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Conserved domains on  [gi|818431575|gb|AKG33286|]
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hypothetical protein VK70_00555 [Paenibacillus durus ATCC 35681]

Protein Classification

TroA family protein( domain architecture ID 513)

TroA family protein; most TroA-like proteins are encoded by ABC-type operons and appear to function as periplasmic components of ABC transporters in metal ion uptake.

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TroA-like super family cl00262
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function ...
 42-354 3.22e-71

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.


The actual alignment was detected with superfamily member cd01142:

Pssm-ID: 469696 [Multi-domain]  Cd Length: 289  Bit Score: 224.16  E-value: 3.22e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818431575  42 PAPSAkPTYTIVDQLGRTVEIPGKVDRIVALQHHTLDIMLELHAQDKLVGVLRDWesLLGSYAADVYPNIRNLETPGSIS 121
Cdd:cd01142    1 PAATA-ATRTITDMAGRKVTIPDEVKRIAALWGAGNAVVAALGGGKLIVATTSTV--QQEPWLYRLAPSLENVATGGTGN 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818431575 122 ELNVEAVASLKPDVVFVSNQIPKETLAQLEQLgIPVVgitlyvadkeqastihpdlvNPDEAYTEGLKQAINLIGQITGT 201
Cdd:cd01142   78 DVNIEELLALKPDVVIVWSTDGKEAGKAVLRL-LNAL--------------------SLRDAELEEVKLTIALLGELLGR 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818431575 202 ENKAAELWNYVVSNRAIVSEHLSTVPEQDRIKVYMANENMYTY-GTGKYVGVAMAKAGARNVAE--TIKGYKQVSVEQVT 278
Cdd:cd01142  137 QEKAEALVAYFDDNLAYVAARTKKLPDSERPRVYYAGPDPLTTdGTGSITNSWIDLAGGINVASeaTKKGSGEVSLEQLL 216

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 818431575 279 AWNPEVIFVQSRYASvlDEIRGDKAWAAIDAVKNGKLIIAPDYTKPWGNPAPEsMALGEIWLAKTLYPDAFKDVDL 354
Cdd:cd01142  217 KWNPDVIIVGNADTK--AAILADPRWQNLRAVKNGRVYVNPEGAFWWDRPSAE-EALLGLWLAKTLYPERFTDDDM 289
 
Name Accession Description Interval E-value
TroA_e cd01142
Periplasmic binding protein TroA_e. These proteins are predicted to function as initial ...
 42-354 3.22e-71

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: 224.16  E-value: 3.22e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818431575  42 PAPSAkPTYTIVDQLGRTVEIPGKVDRIVALQHHTLDIMLELHAQDKLVGVLRDWesLLGSYAADVYPNIRNLETPGSIS 121
Cdd:cd01142    1 PAATA-ATRTITDMAGRKVTIPDEVKRIAALWGAGNAVVAALGGGKLIVATTSTV--QQEPWLYRLAPSLENVATGGTGN 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818431575 122 ELNVEAVASLKPDVVFVSNQIPKETLAQLEQLgIPVVgitlyvadkeqastihpdlvNPDEAYTEGLKQAINLIGQITGT 201
Cdd:cd01142   78 DVNIEELLALKPDVVIVWSTDGKEAGKAVLRL-LNAL--------------------SLRDAELEEVKLTIALLGELLGR 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818431575 202 ENKAAELWNYVVSNRAIVSEHLSTVPEQDRIKVYMANENMYTY-GTGKYVGVAMAKAGARNVAE--TIKGYKQVSVEQVT 278
Cdd:cd01142  137 QEKAEALVAYFDDNLAYVAARTKKLPDSERPRVYYAGPDPLTTdGTGSITNSWIDLAGGINVASeaTKKGSGEVSLEQLL 216

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 818431575 279 AWNPEVIFVQSRYASvlDEIRGDKAWAAIDAVKNGKLIIAPDYTKPWGNPAPEsMALGEIWLAKTLYPDAFKDVDL 354
Cdd:cd01142  217 KWNPDVIIVGNADTK--AAILADPRWQNLRAVKNGRVYVNPEGAFWWDRPSAE-EALLGLWLAKTLYPERFTDDDM 289
FepB COG0614
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ...
 68-350 1.07e-53

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


Pssm-ID: 440379 [Multi-domain]  Cd Length: 264  Bit Score: 178.27  E-value: 1.07e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818431575  68 RIVALQHHTLDIMLELHAQDKLVGVLRDWESLLGSYAADVYPNIrnletpGSISELNVEAVASLKPDVVFVSN-QIPKET 146
Cdd:COG0614    2 RIVSLSPSATELLLALGAGDRLVGVSDWGYCDYPELELKDLPVV------GGTGEPNLEAILALKPDLVLASSsGNDEED 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818431575 147 LAQLEQLGIPVVGItlyvadkeqastihpdlvnpDEAYTEGLKQAINLIGQITGTENKAAELWNYVVSNRAIVSEHLSTv 226
Cdd:COG0614   76 YEQLEKIGIPVVVL--------------------DPRSLEDLYESIRLLGELLGREERAEALIAEYEARLAAVRARLAG- 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818431575 227 pEQDRIKVYMA---NENMYTYGTGKYVGVAMAKAGARNVAETIK-GYKQVSVEQVTAWNPEVIFVQSRY------ASVLD 296
Cdd:COG0614  135 -AEERPTVLYEiwsGDPLYTAGGGSFIGELLELAGGRNVAADLGgGYPEVSLEQVLALDPDVIILSGGGydaetaEEALE 213

