain]  Cd Length: 233  Bit Score: 84.34  E-value: 3.38e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599354    34 VSTTPSVTGILLAMDA--PLVASAATTpsrltdakgfFSQWAKVADQRGVEVLYRNlRFDIEAVIAQDPDLLVASATGAD 111
Cdd:pfam01497   1 AALSPAYTEILYALGAtdSIVGVDAYT----------RDPLKADAVAAIVKVGAYG-EINVERLAALKPDLVILSTGYLT 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599354   112 SAAPyraELEAQGVPTLVVDYSKH--SWQELATELGRHTGLERQAQAAIQRFDAYTAEVAAAIAP-PQGPVSVVGYNIAG 188
Cdd:pfam01497  70 DEAE---ELLSLIIPTVIFESSSTgeSLKEQIKQLGELLGLEDEAEELVAEIDSALAAAKKAVPSlTRKPVLVFGGADGG 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599354   189 SYSI-GRQASPQArLLEALGFQvaelpEALAGKVTraSDFQFISRENLpAAIAGDSVFLLGASDD---DVQAFLADPVLA 264
Cdd:pfam01497 147 GYVVaGSNTYIGD-LLRILGIE-----NIAAELSG--SEYAPISFEAI-LSSNPDVIIVSGRDSFtktGPEFVAANPLWA 217
                         250
                  ....*....|....*.
gi 15599354   265 NLSAVREKRVYALGPS 280
Cdd:pfam01497 218 GLPAVKNGRVYTLPSD 233
 
Name Accession Description Interval E-value
PRK10957 PRK10957
iron-enterobactin transporter periplasmic binding protein; Provisional
27-301 1.83e-154

iron-enterobactin transporter periplasmic binding protein; Provisional


Pssm-ID: 236806 [Multi-domain]  Cd Length: 317  Bit Score: 434.40  E-value: 1.83e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599354   27 EPKPARIVSTTPSVTGILLAMDAPLVASAATTP-SRLTDAKGFFSQWAKVADQRGVEVLYrNLRFDIEAVIAQDPDLLVA 105
Cdd:PRK10957  41 ESKPQRIVSTSVTLTGTLLAIDAPVIASGATTPnTRVADDQGFFRQWSDVAKERGVEVLY-IGEPDAEAVAAQMPDLIVI 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599354  106 SATGADSAAPYRAELEAQGvPTLVVDYSKHSWQELATELGRHTGLERQAQAAIQRFDAYTAEVAAAIAPPQGPVSVVGYN 185
Cdd:PRK10957 120 SATGGDSALALYDQLSAIA-PTLVIDYDDKSWQELATQLGEATGLEKQAAAVIAQFDAQLAEVKAKITLPPQPVSALVYN 198
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599354  186 IAG-SYSIGRQASPQARLLEALGFQVAELPEALAGKVT--RASDFQFISRENLPAAIAGDSVFLLGASDDDVQAFLADPV 262
Cdd:PRK10957 199 GAGhSANLWTPESAQGQLLEQLGFTLAELPAGLQASTSqgKRHDIIQLGGENLAAGLNGETLFLFAGDDKDADAFLADPL 278
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 15599354  263 LANLSAVREKRVYALGPSSFRIDYYSGRQMIDNVARHFR 301
Cdd:PRK10957 279 LANLPAVQNKQVYALGTDTFRLDYYSATQLLDRLAALFG 317
FepB COG4592
ABC-type Fe2+-enterobactin transport system, periplasmic component [Inorganic ion transport ...
27-301 2.74e-123

ABC-type Fe2+-enterobactin transport system, periplasmic component [Inorganic ion transport and metabolism];


