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Conserved domains on  [gi|1821507750|ref|WP_165657228|]
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ABC transporter substrate-binding protein [Sutterella wadsworthensis]

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 ...
 59-297 2.99e-35

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 cd01146:

Pssm-ID: 469696 [Multi-domain]  Cd Length: 256  Bit Score: 128.17  E-value: 2.99e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821507750  59 IPQRPAVLQWDLLENLVGLGVKPAGACDISSWDTWVREPALPA-GIEDLGTRAEPNLERIAKLKPDVILIGPTQLD-LMP 136
Cdd:cd01146     2 KPQRIVALDWGALETLLALGVKPVGVADTAGYKPWIPEPALPLeGVVDVGTRGQPNLEAIAALKPDLILGSASRHDeIYD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821507750 137 VLATIAPVLLFSNYRADAPeneaetALKQFRELAKLFQREAAAEAEIARWFAQIDAYGDAIRKAFGfaPQIQVIRFSSLT 216
Cdd:cd01146    82 QLSQIAPTVLLDSSPWLAE------WKENLRLIAKALGKEEEAEKLLAEYDQRLAELRQKLPDKGP--KPVSVVRFSDAG 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821507750 217 TLFVYTPNAIADWVVRRMGMAQPLTRPAS-AYGLTQVRIRDLKNLtDAYVIYI---RPFAQEAKVMNSILWCATPFARKH 292
Cdd:cd01146   154 SIRLYGPNSFAGSVLEDLGLQNPWAQETTnDSGFATISLERLAKA-DADVLFVftyEDEELAQALQANPLWQNLPAVKNG 232


                  ....*
gi 1821507750 293 HVAPL 297
Cdd:cd01146   233 RVYVV 237
 
Name Accession Description Interval E-value
FhuD cd01146
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ...
 59-297 2.99e-35

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: 128.17  E-value: 2.99e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821507750  59 IPQRPAVLQWDLLENLVGLGVKPAGACDISSWDTWVREPALPA-GIEDLGTRAEPNLERIAKLKPDVILIGPTQLD-LMP 136
Cdd:cd01146     2 KPQRIVALDWGALETLLALGVKPVGVADTAGYKPWIPEPALPLeGVVDVGTRGQPNLEAIAALKPDLILGSASRHDeIYD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821507750 137 VLATIAPVLLFSNYRADAPeneaetALKQFRELAKLFQREAAAEAEIARWFAQIDAYGDAIRKAFGfaPQIQVIRFSSLT 216
Cdd:cd01146    82 QLSQIAPTVLLDSSPWLAE------WKENLRLIAKALGKEEEAEKLLAEYDQRLAELRQKLPDKGP--KPVSVVRFSDAG 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821507750 217 TLFVYTPNAIADWVVRRMGMAQPLTRPAS-AYGLTQVRIRDLKNLtDAYVIYI---RPFAQEAKVMNSILWCATPFARKH 292
Cdd:cd01146   154 SIRLYGPNSFAGSVLEDLGLQNPWAQETTnDSGFATISLERLAKA-DADVLFVftyEDEELAQALQANPLWQNLPAVKNG 232


                  ....*
gi 1821507750 293 HVAPL 297
Cdd:cd01146   233 RVYVV 237
FecB COG4594
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and ...
 20-297 5.26e-35

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


Pssm-ID: 443650 [Multi-domain]  Cd Length: 316  Bit Score: 128.88  E-value: 5.26e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821507750  20 FAAGSLGAASLPNFASNEKLAAVSGITIRDDLGEHVFQTIPQRPAVLQWDLLENLVGLGVKPAGACDISSWDTWVREPA- 98
Cdd:COG4594    12 LALLLLAACGSSSSDSSSSEAAAGARTVKHAMGETTIPGTPKRVVVLEWSFADALLALGVTPVGIADDNDYDRWVPYLRd 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821507750  99 LPAGIEDLGTRAEPNLERIAKLKPDVIlIGPTQL--DLMPVLATIAPVLLFSNYRADAPENeaetaLKQFRELAKLFQRE 176
Cdd:COG4594    92 LIKGVTSVGTRSQPNLEAIAALKPDLI-IADKSRheAIYDQLSKIAPTVLFKSRNGDYQEN-----LESFKTIAKALGKE 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821507750 177 AAAEAEIARWFAQIDAYGDAIRKAFGFApQIQVIRFSSlTTLFVYTPNAIADWVVRRMGMAQPLTR-PASAYGLTQVRIR 255
Cdd:COG4594   166 EEAEAVLADHDQRIAEAKAKLAAADKGK-KVAVGQFRA-DGLRLYTPNSFAGSVLAALGFENPPKQsKDNGYGYSEVSLE 243