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 818431575 297 EIRGDKAWAAIDAVKNGKLIIAPDYTKPWGNPApesMALGEIWLAKTLYPDAFK 350
Cdd:COG0614  214 ALLADPGWQSLPAVKNGRVYVVPGDLLSRPGPR---LLLALEDLAKALHPELFA 264
Peripla_BP_2 pfam01497
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ...
 70-321 1.38e-26

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: 105.91  E-value: 1.38e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818431575   70 VALQHHTLDIMLELHAQDKLVGVlrdwesllGSYAADVYPNIRNLETP--GSISELNVEAVASLKPDVVFVSNQIPKETL 147
Cdd:pfam01497   1 AALSPAYTEILYALGATDSIVGV--------DAYTRDPLKADAVAAIVkvGAYGEINVERLAALKPDLVILSTGYLTDEA 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818431575  148 AQLEQLGIPVVGitlyvadkeqastihpdlVNPDEAYtEGLKQAINLIGQITGTENKAAELWNYVVSN-RAIVSEhlstV 226
Cdd:pfam01497  73 EELLSLIIPTVI------------------FESSSTG-ESLKEQIKQLGELLGLEDEAEELVAEIDSAlAAAKKA----V 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818431575  227 PEQDRIKVYM---ANENMYTY-GTGKYVGVAMAKAGARNVAETI--KGYKQVSVEQVTAWNPEVIFVQSR---YASVLDE 297
Cdd:pfam01497 130 PSLTRKPVLVfggADGGGYVVaGSNTYIGDLLRILGIENIAAELsgSEYAPISFEAILSSNPDVIIVSGRdsfTKTGPEF 209

                         250       260
                  ....*....|....*....|....
gi 818431575  298 IRGDKAWAAIDAVKNGKLIIAPDY 321
Cdd:pfam01497 210 VAANPLWAGLPAVKNGRVYTLPSD 233
btuF PRK09534
corrinoid ABC transporter substrate-binding protein; Reviewed
 37-334 3.10e-19

corrinoid ABC transporter substrate-binding protein; Reviewed


Pssm-ID: 236552 [Multi-domain]  Cd Length: 359  Bit Score: 88.04  E-value: 3.10e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818431575  37 AGEQQPAPSAKPT---------YTIVDQLGRTVEIPGKVDRIVALQHHTLDIMLELHAQDKLVGVLRdwesllgsYAADV 107
Cdd:PRK09534  22 GGALAPAPAAQHAdadracsfpVTETDATGTEITLDERPERVVTLNPSAAQTMWELGARDRVVGVTQ--------YASYL 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818431575 108 yPNI--RNLETPGSISELNVEAVASLKPDVVFVSNQIPKETLAQLEQLGIPVVGITLyvadkeqASTIhpdlvnpdeayt 185
Cdd:PRK09534  94 -DGAeeRTNVSGGQPFGVNVEAVVGLDPDLVLAPNAVAGDTVTRLREAGITVFHFPA-------ATSI------------ 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818431575 186 EGLKQAINLIGQITGTENKAAELWNYVVSNRAIVSEHLSTVpeQDRIKVYMANENMYTYGTGKYVGVAMAKAGARNVA-- 263
Cdd:PRK09534 154 EDVAEKTATIGRLTGNCEAAAETNAEMRDRVDAVEDRTADV--DDRPRVLYPLGDGYTAGGNTFIGALIEAAGGHNVAad 231

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 818431575 264 ETIKGYKQVSVEQVTAWNPEVIFVQSRYASVLDEirgdKAWAAIDAVKNGKLIIAPdyTKPWGNPAP---ESMA 334
Cdd:PRK09534 232 ATTDGYPQLSEEVIVQQDPDVIVVATASALVAET----EPYASTTAGETGNVVTVN--VNHINQPAPrivESMA 299
 
Name Accession Description Interval E-value
TroA_e cd01142
Periplasmic binding protein TroA_e. These proteins are predicted to function as initial ...
 42-354 3.22e-71