Pssm-ID: 443649 [Multi-domain]  Cd Length: 330  Bit Score: 355.79  E-value: 2.74e-123
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599354  27 EPKPARIVSTTPSVTGILLAMDAPLVASAATTPSRLTDAKGFFSQWAKVADQRGVEVLYRNLRFDIEAVIAQDPDLLVAS 106
Cdd:COG4592  54 PAKPQRIVSTSVTLTGSLLAIDAPVVASGATTPNNVTDDQGFFRQWADVAKERGVKRLYIGLEPNAEAIAAAAPDLIIGS 133
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599354 107 ATGADSAAPYRAELEAQgVPTLVVDYSKHSWQELATELGRHTGLERQAQAAIQRFDAYTAEVAAAIAPPQGPVSVVGYNI 186
Cdd:COG4592 134 ATGGDSALDLYDQLSAI-APTLVVNYDDKSWQELATQLGEATGHEAQADAVIAAFDARVAEVKAAITLPPQPVSALVYNE 212
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599354 187 AGSYSIGRQASPQARLLEALGFQVAELPEALAGKVTR--ASDFQFISRENLPAAIAGDSVFLLGASDDDVQAFLADPVLA 264
Cdd:COG4592 213 DGGANLWTPESAQGQLLQALGFTLAPLPAELATSTSQgkRGDIVQLSGENLAAALTGPTLFLFAADDKDVDALKADPLLA 292
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 15599354 265 NLSAVREKRVYALGPSSFRIDYYSGRQMIDNVARHFR 301
Cdd:COG4592 293 HLPAVQAGRVYALGPDSFRLDYYSASNLLDRLEKLFG 329
FhuD cd01146
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ...
29-294 1.17e-52

Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial receptors in ABC transport of Fe3+-siderophores in many eubacterial species. They belong to the TroA-like superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA-like protein is comprised of two globular subdomains connected by a long alpha helix and binds its specific ligands in the cleft between these domains.


Pssm-ID: 238566 [Multi-domain]  Cd Length: 256  Bit Score: 172.86  E-value: 1.17e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599354  29 KPARIVSTTPSVTGILLAMDAPLVASAATtpsrltdakGFFSQWAKVADQRGVEVLYRNLR--FDIEAVIAQDPDLLVAS 106
Cdd:cd01146   2 KPQRIVALDWGALETLLALGVKPVGVADT---------AGYKPWIPEPALPLEGVVDVGTRgqPNLEAIAALKPDLILGS 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599354 107 ATGADsaAPYraELEAQGVPTLVVDYSKH--SWQELATELGRHTGLERQAQAAIQRFDAYTAEVAAAIAPPQG-PVSVVG 183
Cdd:cd01146  73 ASRHD--EIY--DQLSQIAPTVLLDSSPWlaEWKENLRLIAKALGKEEEAEKLLAEYDQRLAELRQKLPDKGPkPVSVVR 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599354 184 YNIAGSYSIGRQASPQARLLEALGFQVAELPEAlagkvTRASDFQFISRENLPAAiAGDSVFLLGASDDD-VQAFLADPV 262
Cdd:cd01146 149 FSDAGSIRLYGPNSFAGSVLEDLGLQNPWAQET-----TNDSGFATISLERLAKA-DADVLFVFTYEDEElAQALQANPL 222
                       250       260       270
                ....*....|....*....|....*....|...
gi 15599354 263 LANLSAVREKRVYALGPS-SFRIDYYSGRQMID 294
Cdd:cd01146 223 WQNLPAVKNGRVYVVDDVwWFFGGGLSAARLLL 255
FepB COG0614
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ...
32-282 2.23e-30

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


Pssm-ID: 440379 [Multi-domain]  Cd Length: 264  Bit Score: 115.10  E-value: 2.23e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599354  32 RIVSTTPSVTGILLAMDAP--LVAsaattpsrLTDAKGFFSQWAKVADqrgVEVLYRNLRFDIEAVIAQDPDLLVASATG 109
Cdd:COG0614   2 RIVSLSPSATELLLALGAGdrLVG--------VSDWGYCDYPELELKD---LPVVGGTGEPNLEAILALKPDLVLASSSG 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599354 110 ADSAApyRAELEAQGVPTLVVDY-SKHSWQELATELGRHTGLERQAQAAIQRFDAYTAEVAAAIAPPQGPVSVVGYNIAG 188
Cdd:COG0614  71 NDEED--YEQLEKIGIPVVVLDPrSLEDLYESIRLLGELLGREERAEALIAEYEARLAAVRARLAGAEERPTVLYEIWSG 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599354 189 S--YSIGRQaSPQARLLEALGF--QVAELPEAlagkvtrasdFQFISRENLPAA-----IAGDSVFLLGASDDDVQAFLA 259
Cdd:COG0614 149 DplYTAGGG-SFIGELLELAGGrnVAADLGGG----------YPEVSLEQVLALdpdviILSGGGYDAETAEEALEALLA 217
                       250       260
                ....*....|....*....|...
gi 15599354 260 DPVLANLSAVREKRVYALGPSSF 282
Cdd:COG0614 218 DPGWQSLPAVKNGRVYVVPGDLL 240
Peripla_BP_2 pfam01497
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ...
34-280 3.38e-19

Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding proteins, several of which are involved in iron and cobalamin transport. Among its ligands are siderophores bacillibactin, enterobactin and iron(III)-hydroxamates (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1 https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 426291 [Multi-domain]  Cd Length: 233  Bit Score: 84.34  E-value: 3.38e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599354    34 VSTTPSVTGILLAMDA--PLVASAATTpsrltdakgfFSQWAKVADQRGVEVLYRNlRFDIEAVIAQDPDLLVASATGAD 111
Cdd:pfam01497   1 AALSPAYTEILYALGAtdSIVGVDAYT----------RDPLKADAVAAIVKVGAYG-EINVERLAALKPDLVILSTGYLT 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599354   112 SAAPyraELEAQGVPTLVVDYSKH--SWQELATELGRHTGLERQAQAAIQRFDAYTAEVAAAIAP-PQGPVSVVGYNIAG 188
Cdd:pfam01497  70 DEAE---ELLSLIIPTVIFESSSTgeSLKEQIKQLGELLGLEDEAEELVAEIDSALAAAKKAVPSlTRKPVLVFGGADGG 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599354   189 SYSI-GRQASPQArLLEALGFQvaelpEALAGKVTraSDFQFISRENLpAAIAGDSVFLLGASDD---DVQAFLADPVLA 264
Cdd:pfam01497 147 GYVVaGSNTYIGD-LLRILGIE-----NIAAELSG--SEYAPISFEAI-LSSNPDVIIVSGRDSFtktGPEFVAANPLWA 217
                         250
                  ....*....|....*.
gi 15599354   265 NLSAVREKRVYALGPS 280
Cdd:pfam01497 218 GLPAVKNGRVYTLPSD 233
FeuA cd01138
Periplasmic binding protein FeuA. These proteins have predicted to function as initial ...
29-282 1.44e-18

Periplasmic binding protein FeuA. These proteins have predicted to function as initial receptors in ABC transport of metal ions in some eubacterial species. They belong to the TroA superfamily of periplasmic metal binding proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind their ligands in the cleft between these domains.


Pssm-ID: 238558 [Multi-domain]  Cd Length: 248  Bit Score: 82.77  E-value: 1.44e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599354  29 KPARIVSTTpSVTGILLAMDAPLVAsaattpsrlTDAKGFFSQWAKVADQRGVEVLyrNLRFDIEAVIAQDPDLLVASAT 108
Cdd:cd01138   8 KPKRIVALS-GETEGLALLGIKPVG---------AASIGGKNPYYKKKTLAKVVGI--VDEPNLEKVLELKPDLIIVSSK 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599354 109 GADSAAPYraeleAQGVPTLVVDYSKHSWQELATELGRHTGLERQAQAAIQRFDAYTAEVAAAIAPPQGPVSVVGyNIAG 188
Cdd:cd01138  76 QEENYEKL-----SKIAPTVPVSYNSSDWEEQLKEIGKLLNKEDEAEKWLADYKQKAKEAKEKIKKKLGNDKSVA-VLRG 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599354 189 S---YSIGRQASPQARLLEA-LGFQVAELPEALAGKVTRASdfqfISRENLPAaIAGDSVFLLGASDDDVQA-FLADPVL 263
Cdd:cd01138 150 RkqiYVFGEDGRGGGPILYAdLGLKAPEKVKEIEDKPGYAA----ISLEVLPE-FDADYIFLLFFTGPEAKAdFESLPIW 224
                       250
                ....*....|....*....
gi 15599354 264 ANLSAVREKRVYALGPSSF 282
Cdd:cd01138 225 KNLPAVKNNHVYIVDAWVF 243
FecB COG4594
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and ...
91-277 3.35e-15

