NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|505384782|ref|WP_015571884|]
View 

MULTISPECIES: iron-siderophore ABC transporter substrate-binding protein [Enterobacter]

Protein Classification

iron-siderophore ABC transporter substrate-binding protein( domain architecture ID 10100157)

iron-siderophore ABC transporter substrate-binding protein functions as the initial receptor in the ABC transport of iron-hydroxamate siderophores such as achromobactin and petrobactin

Gene Ontology:  GO:0015891

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
FhuD cd01146
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ...
 37-302 5.76e-51

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: 169.00  E-value: 5.76e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384782  37 NPKRIVSLHDLDITIpLIELGVPPVAShgrtrPDGSHFLRssgMLTGIDFDNSDITFIGTA-DIDIEAIAAAKPDLIITE 115
Cdd:cd01146    2 KPQRIVALDWGALET-LLALGVKPVGV-----ADTAGYKP---WIPEPALPLEGVVDVGTRgQPNLEAIAALKPDLILGS 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384782 116 PTRNTPV-EQLEKIAPTVSIDHLDGGAP--EIYRKLAQLTGTEARLKILERRYQEQIEALKATI-DTSKLTVSVIQ-ANQ 190
Cdd:cd01146   73 ASRHDEIyDQLSQIAPTVLLDSSPWLAEwkENLRLIAKALGKEEEAEKLLAEYDQRLAELRQKLpDKGPKPVSVVRfSDA 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384782 191 GKINAMHSYHSLGRVLRDAGFRFPPLIESIPEGGRIDVSAERLPELDADFVFATWRGDTggKPQDELAAmdavMPGWcQF 270
Cdd:cd01146  153 GSIRLYGPNSFAGSVLEDLGLQNPWAQETTNDSGFATISLERLAKADADVLFVFTYEDE--ELAQALQA----NPLW-QN 225

                        250       260       270
                 ....*....|....*....|....*....|..
gi 505384782 271 LNACRTGHYVLISREEaisnSFASLGLMAAQV 302
Cdd:cd01146  226 LPAVKNGRVYVVDDVW----WFFGGGLSAARL 253
 
Name Accession Description Interval E-value
FhuD cd01146
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ...
 37-302 5.76e-51

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: 169.00  E-value: 5.76e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384782  37 NPKRIVSLHDLDITIpLIELGVPPVAShgrtrPDGSHFLRssgMLTGIDFDNSDITFIGTA-DIDIEAIAAAKPDLIITE 115
Cdd:cd01146    2 KPQRIVALDWGALET-LLALGVKPVGV-----ADTAGYKP---WIPEPALPLEGVVDVGTRgQPNLEAIAALKPDLILGS 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384782 116 PTRNTPV-EQLEKIAPTVSIDHLDGGAP--EIYRKLAQLTGTEARLKILERRYQEQIEALKATI-DTSKLTVSVIQ-ANQ 190
Cdd:cd01146   73 ASRHDEIyDQLSQIAPTVLLDSSPWLAEwkENLRLIAKALGKEEEAEKLLAEYDQRLAELRQKLpDKGPKPVSVVRfSDA 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384782 191 GKINAMHSYHSLGRVLRDAGFRFPPLIESIPEGGRIDVSAERLPELDADFVFATWRGDTggKPQDELAAmdavMPGWcQF 270
Cdd:cd01146  153 GSIRLYGPNSFAGSVLEDLGLQNPWAQETTNDSGFATISLERLAKADADVLFVFTYEDE--ELAQALQA----NPLW-QN 225

                        250       260       270
                 ....*....|....*....|....*....|..
gi 505384782 271 LNACRTGHYVLISREEaisnSFASLGLMAAQV 302
Cdd:cd01146  226 LPAVKNGRVYVVDDVW----WFFGGGLSAARL 253
FepB COG0614
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ...
 40-291 5.14e-31