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: 224.16  E-value: 3.22e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818431575  42 PAPSAkPTYTIVDQLGRTVEIPGKVDRIVALQHHTLDIMLELHAQDKLVGVLRDWesLLGSYAADVYPNIRNLETPGSIS 121
Cdd:cd01142    1 PAATA-ATRTITDMAGRKVTIPDEVKRIAALWGAGNAVVAALGGGKLIVATTSTV--QQEPWLYRLAPSLENVATGGTGN 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818431575 122 ELNVEAVASLKPDVVFVSNQIPKETLAQLEQLgIPVVgitlyvadkeqastihpdlvNPDEAYTEGLKQAINLIGQITGT 201
Cdd:cd01142   78 DVNIEELLALKPDVVIVWSTDGKEAGKAVLRL-LNAL--------------------SLRDAELEEVKLTIALLGELLGR 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818431575 202 ENKAAELWNYVVSNRAIVSEHLSTVPEQDRIKVYMANENMYTY-GTGKYVGVAMAKAGARNVAE--TIKGYKQVSVEQVT 278
Cdd:cd01142  137 QEKAEALVAYFDDNLAYVAARTKKLPDSERPRVYYAGPDPLTTdGTGSITNSWIDLAGGINVASeaTKKGSGEVSLEQLL 216

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 818431575 279 AWNPEVIFVQSRYASvlDEIRGDKAWAAIDAVKNGKLIIAPDYTKPWGNPAPEsMALGEIWLAKTLYPDAFKDVDL 354
Cdd:cd01142  217 KWNPDVIIVGNADTK--AAILADPRWQNLRAVKNGRVYVNPEGAFWWDRPSAE-EALLGLWLAKTLYPERFTDDDM 289
FepB COG0614
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ...
 68-350 1.07e-53

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


Pssm-ID: 440379 [Multi-domain]  Cd Length: 264  Bit Score: 178.27  E-value: 1.07e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818431575  68 RIVALQHHTLDIMLELHAQDKLVGVLRDWESLLGSYAADVYPNIrnletpGSISELNVEAVASLKPDVVFVSN-QIPKET 146
Cdd:COG0614    2 RIVSLSPSATELLLALGAGDRLVGVSDWGYCDYPELELKDLPVV------GGTGEPNLEAILALKPDLVLASSsGNDEED 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818431575 147 LAQLEQLGIPVVGItlyvadkeqastihpdlvnpDEAYTEGLKQAINLIGQITGTENKAAELWNYVVSNRAIVSEHLSTv 226
Cdd:COG0614   76 YEQLEKIGIPVVVL--------------------DPRSLEDLYESIRLLGELLGREERAEALIAEYEARLAAVRARLAG- 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818431575 227 pEQDRIKVYMA---NENMYTYGTGKYVGVAMAKAGARNVAETIK-GYKQVSVEQVTAWNPEVIFVQSRY------ASVLD 296
Cdd:COG0614  135 -AEERPTVLYEiwsGDPLYTAGGGSFIGELLELAGGRNVAADLGgGYPEVSLEQVLALDPDVIILSGGGydaetaEEALE 213

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 818431575 297 EIRGDKAWAAIDAVKNGKLIIAPDYTKPWGNPApesMALGEIWLAKTLYPDAFK 350
Cdd:COG0614  214 ALLADPGWQSLPAVKNGRVYVVPGDLLSRPGPR---LLLALEDLAKALHPELFA 264
HemV-2 cd01147
Metal binding protein HemV-2. These proteins are predicted to function as initial receptors ...
 62-319 3.49e-36

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: 132.46  E-value: 3.49e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818431575  62 IPGKVDRIVALQHHTLDIMLELHAQDKLVGVLRDWESLLGSYAADVYPNIRNLETPGSI---SELNVEAVASLKPDVVFV 138
Cdd:cd01147    1 VPKPVERVVAAGPGALRLLYALAAPDKIVGVDDAEKSDEGRPYFLASPELKDLPVIGRGgrgNTPNYEKIAALKPDVVID 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818431575 139 SNQIPKETLAQL--EQLGIPVVGITLYVADKEQASTIHpdlvnpdeayteglkqainLIGQITGTENKAAELWNYVVSNR 216
Cdd:cd01147   81 VGSDDPTSIADDlqKKTGIPVVVLDGGDSLEDTPEQIR-------------------LLGKVLGKEERAEELISFIESIL 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818431575 217 AIVSEHLSTVPEQDRIKVYMAnENMYTYGTGKYVGVA-----MAKAGARNVAE--TIKGYKQVSVEQVTAWNPEVIFVQ- 288
Cdd:cd01147  142 ADVEERTKDIPDEEKPTVYFG-RIGTKGAAGLESGLAgsievFELAGGINVADglGGGGLKEVSPEQILLWNPDVIFLDt 220

                        250       260       270
                 ....*....|....*....|....*....|..
gi 818431575 289 -SRYASVLDEIRGDKAWAAIDAVKNGKLIIAP 319
Cdd:cd01147  221 gSFYLSLEGYAKNRPFWQSLKAVKNGRVYLLP 252
TroA_f cd01139
Periplasmic binding protein TroA_f. These proteins are predicted to function as initial ...
 51-371 1.49e-35