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


Pssm-ID: 443650 [Multi-domain]  Cd Length: 316  Bit Score: 74.57  E-value: 3.35e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599354  91 DIEAVIAQDPDLLVASATGAdsaAPYRAELEaQGVPTLVVDYSKHSWQE---LATELGRHTGLERQAQAAIQRFDAYTAE 167
Cdd:COG4594 106 NLEAIAALKPDLIIADKSRH---EAIYDQLS-KIAPTVLFKSRNGDYQEnleSFKTIAKALGKEEEAEAVLADHDQRIAE 181
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599354 168 VAAAIAPPQGPVSV-VGYNIAGSYSIGRQASPQARLLEALGFQVAELPealaGKVTRaSDFQFISRENLPAaIAGDsVFL 246
Cdd:COG4594 182 AKAKLAAADKGKKVaVGQFRADGLRLYTPNSFAGSVLAALGFENPPKQ----SKDNG-YGYSEVSLEQLPA-LDPD-VLF 254
                       170       180       190
                ....*....|....*....|....*....|...
gi 15599354 247 LGASDDD--VQAFLADPVLANLSAVREKRVYAL 277
Cdd:COG4594 255 IATYDDPsiLKEWKNNPLWKNLKAVKNGRVYEV 287
TroA-like cd00636
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function ...
32-173 1.39e-14

Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function in the ABC transport of ferric siderophores and metal ions such as Mn2+, Fe3+, Cu2+ and/or Zn2+. Their ligand binding site is formed in the interface between two globular domains linked by a single helix. Many of these proteins also possess a low complexity region containing a metal-binding histidine-rich motif (repetitive HDH sequence). The TroA-like proteins differ in their fold and ligand-binding mechanism from the PBPI and PBPII proteins, but are structurally similar, however, to the beta-subunit of the nitrogenase molybdenum-iron protein MoFe. Most TroA-like proteins are encoded by ABC-type operons and appear to function as periplasmic components of ABC transporters in metal ion uptake.


Pssm-ID: 238347 [Multi-domain]  Cd Length: 148  Bit Score: 69.51  E-value: 1.39e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599354  32 RIVSTTPSVTGILLAMDAPLVASAATTPSrltdakgFFSQWAKVADQRGVEVLYRNlRFDIEAVIAQDPDLLVASATGAD 111
Cdd:cd00636   2 RVVALDPGATELLLALGGDDKPVGVADPS-------GYPPEAKALLEKVPDVGHGY-EPNLEKIAALKPDLIIANGSGLE 73
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15599354 112 saaPYRAELEAQGVPTLVVD----YSKHSWQELATELGRHTGLERQAQAAIQRFDAYTAEVAAAIA 173
Cdd:cd00636  74 ---AWLDKLSKIAIPVVVVDeaseLSLENIKESIRLIGKALGKEENAEELIAELDARLAELRAKLA 136
FatB cd01140
Siderophore binding protein FatB. These proteins have been shown to function as ABC-type ...
29-297 5.98e-13

Siderophore binding protein FatB. These proteins have been shown to function as ABC-type initial receptors in the siderophore-mediated iron uptake in some eubacterial species. They belong to the TroA superfamily of periplasmic metal binding proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind their ligands in the cleft between these domains.


Pssm-ID: 238560 [Multi-domain]  Cd Length: 270  Bit Score: 67.67  E-value: 5.98e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599354  29 KPARIVSTTPSVTGILLAMDAPLVA--SAATTPSRLTDAKGffsqwAKVADQRGV-EVlyrnlrfDIEAVIAQDPDLLVA 105
Cdd:cd01140  11 NPEKVVVFDVGALDTLDALGVKVVGvpKSSTLPEYLKKYKD-----DKYANVGTLfEP-------DLEAIAALKPDLIII 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599354 106 SATgadsAAPYRAELeAQGVPTLVVDY-SKHSWQEL---ATELGRHTGLERQAQAAIQRFDAYTAEVAAAiAPPQGPVSV 181
Cdd:cd01140  79 GGR----LAEKYDEL-KKIAPTIDLGAdLKNYLESVkqnIETLGKIFGKEEEAKELVAEIDASIAEAKSA-AKGKKKALV 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599354 182 VGYNiAGSYSIgrqASPQAR---LLEALGFqvaelpEALAGKVTRASDFQFISRENLpAAIAGDSVFLL------GASDD 252
Cdd:cd01140 153 VLVN-GGKLSA---FGPGSRfgwLHDLLGF------EPADENIKASSHGQPVSFEYI-LEANPDWLFVIdrgaaiGAEGS 221
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 15599354 253 DVQAFLADPVLANLSAVREKRVYALGPSSFridYYSG------RQMIDNVA 297
Cdd:cd01140 222 SAKEVLDNDLVKNTTAWKNGKVIYLDPDLW---YLSGggleslKQMIDDLK 269
ChuT COG4558
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism] ...
30-277 4.14e-12