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1821507750 256 DLKNLtDAYVIYIRPFAQEA---KVMNSILWCATPFARKHHVAPL 297
Cdd:COG4594   244 QLPAL-DPDVLFIATYDDPSilkEWKNNPLWKNLKAVKNGRVYEV 287
PRK10576 PRK10576
Fe(3+)-hydroxamate ABC transporter substrate-binding protein FhuD;
60-294 6.15e-23

Fe(3+)-hydroxamate ABC transporter substrate-binding protein FhuD;


Pssm-ID: 236719  Cd Length: 292  Bit Score: 96.23  E-value: 6.15e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821507750  60 PQRPAVLQWDLLENLVGLGVKPAGACDISSWDTWVREPALPAGIEDLGTRAEPNLERIAKLKPDVILI----GPTQldlm 135
Cdd:PRK10576   32 PNRIVALEWLPVELLLALGVTPYGVADTHNYRLWVSEPALPDSVIDVGLRTEPNLELLTQMKPSLILWsagyGPSP---- 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821507750 136 PVLATIAPVLLFSNYRADAPENEAETALkqfRELAKLFQReaaaEAEIARWFAQIDAYGDAIRKAFGFAPQIQVIRFSSL 215
Cdd:PRK10576  108 EKLARIAPGRGFAFSDGKKPLAVARKSL---VELAQRLNL----EAAAETHLAQFDDFIASAKPRLAGRGQRPLLLTSLI 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821507750 216 TT--LFVYTPNAIADWVVRRMGMAQPLTRPASAYGLTQVRIRDLKNLTDAYVIYirpF-----AQEAKVMNSILWCATPF 288
Cdd:PRK10576  181 DPrhALVFGPNSLFQEVLDELGIENAWQGETNFWGSTVVGIERLAAYKDADVIC---FdhgnsKDMQQLMATPLWQAMPF 257


                  ....*.
gi 1821507750 289 ARKHHV 294
Cdd:PRK10576  258 VRAGRF 263
Peripla_BP_2 pfam01497
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ...
 64-294 6.64e-11

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: 61.23  E-value: 6.64e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821507750  64 AVLQWDLLENLVGLGVKPAGACDISSWDTWVREPALPAGIEdLGTRAEPNLERIAKLKPDVILIG---PTQLDLMpVLAT 140
Cdd:pfam01497   1 AALSPAYTEILYALGATDSIVGVDAYTRDPLKADAVAAIVK-VGAYGEINVERLAALKPDLVILStgyLTDEAEE-LLSL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821507750 141 IAPVLLFsnyradAPENEAETALKQFRELAKLFQReaaaEAEIARWFAQIDAYGDAIRKAfgfAPQIQ---VIRFSSLTT 217
Cdd:pfam01497  79 IIPTVIF------ESSSTGESLKEQIKQLGELLGL----EDEAEELVAEIDSALAAAKKA---VPSLTrkpVLVFGGADG 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821507750 218 LFVYTPNAIADW--VVRRMGMAQpltrPASAYGLTQVRIRDLKNL--TDAYVIYIRPFAQEAK-----VMNSILWCATPF 288
Cdd:pfam01497 146 GGYVVAGSNTYIgdLLRILGIEN----IAAELSGSEYAPISFEAIlsSNPDVIIVSGRDSFTKtgpefVAANPLWAGLPA 221