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: 132.82  E-value: 1.49e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818431575  51 TIVDQLGRTVEIPGKVDRIV---ALQHHTLDIMLELHAQDKLVGVLRDWESLLGSYAA---DVYPNIRNLETPGSISE-- 122
Cdd:cd01139    2 TVTDVAGRKVTLDAPVERVLlgeGRQLYALALLEGENPFARIVGWGGDLKKGDPDTYAkykEKFPEIADIPLIGSTYNgd 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818431575 123 LNVEAVASLKPDVVFVSN-----QIPKETLAQLEQLGIPVVGITLYVAdkeqastihpdlvnPDEAYTEGLKqainLIGQ 197
Cdd:cd01139   82 FSVEKVLTLKPDLVILNIwakttAEESGILEKLEQAGIPVVFVDFRQK--------------PLKNTTPSMR----LLGK 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818431575 198 ITGTENKAAELWNYVVSNRAIVSEHLSTVPEQdRIKVYM------ANENMYTYGTGKYvGVAMAKAGARNVAETIKG--Y 269
Cdd:cd01139  144 ALGREERAEEFIEFYQERIDRIRDRLAKINEP-KPKVFIelgaggPEECCSTYGNGNW-GELVDAAGGDNIADGLIPgtS 221

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818431575 270 KQVSVEQVTAWNPEVIFV--------------------QSRYASVLDEIRGDKAWAAIDAVKNGKLIIApdytkpW--GN 327
Cdd:cd01139  222 GELNAEYVIAANPEIIIAtggnwakdpsgvslgpdgttADAKESLLRALLKRPGWSSLQAVKNGRVYAL------WhqFY 295

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 818431575 328 PAPESMALGEIwLAKTLYPDAFKDVDLNAMVQHFYKTFYGIEYK 371
Cdd:cd01139  296 RSPYNFVALEA-FAKWLYPELFKDLDPEATLQEFHRQFLPVDYS 338
YvrC cd01143
Periplasmic binding protein YvrC. These proteins are predicted to function as initial ...
 68-287 4.94e-30

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: 113.91  E-value: 4.94e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818431575  68 RIVALQHHTLDIMLELHAQDKLVGVlrdwesllGSYaaDVYP-NIRNLETPGSISELNVEAVASLKPDVVFVSNQIPKET 146
Cdd:cd01143    5 RIVSLSPSITEILFALGAGDKIVGV--------DTY--SNYPkEVRKKPKVGSYSNPNVEKIVALKPDLVIVSSSSLAEL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818431575 147 LAQLEQLGIPVVgitlyvadkeqastihpdLVNPDEAYTEGLKQaINLIGQITGTENKAAELwnyVVSNRAIVSEHLSTV 226
Cdd:cd01143   75 LEKLKDAGIPVV------------------VLPAASSLDEIYDQ-IELIGKITGAEEEAEKL---VKEMKQKIDKVKDKG 132

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 818431575 227 PEQDRIKVY--MANENMYTYGTGKYVGVAMAKAGARNVAETIKGYKQVSVEQVTAWNPEVIFV 287
Cdd:cd01143  133 KTIKKSKVYieVSLGGPYTAGKNTFINELIRLAGAKNIAADSGGWPQVSPEEILKANPDVIIL 195
ChuT COG4558
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism] ...
 68-320 4.23e-27

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


Pssm-ID: 443619 [Multi-domain]  Cd Length: 285  Bit Score: 108.36  E-value: 4.23e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818431575  68 RIVALQHHTLDIMLELHAQDKLVGvlRDWESLLGSYAADVyPNIrnletpGSISELNVEAVASLKPDVVFVSNQI-PKET 146
Cdd:COG4558   29 RIVSLGGSVTEIVYALGAGDRLVG--VDTTSTYPAAAKAL-PDV------GYMRQLSAEGILSLKPTLVLASEGAgPPEV 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818431575 147 LAQLEQLGIPVVGItlyvadkeqastihpdlvnpDEAYT-EGLKQAINLIGQITGTENKAAELWNYVVSNRAIVSEHLST 225
Cdd:COG4558  100 LDQLRAAGVPVVVV--------------------PAAPSlEGVLAKIRAVAAALGVPEAGEALAARLEADLAALAARVAA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818431575 226 VPEQDRIKVYMANENM--YTYGTGKYVGVAMAKAGARNVAETIKGYKQVSVEQVTAWNPEVIFVQSR-YASV--LDEIRG 300
Cdd:COG4558  160 IGKPPRVLFLLSRGGGrpMVAGRGTAADALIRLAGGVNAAAGFEGYKPLSAEALIAAAPDVILVMTRgLESLggVDGLLA 239

                        250       260
                 ....*....|....*....|
gi 818431575 301 DKAWAAIDAVKNGKLIIAPD 320
Cdd:COG4558  240 LPGLAQTPAGKNKRIVAMDD 259
Peripla_BP_2 pfam01497
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ...
 70-321 1.38e-26

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: 105.91  E-value: 1.38e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818431575   70 VALQHHTLDIMLELHAQDKLVGVlrdwesllGSYAADVYPNIRNLETP--GSISELNVEAVASLKPDVVFVSNQIPKETL 147
Cdd:pfam01497   1 AALSPAYTEILYALGATDSIVGV--------DAYTRDPLKADAVAAIVkvGAYGEINVERLAALKPDLVILSTGYLTDEA 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818431575  148 AQLEQLGIPVVGitlyvadkeqastihpdlVNPDEAYtEGLKQAINLIGQITGTENKAAELWNYVVSN-RAIVSEhlstV 226
Cdd:pfam01497  73 EELLSLIIPTVI------------------FESSSTG-ESLKEQIKQLGELLGLEDEAEELVAEIDSAlAAAKKA----V 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818431575  227 PEQDRIKVYM---ANENMYTY-GTGKYVGVAMAKAGARNVAETI--KGYKQVSVEQVTAWNPEVIFVQSR---YASVLDE 297
Cdd:pfam01497 130 PSLTRKPVLVfggADGGGYVVaGSNTYIGDLLRILGIENIAAELsgSEYAPISFEAILSSNPDVIIVSGRdsfTKTGPEF 209