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


Pssm-ID: 443619 [Multi-domain]  Cd Length: 285  Bit Score: 65.21  E-value: 4.14e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599354  30 PARIVSTTPSVTGILLAMDAP--LVA--SAATTPSRLTDAkgffsqwAKVADQRGVevlyrnlrfDIEAVIAQDPDLLVA 105
Cdd:COG4558  27 AERIVSLGGSVTEIVYALGAGdrLVGvdTTSTYPAAAKAL-------PDVGYMRQL---------SAEGILSLKPTLVLA 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599354 106 SAT-GADSAApyrAELEAQGVPTLVVDySKHSWQELA---TELGRHTGLERQAQAAIQRFDAYTAEVAAAIAPPQGPVSV 181
Cdd:COG4558  91 SEGaGPPEVL---DQLRAAGVPVVVVP-AAPSLEGVLakiRAVAAALGVPEAGEALAARLEADLAALAARVAAIGKPPRV 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599354 182 ---VGYNiAGSYSIGRQASPQARLLEALGFQVAelpealagkVTRASDFQFISRENLPAAiAGDSVFLL---GASDDDVQ 255
Cdd:COG4558 167 lflLSRG-GGRPMVAGRGTAADALIRLAGGVNA---------AAGFEGYKPLSAEALIAA-APDVILVMtrgLESLGGVD 235
                       250       260
                ....*....|....*....|..
gi 15599354 256 AFLADPVLANLSAVREKRVYAL 277
Cdd:COG4558 236 GLLALPGLAQTPAGKNKRIVAM 257
TroA_e cd01142
Periplasmic binding protein TroA_e. These proteins are predicted to function as initial ...
29-293 2.27e-10

Periplasmic binding protein TroA_e. These proteins are predicted to function as initial receptors in the ABC metal ion uptake in eubacteria and archaea. They belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind their ligands in the cleft between these domains.


Pssm-ID: 238562 [Multi-domain]  Cd Length: 289  Bit Score: 60.06  E-value: 2.27e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599354  29 KPARIVSTTPSVTGILLAMDAPLVASA-ATTPSRLTDAKGFFSQWAKVADQ-RGVEVLyrnlrfdIEAVIAQDPDLLVAS 106
Cdd:cd01142  23 EVKRIAALWGAGNAVVAALGGGKLIVAtTSTVQQEPWLYRLAPSLENVATGgTGNDVN-------IEELLALKPDVVIVW 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599354 107 ATgadsaapYRAELEAQGVPTLVVDYS----KHSWQELATELGRHTGLERQAQAAIQRFD---AYTAEVAAAIAPPQGPV 179
Cdd:cd01142  96 ST-------DGKEAGKAVLRLLNALSLrdaeLEEVKLTIALLGELLGRQEKAEALVAYFDdnlAYVAARTKKLPDSERPR 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599354 180 SVVGYNIAGSYSiGRQASPQARLLEALGFQVAElpeaLAGKVTRASdfqfISRENLpaaIAGDSVFLLGASDDDVQAFLA 259
Cdd:cd01142 169 VYYAGPDPLTTD-GTGSITNSWIDLAGGINVAS----EATKKGSGE----VSLEQL---LKWNPDVIIVGNADTKAAILA 236
                       250       260       270
                ....*....|....*....|....*....|....
gi 15599354 260 DPVLANLSAVREKRVYALGPSSFRIDYYSGRQMI 293
Cdd:cd01142 237 DPRWQNLRAVKNGRVYVNPEGAFWWDRPSAEEAL 270
YvrC cd01143
Periplasmic binding protein YvrC. These proteins are predicted to function as initial ...
29-193 1.20e-09

Periplasmic binding protein YvrC. These proteins are predicted to function as initial receptors in ABC transport of metal ions in eubacteria and archaea. They belong to the TroA superfamily of periplasmic metal binding proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind the metal ion in the cleft between these domains.