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


Pssm-ID: 440379 [Multi-domain]  Cd Length: 264  Bit Score: 117.41  E-value: 5.14e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384782  40 RIVSLhDLDITIPLIELGVPPvASHGRTRPDGSHFLrssgmltgiDFDNSDITFIG-TADIDIEAIAAAKPDLIITEPTR 118
Cdd:COG0614    2 RIVSL-SPSATELLLALGAGD-RLVGVSDWGYCDYP---------ELELKDLPVVGgTGEPNLEAILALKPDLVLASSSG 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384782 119 NTP--VEQLEKI-APTVSIDHLD-GGAPEIYRKLAQLTGTEARLKILERRYQEQIEALKATI--DTSKLTVSVIQANQGK 192
Cdd:COG0614   71 NDEedYEQLEKIgIPVVVLDPRSlEDLYESIRLLGELLGREERAEALIAEYEARLAAVRARLagAEERPTVLYEIWSGDP 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384782 193 INAMHSYHSLGRVLRDAGFRFpplIESIPEGGRIDVSAERLPELDADFVFATWRGDTGGKPQDELAAMDAvMPGWCQfLN 272
Cdd:COG0614  151 LYTAGGGSFIGELLELAGGRN---VAADLGGGYPEVSLEQVLALDPDVIILSGGGYDAETAEEALEALLA-DPGWQS-LP 225

                        250
                 ....*....|....*....
gi 505384782 273 ACRTGHYVLISREEAISNS 291
Cdd:COG0614  226 AVKNGRVYVVPGDLLSRPG 244
Peripla_BP_2 pfam01497
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ...
 87-278 5.80e-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: 83.96  E-value: 5.80e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384782   87 DNSDITFIGTA-DIDIEAIAAAKPDLII--TEPTRNTPVEQLEKIAPTVSIDHLDGGAP--EIYRKLAQLTGTEARLKIL 161
Cdd:pfam01497  35 AVAAIVKVGAYgEINVERLAALKPDLVIlsTGYLTDEAEELLSLIIPTVIFESSSTGESlkEQIKQLGELLGLEDEAEEL 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384782  162 ERRYQEQIEALKATIDTSKLTVSVI--QANQGKINAMHSYHSLGRVLRDAGFrfPPLIESIPEGGRIDVSAERLPELDAD 239
Cdd:pfam01497 115 VAEIDSALAAAKKAVPSLTRKPVLVfgGADGGGYVVAGSNTYIGDLLRILGI--ENIAAELSGSEYAPISFEAILSSNPD 192

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 505384782  240 FVFATWRGDTGGKPQDELAAmdavMPGWcQFLNACRTGH 278
Cdd:pfam01497 193 VIIVSGRDSFTKTGPEFVAA----NPLW-AGLPAVKNGR 226
PRK10957 PRK10957
iron-enterobactin transporter periplasmic binding protein; Provisional
 3-242 6.47e-11

iron-enterobactin transporter periplasmic binding protein; Provisional


Pssm-ID: 236806 [Multi-domain]  Cd Length: 317  Bit Score: 62.30  E-value: 6.47e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384782   3 VFFAMLVLVGFAvGAAEPTQ----TFTDDLnRNVVVPVNPKRIVSLhDLDITIPLIELGVPPVAShGRTRPdGSHFLRSS 78
Cdd:PRK10957   7 LLLLGLLLSGIA-AAQASAAgwprTVTDSR-GSVTLESKPQRIVST-SVTLTGTLLAIDAPVIAS-GATTP-NTRVADDQ 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384782  79 GMLTgidfDNSDIT--------FIGtaDIDIEAIAAAKPDLIITEPTRNTPV----EQLEKIAPTVSIDHLDGGAPEIYR 146
Cdd:PRK10957  82 GFFR----QWSDVAkergvevlYIG--EPDAEAVAAQMPDLIVISATGGDSAlalyDQLSAIAPTLVIDYDDKSWQELAT 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384782 147 KLAQLTGTEARLKILERRYQEQIEALKATIDTSKLTVSVIQAN-QGKINAMHSYHSL-GRVLRDAGFRFPPLIESIPEGG 224
Cdd:PRK10957 156 QLGEATGLEKQAAAVIAQFDAQLAEVKAKITLPPQPVSALVYNgAGHSANLWTPESAqGQLLEQLGFTLAELPAGLQAST 235