                         250       260
                  ....*....|....*....|....
gi 818431575  298 IRGDKAWAAIDAVKNGKLIIAPDY 321
Cdd:pfam01497 210 VAANPLWAGLPAVKNGRVYTLPSD 233
FecB COG4594
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and ...
 30-320 2.34e-24

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


Pssm-ID: 443650 [Multi-domain]  Cd Length: 316  Bit Score: 101.54  E-value: 2.34e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818431575  30 TAADNTQAGEQQPAPSAKPTYTIVDQLGrTVEIPGKVDRIVALQHHTLDIMLEL----------HAQDKLVGVLRDwesL 99
Cdd:COG4594   17 LAACGSSSSDSSSSEAAAGARTVKHAMG-ETTIPGTPKRVVVLEWSFADALLALgvtpvgiaddNDYDRWVPYLRD---L 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818431575 100 LGSYAaDVypnirnletpGSISELNVEAVASLKPDVVFVSNQIPKETLAQLEQLgipvvgitlyvadkeqASTIHpdLVN 179
Cdd:COG4594   93 IKGVT-SV----------GTRSQPNLEAIAALKPDLIIADKSRHEAIYDQLSKI----------------APTVL--FKS 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818431575 180 PDEAYTEGLKQAiNLIGQITGTENKAaelwnyvvsnRAIVSEHLSTVPEQ-DRIKVYMANEN----------MYTYGTGK 248
Cdd:COG4594  144 RNGDYQENLESF-KTIAKALGKEEEA----------EAVLADHDQRIAEAkAKLAAADKGKKvavgqfradgLRLYTPNS 212

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 818431575 249 YVGVAMAKAGARNVAETIK----GYKQVSVEQVTAWNPEVIFV-QSRYASVLDEIRGDKAWAAIDAVKNGKLIIAPD 320
Cdd:COG4594  213 FAGSVLAALGFENPPKQSKdngyGYSEVSLEQLPALDPDVLFIaTYDDPSILKEWKNNPLWKNLKAVKNGRVYEVDG 289
HutB cd01149
Hemin binding protein HutB. These proteins have been shown to function as initial receptors ...
 66-290 3.47e-23

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: 96.57  E-value: 3.47e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818431575  66 VDRIVALQHHTLDIMLELHAQDKLVGvlRDWESllgsyaadVYP-NIRNLETPGSISELNVEAVASLKPDVVFVSNQI-P 143
Cdd:cd01149    1 PERIVSLGGSVTEIVYALGAGDRLVG--VDSTS--------TYPeAAAKLPDVGYMRQLSAEGVLSLKPTLVIASDEAgP 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818431575 144 KETLAQLEQLGIPVVgitlyvadkeqastihpdlVNPDEAYTEGLKQAINLIGQITGTENKAAELWNYVVSNRAIVSEHL 223
Cdd:cd01149   71 PEALDQLRAAGVPVV-------------------TVPSTPTLDGLLTKIRQVAQALGVPEKGEALAQEVRQRLAALRKTV 131

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 818431575 224 STVPEQDRIKVYMANEN--MYTYGTGKYVGVAMAKAGARNVAETIKGYKQVSVEQVTAWNPEVIFVQSR 290
Cdd:cd01149  132 AAHKKPPRVLFLLSHGGgaAMAAGRNTAADAIIALAGAVNAAAGFRGYKPLSAEALIAAQPDVILVMSR 200
BtuF cd01144
Cobalamin binding protein BtuF. These proteins have been shown to function as initial ...
 68-336 4.26e-23

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: 96.60  E-value: 4.26e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818431575  68 RIVALQHHTLDIMLELHAQDKLVGVLrDWesllgsyaaDVYP-NIRNLETPGSISELNVEAVASLKPDVVFVSNQI-PKE 145
Cdd:cd01144    2 RIVSLAPSATELLYALGLGDQLVGVT-DY---------CDYPpEAKKLPRVGGFYQLDLERVLALKPDLVIAWDDCnVCA 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818431575 146 TLAQLEQLGIPVVgitlyvadkeqaSTIHPDLvnpdeaytEGLKQAINLIGQITGTENKAAELwnyVVSNRAIVSEHLST 225
Cdd:cd01144   72 VVDQLRAAGIPVL------------VSEPQTL--------DDILADIRRLGTLAGRPARAEEL---AEALRRRLAALRKQ 128