Pssm-ID: 238563 [Multi-domain]  Cd Length: 195  Bit Score: 56.90  E-value: 1.20e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599354  29 KPARIVSTTPSVTGILLAMDA--PLVASAATT--PSRLTDAKGFFSQWAkvadqrgvevlyrnlrFDIEAVIAQDPDLLV 104
Cdd:cd01143   2 EPERIVSLSPSITEILFALGAgdKIVGVDTYSnyPKEVRKKPKVGSYSN----------------PNVEKIVALKPDLVI 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599354 105 ASatgADSAAPYRAELEAQGVPTLVVDYSK--HSWQELATELGRHTGLERQAQAAIQRFDAYTAEVAAaiAPPQGPVSVV 182
Cdd:cd01143  66 VS---SSSLAELLEKLKDAGIPVVVLPAASslDEIYDQIELIGKITGAEEEAEKLVKEMKQKIDKVKD--KGKTIKKSKV 140
                       170
                ....*....|...
gi 15599354 183 GYNIA--GSYSIG 193
Cdd:cd01143 141 YIEVSlgGPYTAG 153
HutB cd01149
Hemin binding protein HutB. These proteins have been shown to function as initial receptors ...
30-277 1.60e-08

Hemin binding protein HutB. These proteins have been shown to function as initial receptors in ABC transport of hemin and hemoproteins in many eubacterial species. They belong to the TroA superfamily of periplasmic metal binding proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind the metal ion in the cleft between these domains.


Pssm-ID: 238569 [Multi-domain]  Cd Length: 235  Bit Score: 54.19  E-value: 1.60e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599354  30 PARIVSTTPSVTGILLAMDAP--LVA--SAATTPSRLTDAkgffsqwAKVADQRgvevlyrnlRFDIEAVIAQDPDLLVA 105
Cdd:cd01149   1 PERIVSLGGSVTEIVYALGAGdrLVGvdSTSTYPEAAAKL-------PDVGYMR---------QLSAEGVLSLKPTLVIA 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599354 106 SatgaDSAAPYRA--ELEAQGVPTLVV--DYSKHSWQELATELGRHTGLERQAQAAIQRFDAYTAEVAAAIAPPQGPVSV 181
Cdd:cd01149  65 S----DEAGPPEAldQLRAAGVPVVTVpsTPTLDGLLTKIRQVAQALGVPEKGEALAQEVRQRLAALRKTVAAHKKPPRV 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599354 182 VgyniagsYSIGRQASpqaRLLEALGFQVAELPEALAGKVTRA---SDFQFISRENLpAAIAGDSVFLLGASDD---DVQ 255
Cdd:cd01149 141 L-------FLLSHGGG---AAMAAGRNTAADAIIALAGAVNAAagfRGYKPLSAEAL-IAAQPDVILVMSRGLDavgGVD 209
                       250       260
                ....*....|....*....|..
gi 15599354 256 AFLADPVLANLSAVREKRVYAL 277
Cdd:cd01149 210 GLLKLPGLAQTPAGRNKRILAM 231
TroA_a cd01148
Metal binding protein TroA_a. These proteins are predicted to function as initial receptors ...
29-277 2.61e-08

Metal binding protein TroA_a. These proteins are predicted to function as initial receptors in ABC transport of metal ions in eubacteria. They belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind the metal ion in the cleft between these domains.


Pssm-ID: 238568 [Multi-domain]  Cd Length: 284  Bit Score: 53.88  E-value: 2.61e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599354  29 KPARIVSTTPSVTGILLAMDAP--LVASAATTPSRLTDAKgffsqwakvADQRGVEVL---YRNLrfdiEAVIAQDPDLL 103
Cdd:cd01148  17 APQRVVSNDQNTTEMMLALGLQdrMVGTAGIDNKDLPELK---------AKYDKVPELakkYPSK----ETVLAARPDLV 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599354 104 VAS-ATGADSAAPY-RAELEAQGVPTLV---------VDYS-KHSWQELATeLGRHTGLERQAQAAIQRFDAYTAEVAAA 171
Cdd:cd01148  84 FGGwSYGFDKGGLGtPDSLAELGIKTYIlpescgqrrGEATlDDVYNDIRN-LGKIFDVEDRADKLVADLKARLAEISAK 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599354 172 IAPPQGPVSVVGYNIA--GSYSIGRQASPQARLLEALGFQVAElpeALAGKVTRASDFQFISReNLPAAIAGDsvFLLGA 249
Cdd:cd01148 163 VKGDGKKVAVFVYDSGedKPFTSGRGGIPNAIITAAGGRNVFA---DVDESWTTVSWETVIAR-NPDVIVIID--YGDQN 236
                       250       260
                ....*....|....*....|....*....
gi 15599354 250 SDDDVQAFL-ADPVLANLSAVREKRVYAL 277
Cdd:cd01148 237 AAEQKIKFLkENPALKNVPAVKNNRFIVL 265
TroA_f cd01139
Periplasmic binding protein TroA_f. These proteins are predicted to function as initial ...
90-277 3.39e-07