                        250       260
                 ....*....|....*....|....*.
gi 505384782 225 R-------IDVSAERLPE-LDADFVF 242
Cdd:PRK10957 236 SqgkrhdiIQLGGENLAAgLNGETLF 261
 
Name Accession Description Interval E-value
FhuD cd01146
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ...
 37-302 5.76e-51

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: 169.00  E-value: 5.76e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384782  37 NPKRIVSLHDLDITIpLIELGVPPVAShgrtrPDGSHFLRssgMLTGIDFDNSDITFIGTA-DIDIEAIAAAKPDLIITE 115
Cdd:cd01146    2 KPQRIVALDWGALET-LLALGVKPVGV-----ADTAGYKP---WIPEPALPLEGVVDVGTRgQPNLEAIAALKPDLILGS 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384782 116 PTRNTPV-EQLEKIAPTVSIDHLDGGAP--EIYRKLAQLTGTEARLKILERRYQEQIEALKATI-DTSKLTVSVIQ-ANQ 190
Cdd:cd01146   73 ASRHDEIyDQLSQIAPTVLLDSSPWLAEwkENLRLIAKALGKEEEAEKLLAEYDQRLAELRQKLpDKGPKPVSVVRfSDA 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384782 191 GKINAMHSYHSLGRVLRDAGFRFPPLIESIPEGGRIDVSAERLPELDADFVFATWRGDTggKPQDELAAmdavMPGWcQF 270
Cdd:cd01146  153 GSIRLYGPNSFAGSVLEDLGLQNPWAQETTNDSGFATISLERLAKADADVLFVFTYEDE--ELAQALQA----NPLW-QN 225

                        250       260       270
                 ....*....|....*....|....*....|..
gi 505384782 271 LNACRTGHYVLISREEaisnSFASLGLMAAQV 302
Cdd:cd01146  226 LPAVKNGRVYVVDDVW----WFFGGGLSAARL 253
FepB COG0614
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ...
 40-291 5.14e-31

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


Pssm-ID: 440379 [Multi-domain]  Cd Length: 264  Bit Score: 117.41  E-value: 5.14e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384782  40 RIVSLhDLDITIPLIELGVPPvASHGRTRPDGSHFLrssgmltgiDFDNSDITFIG-TADIDIEAIAAAKPDLIITEPTR 118
Cdd:COG0614    2 RIVSL-SPSATELLLALGAGD-RLVGVSDWGYCDYP---------ELELKDLPVVGgTGEPNLEAILALKPDLVLASSSG 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384782 119 NTP--VEQLEKI-APTVSIDHLD-GGAPEIYRKLAQLTGTEARLKILERRYQEQIEALKATI--DTSKLTVSVIQANQGK 192
Cdd:COG0614   71 NDEedYEQLEKIgIPVVVLDPRSlEDLYESIRLLGELLGREERAEALIAEYEARLAAVRARLagAEERPTVLYEIWSGDP 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384782 193 INAMHSYHSLGRVLRDAGFRFpplIESIPEGGRIDVSAERLPELDADFVFATWRGDTGGKPQDELAAMDAvMPGWCQfLN 272
Cdd:COG0614  151 LYTAGGGSFIGELLELAGGRN---VAADLGGGYPEVSLEQVLALDPDVIILSGGGYDAETAEEALEALLA-DPGWQS-LP 225

                        250
                 ....*....|....*....
gi 505384782 273 ACRTGHYVLISREEAISNS 291
Cdd:COG0614  226 AVKNGRVYVVPGDLLSRPG 244
FecB COG4594
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and ...
 3-278 3.14e-28