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818431575 226 VPEQDRIKVY--------MAnenmytyGTGKYVGVAMAKAGARNVAETI-KGYKQVSVEQVTAWNPEVIFVQSRYASVLD 296
Cdd:cd01144  129 YASKPPPRVFyqewidplMT-------AGGDWVPELIALAGGVNVFADAgERSPQVSWEDVLAANPDVIVLSPCGFGFTP 201

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 818431575 297 EI-RGDKAWAAIDAVKNGKLIIAPDytkPWGNPAPESMALG 336
Cdd:cd01144  202 AIlRKEPAWQALPAVRNGRVYAVDG---NWYFRPSPRLVDG 239
TroA_a cd01148
Metal binding protein TroA_a. These proteins are predicted to function as initial receptors ...
 52-334 1.44e-22

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: 95.87  E-value: 1.44e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818431575  52 IVDQLGRTVEIPGKVDRIVALQHHTLDIMLELHAQDKLVGV----LRDWESLLGSYA-----ADVYPnirnletpgsise 122
Cdd:cd01148    4 TVENCGRSVTFDKAPQRVVSNDQNTTEMMLALGLQDRMVGTagidNKDLPELKAKYDkvpelAKKYP------------- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818431575 123 lNVEAVASLKPDVVFV--SNQIPKE---TLAQLEQLGIPVVGITLYVADKEQASTIhpdlvnpDEAYTEglkqaINLIGQ 197
Cdd:cd01148   71 -SKETVLAARPDLVFGgwSYGFDKGglgTPDSLAELGIKTYILPESCGQRRGEATL-------DDVYND-----IRNLGK 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818431575 198 ITGTENKAAElwnYVVSNRAIVSEHLSTVP-EQDRIKVY---MANENMYTYGTGKYVGVAMAKAGARNVAETIK-GYKQV 272
Cdd:cd01148  138 IFDVEDRADK---LVADLKARLAEISAKVKgDGKKVAVFvydSGEDKPFTSGRGGIPNAIITAAGGRNVFADVDeSWTTV 214

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818431575 273 SVEQVTAWNPEVIFV-----QSRYASVLDEIRGDKAWAAIDAVKNGKLIIAP--DYTKPWGNP-APESMA 334
Cdd:cd01148  215 SWETVIARNPDVIVIidygdQNAAEQKIKFLKENPALKNVPAVKNNRFIVLPlaEATPGIRNVdAIEKLA 284
FatB cd01140
Siderophore binding protein FatB. These proteins have been shown to function as ABC-type ...
 59-319 2.29e-22

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: 95.02  E-value: 2.29e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818431575  59 TVEIPGKVDRIVALQHHTLDIMLELHAqdKLVGVLRDWE--SLLGSYAADVYPNIrnletpGSISELNVEAVASLKPDVV 136
Cdd:cd01140    5 ETKVPKNPEKVVVFDVGALDTLDALGV--KVVGVPKSSTlpEYLKKYKDDKYANV------GTLFEPDLEAIAALKPDLI 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818431575 137 FVSNQipkeTLAQLEQLgipvvgitlyvadKEQASTIHPDlVNPDEaYTEGLKQAINLIGQITGTENKAAELwnyVVSNR 216
Cdd:cd01140   77 IIGGR----LAEKYDEL-------------KKIAPTIDLG-ADLKN-YLESVKQNIETLGKIFGKEEEAKEL---VAEID 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818431575 217 AIVSEHLSTVPEQDRIKVYMANE-NMYTYGTGKYVGVAMAKAGARNVAETIKG---YKQVSVEQVTAWNPEVIFVQSRYA 292
Cdd:cd01140  135 ASIAEAKSAAKGKKKALVVLVNGgKLSAFGPGSRFGWLHDLLGFEPADENIKAsshGQPVSFEYILEANPDWLFVIDRGA 214

                        250       260       270
                 ....*....|....*....|....*....|...
gi 818431575 293 SVLDEIRGDKA------WAAIDAVKNGKLIIAP 319
Cdd:cd01140  215 AIGAEGSSAKEvldndlVKNTTAWKNGKVIYLD 247
CeuA COG4607
ABC-type enterochelin transport system, periplasmic component [Inorganic ion transport and ...
 23-319 2.42e-19

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


Pssm-ID: 443657 [Multi-domain]  Cd Length: 310  Bit Score: 87.54  E-value: 2.42e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818431575  23 GCGNGTNTAAdntqageqqpAPSAKPTYTIVDQLGrTVEIPGKVDRIVALQHHTLDIMLELHAqdKLVGVLRD-WESLLG 101
Cdd:COG4607   19 ACGSSSAAAA----------SAAAAETVTVEHALG-TVEVPKNPKRVVVFDNGALDTLDALGV--EVAGVPKGlLPDYLS 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818431575 102 SYAADVYPNIrnletpGSISELNVEAVASLKPDVVFVSNQipkeTLAQLEQLgipvvgitlyvadKEQASTIhpDLVNPD 181
Cdd:COG4607   86 KYADDKYANV------GTLFEPDLEAIAALKPDLIIIGGR----SAKKYDEL-------------SKIAPTI--DLTVDG 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818431575 182 EAYTEGLKQAINLIGQITGTENKAAELwnyVVSNRAIVSEHLSTVPEQDRIKVYMANE-NMYTYGTGKYVGVAMAKAGAR 260
Cdd:COG4607  141 EDYLESLKRNTETLGEIFGKEDEAEEL---VADLDAKIAALKAAAAGKGTALIVLTNGgKISAYGPGSRFGPIHDVLGFK 217