Periplasmic binding protein TroA_f. These proteins are predicted to function as initial receptors in the ABC metal ion uptake in eubacteria and archaea. They belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind their ligands in the cleft between these domains.


Pssm-ID: 238559 [Multi-domain]  Cd Length: 342  Bit Score: 50.77  E-value: 3.39e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599354  90 FDIEAVIAQDPDLLVASATGADS--AAPYRAELEAQGVPTLVVDYS----KHSwQELATELGRHTGLERQAQAAIQRFDA 163
Cdd:cd01139  82 FSVEKVLTLKPDLVILNIWAKTTaeESGILEKLEQAGIPVVFVDFRqkplKNT-TPSMRLLGKALGREERAEEFIEFYQE 160
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599354 164 YTAEVAAAIAPPQGPVSVVGYNIAGSYS--IGRQASPQ--ARLLEALG-------FQVAELPEALAGKVTRAS-DFQFIS 231
Cdd:cd01139 161 RIDRIRDRLAKINEPKPKVFIELGAGGPeeCCSTYGNGnwGELVDAAGgdniadgLIPGTSGELNAEYVIAANpEIIIAT 240
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 15599354 232 RENLPAAIAGDSVFLLGASDDDVQAF----LADPVLANLSAVREKRVYAL 277
Cdd:cd01139 241 GGNWAKDPSGVSLGPDGTTADAKESLlralLKRPGWSSLQAVKNGRVYAL 290
HemV-2 cd01147
Metal binding protein HemV-2. These proteins are predicted to function as initial receptors ...
27-282 5.44e-07

Metal binding protein HemV-2. These proteins are predicted to function as initial receptors in ABC transport of metal ions. They belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind the metal ion in the cleft between these domains. In addition, these proteins sometimes have a low complexity region containing a metal-binding histidine-rich motif (repetitive HDH sequence).


Pssm-ID: 238567 [Multi-domain]  Cd Length: 262  Bit Score: 50.03  E-value: 5.44e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599354  27 EPKP-ARIVSTTPSVTGILLAMDAP--LVASAATTPSrlTDAKGFFSQWAKVADQRGVEVLYRNLRFDIEAVIAQDPDLL 103
Cdd:cd01147   1 VPKPvERVVAAGPGALRLLYALAAPdkIVGVDDAEKS--DEGRPYFLASPELKDLPVIGRGGRGNTPNYEKIAALKPDVV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599354 104 VASATGADSAAPYRAElEAQGVPTLVVDY--SKHSWQELATELGRHTGLERQAQAAIQRFDAYTAEV---AAAIAPPQGP 178
Cdd:cd01147  79 IDVGSDDPTSIADDLQ-KKTGIPVVVLDGgdSLEDTPEQIRLLGKVLGKEERAEELISFIESILADVeerTKDIPDEEKP 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599354 179 VSVVGY----NIAGSYSiGRQASPQARLLeALGFQVAELPEALAGKvtrasdfqFISRENLPAAiAGDSVFLLGASDDDV 254
Cdd:cd01147 158 TVYFGRigtkGAAGLES-GLAGSIEVFEL-AGGINVADGLGGGGLK--------EVSPEQILLW-NPDVIFLDTGSFYLS 226
                       250       260       270
                ....*....|....*....|....*....|
gi 15599354 255 QAFLA--DPVLANLSAVREKRVYALGPSSF 282
Cdd:cd01147 227 LEGYAknRPFWQSLKAVKNGRVYLLPALPF 256
BtuF cd01144
Cobalamin binding protein BtuF. These proteins have been shown to function as initial ...
32-178 4.50e-06

Cobalamin binding protein BtuF. These proteins have been shown to function as initial receptors in ABC transport of vitamin B12 (cobalamin) in eubacterial and some archaeal species. They belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind the metal ion in the cleft between these domains. In addition, these proteins sometimes have a low complexity region containing a metal-binding histidine-rich motif (repetitive HDH sequence).