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


Pssm-ID: 443650 [Multi-domain]  Cd Length: 316  Bit Score: 111.17  E-value: 3.14e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384782   3 VFFAMLVLVG--------FAVGAAEPTQTFTDDLNrNVVVPVNPKRIVSLhDLDITIPLIELGVPPVAS----------- 63
Cdd:COG4594   10 LLLALLLLAAcgssssdsSSSEAAAGARTVKHAMG-ETTIPGTPKRVVVL-EWSFADALLALGVTPVGIaddndydrwvp 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384782  64 HGRTRPDgshflrssgmltgidfdnsDITFIGT-ADIDIEAIAAAKPDLIITEPTRNTPV-EQLEKIAPTVSIDHLDGGA 141
Cdd:COG4594   88 YLRDLIK-------------------GVTSVGTrSQPNLEAIAALKPDLIIADKSRHEAIyDQLSKIAPTVLFKSRNGDY 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384782 142 PEI---YRKLAQLTGTEARLKILERRYQEQIEALKATI--DTSKLTVSVIQANQGKINAMHSYHSLGRVLRDAGFRFPPL 216
Cdd:COG4594  149 QENlesFKTIAKALGKEEEAEAVLADHDQRIAEAKAKLaaADKGKKVAVGQFRADGLRLYTPNSFAGSVLAALGFENPPK 228

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505384782 217 IESIPEGGRIDVSAERLPELDADFVFATWRGDtgGKPQDELAAmDAVmpgWcQFLNACRTGH 278
Cdd:COG4594  229 QSKDNGYGYSEVSLEQLPALDPDVLFIATYDD--PSILKEWKN-NPL---W-KNLKAVKNGR 283
FeuA cd01138
Periplasmic binding protein FeuA. These proteins have predicted to function as initial ...
 30-278 1.55e-23

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: 96.63  E-value: 1.55e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384782  30 RNVVVPVNPKRIVSLHDLDITipLIELGVPPVA--SHGRTRPDgshflrssgMLTGIDFDNSDITfigtADIDIEAIAAA 107
Cdd:cd01138    1 GEVEIPAKPKRIVALSGETEG--LALLGIKPVGaaSIGGKNPY---------YKKKTLAKVVGIV----DEPNLEKVLEL 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384782 108 KPDLIITEPTRNTPVEQLEKIAPTVSIDHLDGGAPEIYRKLAQLTGTEARL-KILErRYQEQIEALKATI---DTSKLTV 183
Cdd:cd01138   66 KPDLIIVSSKQEENYEKLSKIAPTVPVSYNSSDWEEQLKEIGKLLNKEDEAeKWLA-DYKQKAKEAKEKIkkkLGNDKSV 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384782 184 SVIQAnQGKINAMHSYH-SLGRVL-RDAGFRFPPLIESIPEG-GRIDVSAERLPELDADFVFATwrGDTGGKPQDELAAM 260
Cdd:cd01138  145 AVLRG-RKQIYVFGEDGrGGGPILyADLGLKAPEKVKEIEDKpGYAAISLEVLPEFDADYIFLL--FFTGPEAKADFESL 221

                        250
                 ....*....|....*...
gi 505384782 261 DAvmpgWcQFLNACRTGH 278
Cdd:cd01138  222 PI----W-KNLPAVKNNH 234
CeuA COG4607
ABC-type enterochelin transport system, periplasmic component [Inorganic ion transport and ...
 3-242 1.76e-20

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


Pssm-ID: 443657 [Multi-domain]  Cd Length: 310  Bit Score: 89.47  E-value: 1.76e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384782   3 VFFAMLVLVG-----FAVGAAEPTQTFT-DDLNRNVVVPVNPKRIVSLhD---LDItipLIELGVPPVASHGRTRPDgsh 73
Cdd:COG4607   10 ALAAALALAAcgsssAAAASAAAAETVTvEHALGTVEVPKNPKRVVVF-DngaLDT---LDALGVEVAGVPKGLLPD--- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384782  74 FLRssgmltgiDFDNSDITFIGT-ADIDIEAIAAAKPDLIITEPTRNTPVEQLEKIAPTVSID----HLDGGAPEIYRKL 148
Cdd:COG4607   83 YLS--------KYADDKYANVGTlFEPDLEAIAALKPDLIIIGGRSAKKYDELSKIAPTIDLTvdgeDYLESLKRNTETL 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384782 149 AQLTGTEARLKILERRYQEQIEALKATIDtSKLTVSVIQANQGKInamhSYHSLGR---VLRDAgFRFPPLIESIPEGGR 225
Cdd:COG4607  155 GEIFGKEDEAEELVADLDAKIAALKAAAA-GKGTALIVLTNGGKI----SAYGPGSrfgPIHDV-LGFKPADEDIEASTH 228