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 818431575 261 NVAETIKGYK---QVSVEQVTAWNPEVIFVQSRYASVLDEIRGDK------AWAAIDAVKNGKLIIAP 319
Cdd:COG4607  218 PADEDIEASThgqAISFEFIAEANPDWLFVIDRDAAIGGEGPAAKqvldneLVKQTTAWKNGQIVYLD 285
btuF PRK09534
corrinoid ABC transporter substrate-binding protein; Reviewed
 37-334 3.10e-19

corrinoid ABC transporter substrate-binding protein; Reviewed


Pssm-ID: 236552 [Multi-domain]  Cd Length: 359  Bit Score: 88.04  E-value: 3.10e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818431575  37 AGEQQPAPSAKPT---------YTIVDQLGRTVEIPGKVDRIVALQHHTLDIMLELHAQDKLVGVLRdwesllgsYAADV 107
Cdd:PRK09534  22 GGALAPAPAAQHAdadracsfpVTETDATGTEITLDERPERVVTLNPSAAQTMWELGARDRVVGVTQ--------YASYL 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818431575 108 yPNI--RNLETPGSISELNVEAVASLKPDVVFVSNQIPKETLAQLEQLGIPVVGITLyvadkeqASTIhpdlvnpdeayt 185
Cdd:PRK09534  94 -DGAeeRTNVSGGQPFGVNVEAVVGLDPDLVLAPNAVAGDTVTRLREAGITVFHFPA-------ATSI------------ 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818431575 186 EGLKQAINLIGQITGTENKAAELWNYVVSNRAIVSEHLSTVpeQDRIKVYMANENMYTYGTGKYVGVAMAKAGARNVA-- 263
Cdd:PRK09534 154 EDVAEKTATIGRLTGNCEAAAETNAEMRDRVDAVEDRTADV--DDRPRVLYPLGDGYTAGGNTFIGALIEAAGGHNVAad 231

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 818431575 264 ETIKGYKQVSVEQVTAWNPEVIFVQSRYASVLDEirgdKAWAAIDAVKNGKLIIAPdyTKPWGNPAP---ESMA 334
Cdd:PRK09534 232 ATTDGYPQLSEEVIVQQDPDVIVVATASALVAET----EPYASTTAGETGNVVTVN--VNHINQPAPrivESMA 299
TroA-like cd00636
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function ...
 68-236 8.36e-17

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: 76.44  E-value: 8.36e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818431575  68 RIVALQHHTLDIMLELHAQDKLVGVLRDWesllgSYAADVYPNIRNLETPGSISELNVEAVASLKPDVVFVSNQIPKETL 147
Cdd:cd00636    2 RVVALDPGATELLLALGGDDKPVGVADPS-----GYPPEAKALLEKVPDVGHGYEPNLEKIAALKPDLIIANGSGLEAWL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818431575 148 AQLEQLGIPVVgitlyVADKEQASTIhpdlvnpdeaytEGLKQAINLIGQITGTENKAAELWNYVVSNRAIVSEHLSTVP 227
Cdd:cd00636   77 DKLSKIAIPVV-----VVDEASELSL------------ENIKESIRLIGKALGKEENAEELIAELDARLAELRAKLAKIP 139


                 ....*....
gi 818431575 228 EQDRIKVYM 236
Cdd:cd00636  140 KKKVSLVVG 148
FhuD cd01146
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ...
 68-328 4.94e-14

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: 71.16  E-value: 4.94e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818431575  68 RIVALQHHTLDIMLELHAqdKLVGVlRDWESLL--GSYAADVYPNIRNLetpGSISELNVEAVASLKPDVVFVSNQIPKE 145
Cdd:cd01146    5 RIVALDWGALETLLALGV--KPVGV-ADTAGYKpwIPEPALPLEGVVDV---GTRGQPNLEAIAALKPDLILGSASRHDE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818431575 146 TLAQLEQLGiPVVGITLYVADKEqastihpdlvnpdeaytegLKQAINLIGQITGTENKAAELWNYVvsnRAIVSEHLST 225
Cdd:cd01146   79 IYDQLSQIA-PTVLLDSSPWLAE-------------------WKENLRLIAKALGKEEEAEKLLAEY---DQRLAELRQK 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818431575 226 VPEQDRIKV----YMANENMYTYGTGKYVGVAMAKAGARNVAE----TIKGYKQVSVEQVTAWNPEVIFVQSRY-ASVLD 296
Cdd:cd01146  136 LPDKGPKPVsvvrFSDAGSIRLYGPNSFAGSVLEDLGLQNPWAqettNDSGFATISLERLAKADADVLFVFTYEdEELAQ 215