                  ....*.
gi 1821507750 289 ARKHHV 294
Cdd:pfam01497 222 VKNGRV 227
 
Name Accession Description Interval E-value
FhuD cd01146
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ...
 59-297 2.99e-35

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: 128.17  E-value: 2.99e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821507750  59 IPQRPAVLQWDLLENLVGLGVKPAGACDISSWDTWVREPALPA-GIEDLGTRAEPNLERIAKLKPDVILIGPTQLD-LMP 136
Cdd:cd01146     2 KPQRIVALDWGALETLLALGVKPVGVADTAGYKPWIPEPALPLeGVVDVGTRGQPNLEAIAALKPDLILGSASRHDeIYD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821507750 137 VLATIAPVLLFSNYRADAPeneaetALKQFRELAKLFQREAAAEAEIARWFAQIDAYGDAIRKAFGfaPQIQVIRFSSLT 216
Cdd:cd01146    82 QLSQIAPTVLLDSSPWLAE------WKENLRLIAKALGKEEEAEKLLAEYDQRLAELRQKLPDKGP--KPVSVVRFSDAG 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821507750 217 TLFVYTPNAIADWVVRRMGMAQPLTRPAS-AYGLTQVRIRDLKNLtDAYVIYI---RPFAQEAKVMNSILWCATPFARKH 292
Cdd:cd01146   154 SIRLYGPNSFAGSVLEDLGLQNPWAQETTnDSGFATISLERLAKA-DADVLFVftyEDEELAQALQANPLWQNLPAVKNG 232


                  ....*
gi 1821507750 293 HVAPL 297
Cdd:cd01146   233 RVYVV 237
FecB COG4594
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and ...
 20-297 5.26e-35

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


Pssm-ID: 443650 [Multi-domain]  Cd Length: 316  Bit Score: 128.88  E-value: 5.26e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821507750  20 FAAGSLGAASLPNFASNEKLAAVSGITIRDDLGEHVFQTIPQRPAVLQWDLLENLVGLGVKPAGACDISSWDTWVREPA- 98
Cdd:COG4594    12 LALLLLAACGSSSSDSSSSEAAAGARTVKHAMGETTIPGTPKRVVVLEWSFADALLALGVTPVGIADDNDYDRWVPYLRd 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821507750  99 LPAGIEDLGTRAEPNLERIAKLKPDVIlIGPTQL--DLMPVLATIAPVLLFSNYRADAPENeaetaLKQFRELAKLFQRE 176
Cdd:COG4594    92 LIKGVTSVGTRSQPNLEAIAALKPDLI-IADKSRheAIYDQLSKIAPTVLFKSRNGDYQEN-----LESFKTIAKALGKE 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821507750 177 AAAEAEIARWFAQIDAYGDAIRKAFGFApQIQVIRFSSlTTLFVYTPNAIADWVVRRMGMAQPLTR-PASAYGLTQVRIR 255
Cdd:COG4594   166 EEAEAVLADHDQRIAEAKAKLAAADKGK-KVAVGQFRA-DGLRLYTPNSFAGSVLAALGFENPPKQsKDNGYGYSEVSLE 243

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1821507750 256 DLKNLtDAYVIYIRPFAQEA---KVMNSILWCATPFARKHHVAPL 297
Cdd:COG4594   244 QLPAL-DPDVLFIATYDDPSilkEWKNNPLWKNLKAVKNGRVYEV 287
PRK10576 PRK10576
Fe(3+)-hydroxamate ABC transporter substrate-binding protein FhuD;
60-294 6.15e-23

Fe(3+)-hydroxamate ABC transporter substrate-binding protein FhuD;