                        250
                 ....*....|....*...
gi 505384782 226 -IDVSAERLPELDADFVF 242
Cdd:COG4607  229 gQAISFEFIAEANPDWLF 246
FatB cd01140
Siderophore binding protein FatB. These proteins have been shown to function as ABC-type ...
 32-256 3.26e-20

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: 88.08  E-value: 3.26e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384782  32 VVVPVNPKRIVSLhDLDITIPLIELGVPPVAshgrtRPDGS---HFLRssgmltgiDFDNSDITFIGTA-DIDIEAIAAA 107
Cdd:cd01140    6 TKVPKNPEKVVVF-DVGALDTLDALGVKVVG-----VPKSStlpEYLK--------KYKDDKYANVGTLfEPDLEAIAAL 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384782 108 KPDLIITEPTRNTPVEQLEKIAPTVSI-----DHLDGGAPEIyRKLAQLTGTEARLKILERRYQEQIEALKATIDTSKlT 182
Cdd:cd01140   72 KPDLIIIGGRLAEKYDELKKIAPTIDLgadlkNYLESVKQNI-ETLGKIFGKEEEAKELVAEIDASIAEAKSAAKGKK-K 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505384782 183 VSVIQANQGKINAM--HSYhsLGRVLRDAGfrFPPLIESIPEGGRID-VSAERLPELDADFVFATWRG--DTGGKPQDE 256
Cdd:cd01140  150 ALVVLVNGGKLSAFgpGSR--FGWLHDLLG--FEPADENIKASSHGQpVSFEYILEANPDWLFVIDRGaaIGAEGSSAK 224
FepB COG4592
ABC-type Fe2+-enterobactin transport system, periplasmic component [Inorganic ion transport ...
 32-243 3.93e-19

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


Pssm-ID: 443649 [Multi-domain]  Cd Length: 330  Bit Score: 86.15  E-value: 3.93e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384782  32 VVVPVNPKRIVSLhDLDITIPLIELGVPPVAShGRTRP----DGSHFLRSSGMltgiDFDNSDITFI-GTADIDIEAIAA 106
Cdd:COG4592   51 VTLPAKPQRIVST-SVTLTGSLLAIDAPVVAS-GATTPnnvtDDQGFFRQWAD----VAKERGVKRLyIGLEPNAEAIAA 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384782 107 AKPDLIITEPTRNTPV----EQLEKIAPTVSIDHLDGGAPEIYRKLAQLTGTEARLKILERRYQEQIEALKATIDTSKLT 182
Cdd:COG4592  125 AAPDLIIGSATGGDSAldlyDQLSAIAPTLVVNYDDKSWQELATQLGEATGHEAQADAVIAAFDARVAEVKAAITLPPQP 204

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505384782 183 VSVIQAN-QGKINAMHSYHSLGRVLRDAGFRFPPLIESIPE----GGRID---VSAERLPE-LDAD--FVFA 243
Cdd:COG4592  205 VSALVYNeDGGANLWTPESAQGQLLQALGFTLAPLPAELATstsqGKRGDivqLSGENLAAaLTGPtlFLFA 276
Peripla_BP_2 pfam01497
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ...
 87-278 5.80e-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: 83.96  E-value: 5.80e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384782   87 DNSDITFIGTA-DIDIEAIAAAKPDLII--TEPTRNTPVEQLEKIAPTVSIDHLDGGAP--EIYRKLAQLTGTEARLKIL 161
Cdd:pfam01497  35 AVAAIVKVGAYgEINVERLAALKPDLVIlsTGYLTDEAEELLSLIIPTVIFESSSTGESlkEQIKQLGELLGLEDEAEEL 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384782  162 ERRYQEQIEALKATIDTSKLTVSVI--QANQGKINAMHSYHSLGRVLRDAGFrfPPLIESIPEGGRIDVSAERLPELDAD 239
Cdd:pfam01497 115 VAEIDSALAAAKKAVPSLTRKPVLVfgGADGGGYVVAGSNTYIGDLLRILGI--ENIAAELSGSEYAPISFEAILSSNPD 192