                        250       260       270
                 ....*....|....*....|....*....|..
gi 818431575 297 EIRGDKAWAAIDAVKNGKLIIAPDYTKPWGNP 328
Cdd:cd01146  216 ALQANPLWQNLPAVKNGRVYVVDDVWWFFGGG 247
FeuA cd01138
Periplasmic binding protein FeuA. These proteins have predicted to function as initial ...
 58-317 3.14e-12

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: 65.82  E-value: 3.14e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818431575  58 RTVEIPGKVDRIVALQHHTldiMLELHAQDKLVGVlRDWESLLGSYAADVYPNIrnletPGSISELNVEAVASLKPDVVF 137
Cdd:cd01138    1 GEVEIPAKPKRIVALSGET---EGLALLGIKPVGA-ASIGGKNPYYKKKTLAKV-----VGIVDEPNLEKVLELKPDLII 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818431575 138 VSNQIPKEtlaqLEQLgipvvgitlyvadkeqaSTIHPDLVNPDEA--YTEGLKQainlIGQITGTENKAAE-LWNYVVS 214
Cdd:cd01138   72 VSSKQEEN----YEKL-----------------SKIAPTVPVSYNSsdWEEQLKE----IGKLLNKEDEAEKwLADYKQK 126

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818431575 215 NRAiVSEHLSTVPEQDR-IKVYMANENMYTYGTGKYVGVAMAKAG----ARNVAETI---KGYKQVSVEQVTAWNPEVIF 286
Cdd:cd01138  127 AKE-AKEKIKKKLGNDKsVAVLRGRKQIYVFGEDGRGGGPILYADlglkAPEKVKEIedkPGYAAISLEVLPEFDADYIF 205

                        250       260       270
                 ....*....|....*....|....*....|..
gi 818431575 287 VQ-SRYASVLDEIRGDKAWAAIDAVKNGKLII 317
Cdd:cd01138  206 LLfFTGPEAKADFESLPIWKNLPAVKNNHVYI 237
TroA_d cd01141
Periplasmic binding protein TroA_d. These proteins are predicted to function as initial ...
 57-260 2.76e-11

Periplasmic binding protein TroA_d. 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: 238561 [Multi-domain]  Cd Length: 186  Bit Score: 62.05  E-value: 2.76e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818431575  57 GRTVEIPgkVDRIVALQHHTLDIMLELHAQDKLVGVLRdwesllgsYAADVY-PNIRNL--ETPGSISELNVEAVASLKP 133
Cdd:cd01141    1 AKTIKVP--PKRIVVLSPTHVDLLLALDKADKIVGVSA--------SAYDLNtPAVKERidIQVGPTGSLNVELIVALKP 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818431575 134 DVVFVSNQIPKETLAQ-LEQLGIPVVgitlyvadkeqastihpdlVNPDEAYTEGLKQAINLIGQITG--TENKAAELWN 210
Cdd:cd01141   71 DLVILYGGFQAQTILDkLEQLGIPVL-------------------YVNEYPSPLGRAEWIKFAAAFYGvgKEDKADEAFA 131

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 818431575 211 YVVSN-RAIVSehLSTVPEQDRIKVYM-ANENMYTYGTGKYVGVAMAKAGAR 260
Cdd:cd01141  132 QIAGRyRDLAK--KVSNLNKPTVAIGKpVKGLWYMPGGNSYVAKMLRDAGGR 181
fecB PRK11411
iron-dicitrate transporter substrate-binding subunit; Provisional
 51-316 1.96e-09

iron-dicitrate transporter substrate-binding subunit; Provisional


Pssm-ID: 183123 [Multi-domain]  Cd Length: 303  Bit Score: 58.15  E-value: 1.96e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818431575  51 TIVDQLGrTVEIPGKVDRIVALQHHTLDIMlelhAQdklVGVlrdweSLLGsyAAD------VYPNIRNLETP----GSI 120
Cdd:PRK11411  25 TVQDEQG-TFTLEKTPQRIVVLELSFVDAL----AA---VGV-----SPVG--VADdndakrILPEVRAHLKPwqsvGTR 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818431575 121 SELNVEAVASLKPDvvfvsnqipketlaqleqlgipvvgitLYVADKEQASTIHPDL--VNP-------DEAYTEGLKQA 191
Cdd:PRK11411  90 SQPSLEAIAALKPD---------------------------LIIADSSRHAGVYIALqkIAPtlllksrNETYQENLQSA 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818431575 192 iNLIGQITGtenKAAELWNYVVSNRAIVSEHLSTVPEQDRIKVYMANEN-MYTYGTGKYVGVAMAKAGAR--NVAETIKG 268
Cdd:PRK11411 143 -AIIGEVLG---KKREMQARIEQHKERMAQFASQLPKGTRVAFGTSREQqFNLHSPESYTGSVLAALGLNvpKAPMNGAA 218

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 818431575 269 YKQVSVEQVTAWNPEVIFV-QSRYASVLDEIRGDKAWAAIDAVKNGKLI 316
Cdd:PRK11411 219 MPSISLEQLLALNPDWLLVaHYRQESIVKRWQQDPLWQMLTAAKKQQVA 267
 
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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