Pssm-ID: 236719  Cd Length: 292  Bit Score: 96.23  E-value: 6.15e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821507750  60 PQRPAVLQWDLLENLVGLGVKPAGACDISSWDTWVREPALPAGIEDLGTRAEPNLERIAKLKPDVILI----GPTQldlm 135
Cdd:PRK10576   32 PNRIVALEWLPVELLLALGVTPYGVADTHNYRLWVSEPALPDSVIDVGLRTEPNLELLTQMKPSLILWsagyGPSP---- 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821507750 136 PVLATIAPVLLFSNYRADAPENEAETALkqfRELAKLFQReaaaEAEIARWFAQIDAYGDAIRKAFGFAPQIQVIRFSSL 215
Cdd:PRK10576  108 EKLARIAPGRGFAFSDGKKPLAVARKSL---VELAQRLNL----EAAAETHLAQFDDFIASAKPRLAGRGQRPLLLTSLI 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821507750 216 TT--LFVYTPNAIADWVVRRMGMAQPLTRPASAYGLTQVRIRDLKNLTDAYVIYirpF-----AQEAKVMNSILWCATPF 288
Cdd:PRK10576  181 DPrhALVFGPNSLFQEVLDELGIENAWQGETNFWGSTVVGIERLAAYKDADVIC---FdhgnsKDMQQLMATPLWQAMPF 257


                  ....*.
gi 1821507750 289 ARKHHV 294
Cdd:PRK10576  258 VRAGRF 263
CeuA COG4607
ABC-type enterochelin transport system, periplasmic component [Inorganic ion transport and ...
 20-175 3.14e-18

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


Pssm-ID: 443657 [Multi-domain]  Cd Length: 310  Bit Score: 83.31  E-value: 3.14e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821507750  20 FAAGSLGAASlPNFASNEKLAAVSGITIRDDLGEHVFQTIPQRPAVLQWDLLENLVGLGVKPAGacdisswdtwVREPAL 99
Cdd:COG4607    12 AAALALAACG-SSSAAAASAAAAETVTVEHALGTVEVPKNPKRVVVFDNGALDTLDALGVEVAG----------VPKGLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821507750 100 PA--------GIEDLGTRAEPNLERIAKLKPDVILIGPTQLDLMPVLATIAPVLLFSnyrADaPENEAETALKQFRELAK 171
Cdd:COG4607    81 PDylskyaddKYANVGTLFEPDLEAIAALKPDLIIIGGRSAKKYDELSKIAPTIDLT---VD-GEDYLESLKRNTETLGE 156


                  ....
gi 1821507750 172 LFQR 175
Cdd:COG4607   157 IFGK 160
FatB cd01140
Siderophore binding protein FatB. These proteins have been shown to function as ABC-type ...
 49-200 2.43e-15

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: 74.60  E-value: 2.43e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821507750  49 DDLGEHVFQTIPQRPAVLQWDLLENLVGLGVKPAGACDISSWDTWVREpALPAGIEDLGTRAEPNLERIAKLKPDVILIG 128
Cdd:cd01140     1 HALGETKVPKNPEKVVVFDVGALDTLDALGVKVVGVPKSSTLPEYLKK-YKDDKYANVGTLFEPDLEAIAALKPDLIIIG 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1821507750 129 PTQLDLMPVLATIAPVLLFSnyrADaPENEAETALKQFRELAKLFQREAAAEAEIarwfAQIDAYGDAIRKA 200
Cdd:cd01140    80 GRLAEKYDELKKIAPTIDLG---AD-LKNYLESVKQNIETLGKIFGKEEEAKELV----AEIDASIAEAKSA 143
FepB COG0614
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ...
 62-297 6.92e-14

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


Pssm-ID: 440379 [Multi-domain]  Cd Length: 264  Bit Score: 70.41  E-value: 6.92e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821507750  62 RPAVLQWDLLENLVGLGVKPAGACdISSWDTWVREPALPAGIEDLGTRAEPNLERIAKLKPDVILIGPTQL--DLMPVLA 139
Cdd:COG0614     2 RIVSLSPSATELLLALGAGDRLVG-VSDWGYCDYPELELKDLPVVGGTGEPNLEAILALKPDLVLASSSGNdeEDYEQLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821507750 140 TI-APVLLFsnyradaPENEAETALKQFRELAKLFQReaaaEAEIARWFAQIDAYGDAIRKAF-GFAPQIQV-IRFSSLT 216
Cdd:COG0614    81 KIgIPVVVL-------DPRSLEDLYESIRLLGELLGR----EERAEALIAEYEARLAAVRARLaGAEERPTVlYEIWSGD 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821507750 217 TLFVYTPNAIADWVVRRMGM---AQPLTRPASAYGLTQVRIRDlknlTDAYVIYIRPFAQE------AKVMNSILWCATP 287
Cdd:COG0614   150 PLYTAGGGSFIGELLELAGGrnvAADLGGGYPEVSLEQVLALD----PDVIILSGGGYDAEtaeealEALLADPGWQSLP 225