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 505384782  240 FVFATWRGDTGGKPQDELAAmdavMPGWcQFLNACRTGH 278
Cdd:pfam01497 193 VIIVSGRDSFTKTGPEFVAA----NPLW-AGLPAVKNGR 226
TroA_e cd01142
Periplasmic binding protein TroA_e. These proteins are predicted to function as initial ...
 16-249 7.15e-12

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: 64.68  E-value: 7.15e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384782  16 GAAEPTQTFTDDLNRNVVVPVNPKRIVSLHDLDITIPLIELGVPPVASHGRTRPDGSHFLRSSGMLTGIdfdnsdITFIG 95
Cdd:cd01142    2 AATAATRTITDMAGRKVTIPDEVKRIAALWGAGNAVVAALGGGKLIVATTSTVQQEPWLYRLAPSLENV------ATGGT 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384782  96 TADIDIEAIAAAKPDLIITEPTRNT-PVEQLEKIAPTVSIDHLD-GGAPEIYRKLAQLTGTEARLKILERRYQEQI---- 169
Cdd:cd01142   76 GNDVNIEELLALKPDVVIVWSTDGKeAGKAVLRLLNALSLRDAElEEVKLTIALLGELLGRQEKAEALVAYFDDNLayva 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384782 170 EALKATIDTSKLTVSVIQANQGKINAMHSYHSLgrVLRDAGFRfpPLIESIPEGGRIDVSAERLPELDADFVFaTWRGDT 249
Cdd:cd01142  156 ARTKKLPDSERPRVYYAGPDPLTTDGTGSITNS--WIDLAGGI--NVASEATKKGSGEVSLEQLLKWNPDVII-VGNADT 230
TroA-like cd00636
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function ...
 39-186 3.18e-11

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: 60.65  E-value: 3.18e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384782  39 KRIVSL-HDLDITIPLIELGVPPVAShgrtrpdgshfLRSSGMLTGIDFDNSDITFIGTA-DIDIEAIAAAKPDLIITEP 116
Cdd:cd00636    1 KRVVALdPGATELLLALGGDDKPVGV-----------ADPSGYPPEAKALLEKVPDVGHGyEPNLEKIAALKPDLIIANG 69

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505384782 117 TRNTP-VEQLEKIA-PTVSIDHLDG----GAPEIYRKLAQLTGTEARLKILERRYQEQIEALKATI-DTSKLTVSVI 186
Cdd:cd00636   70 SGLEAwLDKLSKIAiPVVVVDEASElsleNIKESIRLIGKALGKEENAEELIAELDARLAELRAKLaKIPKKKVSLV 146
PRK10957 PRK10957
iron-enterobactin transporter periplasmic binding protein; Provisional
 3-242 6.47e-11

iron-enterobactin transporter periplasmic binding protein; Provisional


Pssm-ID: 236806 [Multi-domain]  Cd Length: 317  Bit Score: 62.30  E-value: 6.47e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384782   3 VFFAMLVLVGFAvGAAEPTQ----TFTDDLnRNVVVPVNPKRIVSLhDLDITIPLIELGVPPVAShGRTRPdGSHFLRSS 78
Cdd:PRK10957   7 LLLLGLLLSGIA-AAQASAAgwprTVTDSR-GSVTLESKPQRIVST-SVTLTGTLLAIDAPVIAS-GATTP-NTRVADDQ 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384782  79 GMLTgidfDNSDIT--------FIGtaDIDIEAIAAAKPDLIITEPTRNTPV----EQLEKIAPTVSIDHLDGGAPEIYR 146
Cdd:PRK10957  82 GFFR----QWSDVAkergvevlYIG--EPDAEAVAAQMPDLIVISATGGDSAlalyDQLSAIAPTLVIDYDDKSWQELAT 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384782 147 KLAQLTGTEARLKILERRYQEQIEALKATIDTSKLTVSVIQAN-QGKINAMHSYHSL-GRVLRDAGFRFPPLIESIPEGG 224
Cdd:PRK10957 156 QLGEATGLEKQAAAVIAQFDAQLAEVKAKITLPPQPVSALVYNgAGHSANLWTPESAqGQLLEQLGFTLAELPAGLQAST 235