Pssm-ID: 238564 [Multi-domain]  Cd Length: 245  Bit Score: 46.91  E-value: 4.50e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599354  32 RIVSTTPSVTGILLAMDAP--LVA--SAATTPSRLtdakgffsqwakvadqRGVEVLYRNLRFDIEAVIAQDPDLLVASA 107
Cdd:cd01144   2 RIVSLAPSATELLYALGLGdqLVGvtDYCDYPPEA----------------KKLPRVGGFYQLDLERVLALKPDLVIAWD 65
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15599354 108 TGAdsAAPYRAELEAQGVPTLVVDysKHSWQELA---TELGRHTGLERQAQAAIQRFDAYTAEVAAAIAPPQGP 178
Cdd:cd01144  66 DCN--VCAVVDQLRAAGIPVLVSE--PQTLDDILadiRRLGTLAGRPARAEELAEALRRRLAALRKQYASKPPP 135
PBP1_ABC_sugar_binding-like cd01536
periplasmic sugar-binding domain of active transport systems that are members of the type 1 ...
68-131 1.96e-03

periplasmic sugar-binding domain of active transport systems that are members of the type 1 periplasmic binding protein (PBP1) superfamily; Periplasmic sugar-binding domain of active transport systems that are members of the type 1 periplasmic binding protein (PBP1) superfamily. The members of this family function as the primary receptors for chemotaxis and transport of many sugar based solutes in bacteria and archaea. The sugar binding domain is also homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR. Moreover, this periplasmic binding domain, also known as Venus flytrap domain, undergoes transition from an open to a closed conformational state upon the binding of ligands such as lactose, ribose, fructose, xylose, arabinose, galactose/glucose, and other sugars. This family also includes the periplasmic binding domain of autoinducer-2 (AI-2) receptors such as LsrB and LuxP which are highly homologous to periplasmic pentose/hexose sugar-binding proteins.


Pssm-ID: 380478 [Multi-domain]  Cd Length: 268  Bit Score: 39.09  E-value: 1.96e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15599354  68 FFSQWA----KVADQRGVEVLYRNLRFD-------IEAVIAQDPDLLVASATGADSAAPYRAELEAQGVPTLVVD 131
Cdd:cd01536  13 FWVAVKkgaeAAAKELGVELVVLDAQGDvakqisqIEDLIAQGVDAIIIAPVDSEALVPAVKKANAAGIPVVAVD 87
RbsB COG1879
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ...
67-131 5.28e-03

ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH domain [Carbohydrate transport and metabolism];


Pssm-ID: 441483 [Multi-domain]  Cd Length: 307  Bit Score: 37.98  E-value: 5.28e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15599354  67 GFFSQWAK----VADQRGVEVLYRNLRFD-------IEAVIAQDPDLLVASATGADSAAPYRAELEAQGVPTLVVD 131
Cdd:COG1879  46 PFFVAVRKgaeaAAKELGVELIVVDAEGDaakqisqIEDLIAQGVDAIIVSPVDPDALAPALKKAKAAGIPVVTVD 121
PBP1_sensor_kinase-like cd06308
periplasmic binding domain of two-component sensor kinase signaling systems; Periplasmic ...
75-131 9.74e-03

periplasmic binding domain of two-component sensor kinase signaling systems; Periplasmic binding domain of two-component sensor kinase signaling systems, some of which are fused with a C-terminal histidine kinase A domain (HisK) and/or a signal receiver domain (REC). Members of this group share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily and are predicted to be involved in sensing of environmental stimuli; their substrate specificities, however, are not known in detail.


Pssm-ID: 380531 [Multi-domain]  Cd Length: 268  Bit Score: 36.76  E-value: 9.74e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15599354  75 VADQRGVEVLYRN-------LRFDIEAVIAQDPDLLVASATGADSAAPYRAELEAQGVPTLVVD 131
Cdd:cd06308  25 AAKYPNVELIVTDaqgdaakQIADIEDLIAQGVDLLIVSPNEADALTPVVKKAYDAGIPVIVLD 88
 
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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