                         250
                  ....*....|
gi 1821507750 288 FARKHHVAPL 297
Cdd:COG0614   226 AVKNGRVYVV 235
fecB PRK11411
iron-dicitrate transporter substrate-binding subunit; Provisional
 39-295 2.14e-13

iron-dicitrate transporter substrate-binding subunit; Provisional


Pssm-ID: 183123 [Multi-domain]  Cd Length: 303  Bit Score: 69.32  E-value: 2.14e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821507750  39 LAAVSGITIRDDLGEHVFQTIPQRPAVLQWDLLENLVGLGVKPAGACDISSWD---TWVREPALPAgiEDLGTRAEPNLE 115
Cdd:PRK11411   18 SSHAFAVTVQDEQGTFTLEKTPQRIVVLELSFVDALAAVGVSPVGVADDNDAKrilPEVRAHLKPW--QSVGTRSQPSLE 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821507750 116 RIAKLKPDVILIGPTQ-LDLMPVLATIAPVLLFSNYRADAPENeAETALKQFRELAK---LFQREAAAEAEIARWFAQID 191
Cdd:PRK11411   96 AIAALKPDLIIADSSRhAGVYIALQKIAPTLLLKSRNETYQEN-LQSAAIIGEVLGKkreMQARIEQHKERMAQFASQLP 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821507750 192 AyGDAIrkAFGFAPQIQvirFSslttlfVYTPNAIADWVVRRMGMAQPLTRPASAyGLTQVRIRDLKNLTDAYVIyIRPF 271
Cdd:PRK11411  175 K-GTRV--AFGTSREQQ---FN------LHSPESYTGSVLAALGLNVPKAPMNGA-AMPSISLEQLLALNPDWLL-VAHY 240

                         250       260
                  ....*....|....*....|....*..
gi 1821507750 272 AQEAKV---MNSILWCATPFARKHHVA 295
Cdd:PRK11411  241 RQESIVkrwQQDPLWQMLTAAKKQQVA 267
TroA-like cd00636
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function ...
 61-175 8.14e-12

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: 62.19  E-value: 8.14e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821507750  61 QRPAVLQWDLLENL--VGLGVKPAGACDISSWDTWVREPalPAGIEDLGTRAEPNLERIAKLKPDVILIGPTQLD-LMPV 137
Cdd:cd00636     1 KRVVALDPGATELLlaLGGDDKPVGVADPSGYPPEAKAL--LEKVPDVGHGYEPNLEKIAALKPDLIIANGSGLEaWLDK 78

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1821507750 138 LATIA-PVLLFSNYRADAPENeaetALKQFRELAKLFQR 175
Cdd:cd00636    79 LSKIAiPVVVVDEASELSLEN----IKESIRLIGKALGK 113
Peripla_BP_2 pfam01497
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ...
 64-294 6.64e-11