                        250       260
                 ....*....|....*....|....*.
gi 505384782 225 R-------IDVSAERLPE-LDADFVF 242
Cdd:PRK10957 236 SqgkrhdiIQLGGENLAAgLNGETLF 261
fecB PRK11411
iron-dicitrate transporter substrate-binding subunit; Provisional
 2-307 2.38e-07

iron-dicitrate transporter substrate-binding subunit; Provisional


Pssm-ID: 183123 [Multi-domain]  Cd Length: 303  Bit Score: 51.21  E-value: 2.38e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384782   2 RVFFAMLVLVGFAVGAAEPTqtfTDDLNRNVVVPVNPKRIVSLhDLDITIPLIELGVPPVashgrtrpdgshflrssgml 81
Cdd:PRK11411   6 RLLFAGLLLLSGSSHAFAVT---VQDEQGTFTLEKTPQRIVVL-ELSFVDALAAVGVSPV-------------------- 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384782  82 tGIDFDNsDITFI--------------GT-ADIDIEAIAAAKPDLIITEPTRNTPV-EQLEKIAPTVSID--------HL 137
Cdd:PRK11411  62 -GVADDN-DAKRIlpevrahlkpwqsvGTrSQPSLEAIAALKPDLIIADSSRHAGVyIALQKIAPTLLLKsrnetyqeNL 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384782 138 DGGApeiyrKLAQLTGTEARLKILERRYQEQIEALKATIDTSKlTVSVIQANQGKINaMHSYHS-LGRVLRDAGFRFPpl 216
Cdd:PRK11411 140 QSAA-----IIGEVLGKKREMQARIEQHKERMAQFASQLPKGT-RVAFGTSREQQFN-LHSPESyTGSVLAALGLNVP-- 210

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384782 217 IESIPEGGRIDVSAERLPELDADFVFA----------TWRGDtggkpqdelaamdavmPGWcQFLNACRTGHYVLISree 286
Cdd:PRK11411 211 KAPMNGAAMPSISLEQLLALNPDWLLVahyrqesivkRWQQD----------------PLW-QMLTAAKKQQVASVD--- 270

                        330       340
                 ....*....|....*....|..
gi 505384782 287 aiSNSFASL-GLMAAQvqsQIA 307
Cdd:PRK11411 271 --SNTWARMrGIFAAE---RIA 287
BtuF cd01144
Cobalamin binding protein BtuF. These proteins have been shown to function as initial ...
 95-278 3.55e-07

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: 50.38  E-value: 3.55e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384782  95 GTADIDIEAIAAAKPDLIITEPTRNTP--VEQLEKIAPTVSIDH---LDgGAPEIYRKLAQLTGTEARLKILERRYQEQI 169
Cdd:cd01144   44 GFYQLDLERVLALKPDLVIAWDDCNVCavVDQLRAAGIPVLVSEpqtLD-DILADIRRLGTLAGRPARAEELAEALRRRL 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384782 170 EALKA-TIDTSKLTVSVIQANQGKINAMHSYhsLGRVLRDAGFRfpPLIESIPEGGRIdVSAERLPELDADFVFATWRGD 248
Cdd:cd01144  123 AALRKqYASKPPPRVFYQEWIDPLMTAGGDW--VPELIALAGGV--NVFADAGERSPQ-VSWEDVLAANPDVIVLSPCGF 197

                        170       180       190
                 ....*....|....*....|....*....|
gi 505384782 249 TGGKPQdelaamDAVMPGWCQfLNACRTGH 278
Cdd:cd01144  198 GFTPAI------LRKEPAWQA-LPAVRNGR 220
YvrC cd01143
Periplasmic binding protein YvrC. These proteins are predicted to function as initial ...
 37-183 4.23e-07

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: 49.58  E-value: 4.23e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384782  37 NPKRIVSLhDLDITIPLIELGVppvashgrtrpdGSHflrssgmLTGID-FDN-----SDITFIGTAD-IDIEAIAAAKP 109
Cdd:cd01143    2 EPERIVSL-SPSITEILFALGA------------GDK-------IVGVDtYSNypkevRKKPKVGSYSnPNVEKIVALKP 61