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: 61.23  E-value: 6.64e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821507750  64 AVLQWDLLENLVGLGVKPAGACDISSWDTWVREPALPAGIEdLGTRAEPNLERIAKLKPDVILIG---PTQLDLMpVLAT 140
Cdd:pfam01497   1 AALSPAYTEILYALGATDSIVGVDAYTRDPLKADAVAAIVK-VGAYGEINVERLAALKPDLVILStgyLTDEAEE-LLSL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821507750 141 IAPVLLFsnyradAPENEAETALKQFRELAKLFQReaaaEAEIARWFAQIDAYGDAIRKAfgfAPQIQ---VIRFSSLTT 217
Cdd:pfam01497  79 IIPTVIF------ESSSTGESLKEQIKQLGELLGL----EDEAEELVAEIDSALAAAKKA---VPSLTrkpVLVFGGADG 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821507750 218 LFVYTPNAIADW--VVRRMGMAQpltrPASAYGLTQVRIRDLKNL--TDAYVIYIRPFAQEAK-----VMNSILWCATPF 288
Cdd:pfam01497 146 GGYVVAGSNTYIgdLLRILGIEN----IAAELSGSEYAPISFEAIlsSNPDVIIVSGRDSFTKtgpefVAANPLWAGLPA 221


                  ....*.
gi 1821507750 289 ARKHHV 294
Cdd:pfam01497 222 VKNGRV 227
FeuA cd01138
Periplasmic binding protein FeuA. These proteins have predicted to function as initial ...
 58-294 2.76e-10

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: 59.65  E-value: 2.76e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821507750  58 TIPQRP--AVLQWDLLENLVGLGVKPAGAcdiSSWDTWVrePALPAGIEDLGT--RAEPNLERIAKLKPDVILIGPTQLD 133
Cdd:cd01138     4 EIPAKPkrIVALSGETEGLALLGIKPVGA---ASIGGKN--PYYKKKTLAKVVgiVDEPNLEKVLELKPDLIIVSSKQEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821507750 134 LMPVLATIAPVLLFSnyradapeNEAETALKQFRELAKLFQREAAAEAEIARWFAQIDAYGDAIRKAFGfaPQIQVIRFS 213
Cdd:cd01138    79 NYEKLSKIAPTVPVS--------YNSSDWEEQLKEIGKLLNKEDEAEKWLADYKQKAKEAKEKIKKKLG--NDKSVAVLR 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821507750 214 SLTTLFVYTpnaiaDWVVR-------RMGMAQPLTRPASAYGLTQVRIrDLKNLTDA---YVIYIRPFAQEAKV--MNSI 281
Cdd:cd01138   149 GRKQIYVFG-----EDGRGggpilyaDLGLKAPEKVKEIEDKPGYAAI-SLEVLPEFdadYIFLLFFTGPEAKAdfESLP 222

                         250
                  ....*....|...
gi 1821507750 282 LWCATPFARKHHV 294
Cdd:cd01138   223 IWKNLPAVKNNHV 235
TroA_e cd01142
Periplasmic binding protein TroA_e. These proteins are predicted to function as initial ...
 46-126 3.24e-03

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: 38.49  E-value: 3.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821507750  46 TIRDDLGEHVfqTIP---QRPAVLQWDLLENLVGLGvkpAGACDISSWDTWVREPALP------AGIEDLGTRAEPNLER 116
Cdd:cd01142     9 TITDMAGRKV--TIPdevKRIAALWGAGNAVVAALG---GGKLIVATTSTVQQEPWLYrlapslENVATGGTGNDVNIEE 83

                          90
                  ....*....|
gi 1821507750 117 IAKLKPDVIL 126
Cdd:cd01142    84 LLALKPDVVI 93
TroA_d cd01141
Periplasmic binding protein TroA_d. These proteins are predicted to function as initial ...
 60-199 9.52e-03

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: 36.63  E-value: 9.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821507750  60 PQRPAVLQWDLLENLVGLGV--KPAGacdISSWDTWVREPALPAGIE-DLGTRAEPNLERIAKLKPDVILI--GPTQLDL 134
Cdd:cd01141     8 PKRIVVLSPTHVDLLLALDKadKIVG---VSASAYDLNTPAVKERIDiQVGPTGSLNVELIVALKPDLVILygGFQAQTI 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1821507750 135 MPVLATIA-PVLLFSNYRADAPENEAETALKQFRELAKLFQreaaaeaeIARWFAQIDAYGDAIRK 199
Cdd:cd01141    85 LDKLEQLGiPVLYVNEYPSPLGRAEWIKFAAAFYGVGKEDK--------ADEAFAQIAGRYRDLAK 142
 
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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