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505384782 110 DLIITEPT-RNTPVEQLEKIAPTVSIDHLDGGAPEIYR---KLAQLTGTEARLKILERRYQEQIEALKATIDT-SKLTV 183
Cdd:cd01143   62 DLVIVSSSsLAELLEKLKDAGIPVVVLPAASSLDEIYDqieLIGKITGAEEEAEKLVKEMKQKIDKVKDKGKTiKKSKV 140
TroA_f cd01139
Periplasmic binding protein TroA_f. These proteins are predicted to function as initial ...
 23-278 5.12e-05

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: 44.22  E-value: 5.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384782  23 TFTDDLNRNVVVPVNPKRIV-SLHDLDITIPLIElGVPPVASHGRTRPDGSHFLRSSGMLTGIDF-DNSDITFIGT---A 97
Cdd:cd01139    2 TVTDVAGRKVTLDAPVERVLlGEGRQLYALALLE-GENPFARIVGWGGDLKKGDPDTYAKYKEKFpEIADIPLIGStynG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384782  98 DIDIEAIAAAKPDLII-------TEPTRNTpVEQLEKIA-PTVSID---HLDGGAPEIYRKLAQLTGTEARLKILERRYQ 166
Cdd:cd01139   81 DFSVEKVLTLKPDLVIlniwaktTAEESGI-LEKLEQAGiPVVFVDfrqKPLKNTTPSMRLLGKALGREERAEEFIEFYQ 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384782 167 EQIEALKATIDTSKLT---VSVIQANQGKINAMHSYHS--LGRVLRDAGFR--FPPLIESIPEggriDVSAERLPELDAD 239
Cdd:cd01139  160 ERIDRIRDRLAKINEPkpkVFIELGAGGPEECCSTYGNgnWGELVDAAGGDniADGLIPGTSG----ELNAEYVIAANPE 235

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 505384782 240 FVFAT---WRGDTGG--------KPQDELAAMDAVM--PGWCQfLNACRTGH 278
Cdd:cd01139  236 IIIATggnWAKDPSGvslgpdgtTADAKESLLRALLkrPGWSS-LQAVKNGR 286
ChuT COG4558
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism] ...
 1-186 1.77e-04

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


Pssm-ID: 443619 [Multi-domain]  Cd Length: 285  Bit Score: 42.49  E-value: 1.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384782   1 MRVFFAMLVLVGFAVGAAEPTQTFTDdlnrnvvvpvnPKRIVSLHDlDITIPLIELGV-------------PPVAshgRT 67
Cdd:COG4558    1 MKRLALALLLLALAALAAGASVAAAA-----------AERIVSLGG-SVTEIVYALGAgdrlvgvdttstyPAAA---KA 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384782  68 RPD-GSHFlrssgmltgidfdnsditfigtaDIDIEAIAAAKPDLIITEPTRNTP--VEQLEKIA-PTVSIDH---LDGG 140
Cdd:COG4558   66 LPDvGYMR-----------------------QLSAEGILSLKPTLVLASEGAGPPevLDQLRAAGvPVVVVPAapsLEGV 122

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 505384782 141 APEIyRKLAQLTGTEARLKILERRYQEQIEALKATIDTSKLTVSVI 186
Cdd:COG4558  123 LAKI-RAVAAALGVPEAGEALAARLEADLAALAARVAAIGKPPRVL 167
HutB cd01149
Hemin binding protein HutB. These proteins have been shown to function as initial receptors ...
 102-186 3.16e-03

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: 38.40  E-value: 3.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384782 102 EAIAAAKPDLIITEPTRNTP--VEQLEKIAPTV----SIDHLDGGAPEIyRKLAQLTGTEARLKILERRYQEQIEALKAT 175
Cdd:cd01149   52 EGVLSLKPTLVIASDEAGPPeaLDQLRAAGVPVvtvpSTPTLDGLLTKI-RQVAQALGVPEKGEALAQEVRQRLAALRKT 130

                         90
                 ....*....|.
gi 505384782 176 IDTSKLTVSVI 186
Cdd:cd01149  131 VAAHKKPPRVL 141
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH