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Conserved domains on  [gi|1410802043|emb|SPX83327|]
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Probable siderophore-binding lipoprotein yfiY precursor [Listeria innocua]

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 ...
 48-289 1.10e-68

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 cd01138:

Pssm-ID: 469696 [Multi-domain]  Cd Length: 248  Bit Score: 214.12  E-value: 1.10e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410802043  48 RKVEVPTTPKRIVALQNVSEMEIL-GVKPVGTTDYYITT--YPKATKGTESVGNDKPSIEKIANLKPDLIIISDYQKDLL 124
Cdd:cd01138     1 GEVEIPAKPKRIVALSGETEGLALlGIKPVGAASIGGKNpyYKKKTLAKVVGIVDEPNLEKVLELKPDLIIVSSKQEENY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410802043 125 ENLEKVAP-VYISHFGDTPDKQLSNIANLLNKKSEKEKWDKDYAKSSKEAKATLKDAGveNEKAAVIQFYG-KEIYVHDA 202
Cdd:cd01138    81 EKLSKIAPtVPVSYNSSDWEEQLKEIGKLLNKEDEAEKWLADYKQKAKEAKEKIKKKL--GNDKSVAVLRGrKQIYVFGE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410802043 203 kvfDGLFSGAGFTPTDGAKANKETK---------AISSEAIPEYAagADRLFILMPtDGNEDSVNEMLNGVWKDIPAVKK 273
Cdd:cd01138   159 ---DGRGGGPILYADLGLKAPEKVKeiedkpgyaAISLEVLPEFD--ADYIFLLFF-TGPEAKADFESLPIWKNLPAVKN 232

                         250
                  ....*....|....*.
gi 1410802043 274 NQVYKVDNtkWSDYSA 289
Cdd:cd01138   233 NHVYIVDA--WVFYFA 246
 
Name Accession Description Interval E-value
FeuA cd01138
Periplasmic binding protein FeuA. These proteins have predicted to function as initial ...
 48-289 1.10e-68

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: 214.12  E-value: 1.10e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410802043  48 RKVEVPTTPKRIVALQNVSEMEIL-GVKPVGTTDYYITT--YPKATKGTESVGNDKPSIEKIANLKPDLIIISDYQKDLL 124
Cdd:cd01138     1 GEVEIPAKPKRIVALSGETEGLALlGIKPVGAASIGGKNpyYKKKTLAKVVGIVDEPNLEKVLELKPDLIIVSSKQEENY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410802043 125 ENLEKVAP-VYISHFGDTPDKQLSNIANLLNKKSEKEKWDKDYAKSSKEAKATLKDAGveNEKAAVIQFYG-KEIYVHDA 202
Cdd:cd01138    81 EKLSKIAPtVPVSYNSSDWEEQLKEIGKLLNKEDEAEKWLADYKQKAKEAKEKIKKKL--GNDKSVAVLRGrKQIYVFGE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410802043 203 kvfDGLFSGAGFTPTDGAKANKETK---------AISSEAIPEYAagADRLFILMPtDGNEDSVNEMLNGVWKDIPAVKK 273
Cdd:cd01138   159 ---DGRGGGPILYADLGLKAPEKVKeiedkpgyaAISLEVLPEFD--ADYIFLLFF-TGPEAKADFESLPIWKNLPAVKN 232

                         250
                  ....*....|....*.
gi 1410802043 274 NQVYKVDNtkWSDYSA 289
Cdd:cd01138   233 NHVYIVDA--WVFYFA 246
FecB COG4594
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and ...
 6-302 9.61e-54

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


Pssm-ID: 443650 [Multi-domain]  Cd Length: 316  Bit Score: 177.81  E-value: 9.61e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410802043   6 KWAAILMTVLLAVVLTACGNSSDKDSSKEKEAATKTVTDTMDrKVEVPTTPKRIVALQN--VSEMEILGVKPVGTTDY-- 81
Cdd:COG4594     3 KLLLLLILLLALLLLAACGSSSSDSSSSEAAAGARTVKHAMG-ETTIPGTPKRVVVLEWsfADALLALGVTPVGIADDnd 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410802043  82 YITTYP---KATKGTESVGNDK-PSIEKIANLKPDLIIISDY-QKDLLENLEKVAPV-----YISHFGDTPDkQLSNIAN 151
Cdd:COG4594    82 YDRWVPylrDLIKGVTSVGTRSqPNLEAIAALKPDLIIADKSrHEAIYDQLSKIAPTvlfksRNGDYQENLE-SFKTIAK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410802043 152 LLNKKSEKEKWDKDYAKSSKEAKATLKDAgVENEKAAVIQFYGKEIYVHDAKVFDG-LFSGAGFT--PTDGAKANKETKA 228
Cdd:COG4594   161 ALGKEEEAEAVLADHDQRIAEAKAKLAAA-DKGKKVAVGQFRADGLRLYTPNSFAGsVLAALGFEnpPKQSKDNGYGYSE 239

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1410802043 229 ISSEAIPEYAagADRLFILmpTDGNEDSVNEML-NGVWKDIPAVKKNQVYKVDNTKWSDY----SAAAQLYQMEDAVKQ 302
Cdd:COG4594   240 VSLEQLPALD--PDVLFIA--TYDDPSILKEWKnNPLWKNLKAVKNGRVYEVDGDLWTRGrgplAAELMADDLVEILLK 314
Peripla_BP_2 pfam01497
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ...
 75-277 1.23e-16

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: 77.41  E-value: 1.23e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410802043  75 PVGTTDYYITTYPKATKGTESVGNDKPSIEKIANLKPDLIIIS-DYQKDLLENLEKV-APVYISHFGDTPDK---QLSNI 149
Cdd:pfam01497  22 GVDAYTRDPLKADAVAAIVKVGAYGEINVERLAALKPDLVILStGYLTDEAEELLSLiIPTVIFESSSTGESlkeQIKQL 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410802043 150 ANLLNKKSEKEKWDKDYAKSSKEAKatlKDAGVENEKAAVIQFYGKE---IYVHDAKVFDGLFSGAGFTPTDGAKANKET 226
Cdd:pfam01497 102 GELLGLEDEAEELVAEIDSALAAAK---KAVPSLTRKPVLVFGGADGggyVVAGSNTYIGDLLRILGIENIAAELSGSEY 178

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1410802043 227 KAISSEAIPEYAagADRLFILMPTDGNEDSVNEML-NGVWKDIPAVKKNQVY 277
Cdd:pfam01497 179 APISFEAILSSN--PDVIIVSGRDSFTKTGPEFVAaNPLWAGLPAVKNGRVY 228
fecB PRK11411
iron-dicitrate transporter substrate-binding subunit; Provisional
 37-285 1.65e-12

iron-dicitrate transporter substrate-binding subunit; Provisional


Pssm-ID: 183123 [Multi-domain]  Cd Length: 303  Bit Score: 66.62  E-value: 1.65e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410802043  37 AATKTVTDTMDrKVEVPTTPKRIVALQN--VSEMEILGVKPVGTTD-----YYITTYPKATKGTESVG-NDKPSIEKIAN 108
Cdd:PRK11411   21 AFAVTVQDEQG-TFTLEKTPQRIVVLELsfVDALAAVGVSPVGVADdndakRILPEVRAHLKPWQSVGtRSQPSLEAIAA 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410802043 109 LKPDLiIISDYQKD--LLENLEKVAPVYI--SHfGDTPDKQLSN---IANLLNKKSEKEKWDKDYAKSSKEAKATLKDA- 180
Cdd:PRK11411  100 LKPDL-IIADSSRHagVYIALQKIAPTLLlkSR-NETYQENLQSaaiIGEVLGKKREMQARIEQHKERMAQFASQLPKGt 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410802043 181 ----GVENEKaaviQF--YGKEIYVhdakvfDGLFSGAGFTPTDGAKANKETKAISSEAIpeYAAGADRLFILMPTDGN- 253
Cdd:PRK11411  178 rvafGTSREQ----QFnlHSPESYT------GSVLAALGLNVPKAPMNGAAMPSISLEQL--LALNPDWLLVAHYRQESi 245

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1410802043 254 -EDSVNEMLngvWKDIPAVKKNQVYKVDNTKWS 285
Cdd:PRK11411  246 vKRWQQDPL---WQMLTAAKKQQVASVDSNTWA 275
 
Name Accession Description Interval E-value
FeuA cd01138
Periplasmic binding protein FeuA. These proteins have predicted to function as initial ...
 48-289 1.10e-68

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: 214.12  E-value: 1.10e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410802043  48 RKVEVPTTPKRIVALQNVSEMEIL-GVKPVGTTDYYITT--YPKATKGTESVGNDKPSIEKIANLKPDLIIISDYQKDLL 124
Cdd:cd01138     1 GEVEIPAKPKRIVALSGETEGLALlGIKPVGAASIGGKNpyYKKKTLAKVVGIVDEPNLEKVLELKPDLIIVSSKQEENY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410802043 125 ENLEKVAP-VYISHFGDTPDKQLSNIANLLNKKSEKEKWDKDYAKSSKEAKATLKDAGveNEKAAVIQFYG-KEIYVHDA 202
Cdd:cd01138    81 EKLSKIAPtVPVSYNSSDWEEQLKEIGKLLNKEDEAEKWLADYKQKAKEAKEKIKKKL--GNDKSVAVLRGrKQIYVFGE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410802043 203 kvfDGLFSGAGFTPTDGAKANKETK---------AISSEAIPEYAagADRLFILMPtDGNEDSVNEMLNGVWKDIPAVKK 273
Cdd:cd01138   159 ---DGRGGGPILYADLGLKAPEKVKeiedkpgyaAISLEVLPEFD--ADYIFLLFF-TGPEAKADFESLPIWKNLPAVKN 232

                         250
                  ....*....|....*.
gi 1410802043 274 NQVYKVDNtkWSDYSA 289
Cdd:cd01138   233 NHVYIVDA--WVFYFA 246
FecB COG4594
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and ...
 6-302 9.61e-54

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


Pssm-ID: 443650 [Multi-domain]  Cd Length: 316  Bit Score: 177.81  E-value: 9.61e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410802043   6 KWAAILMTVLLAVVLTACGNSSDKDSSKEKEAATKTVTDTMDrKVEVPTTPKRIVALQN--VSEMEILGVKPVGTTDY-- 81
Cdd:COG4594     3 KLLLLLILLLALLLLAACGSSSSDSSSSEAAAGARTVKHAMG-ETTIPGTPKRVVVLEWsfADALLALGVTPVGIADDnd 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410802043  82 YITTYP---KATKGTESVGNDK-PSIEKIANLKPDLIIISDY-QKDLLENLEKVAPV-----YISHFGDTPDkQLSNIAN 151
Cdd:COG4594    82 YDRWVPylrDLIKGVTSVGTRSqPNLEAIAALKPDLIIADKSrHEAIYDQLSKIAPTvlfksRNGDYQENLE-SFKTIAK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410802043 152 LLNKKSEKEKWDKDYAKSSKEAKATLKDAgVENEKAAVIQFYGKEIYVHDAKVFDG-LFSGAGFT--PTDGAKANKETKA 228
Cdd:COG4594   161 ALGKEEEAEAVLADHDQRIAEAKAKLAAA-DKGKKVAVGQFRADGLRLYTPNSFAGsVLAALGFEnpPKQSKDNGYGYSE 239

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1410802043 229 ISSEAIPEYAagADRLFILmpTDGNEDSVNEML-NGVWKDIPAVKKNQVYKVDNTKWSDY----SAAAQLYQMEDAVKQ 302
Cdd:COG4594   240 VSLEQLPALD--PDVLFIA--TYDDPSILKEWKnNPLWKNLKAVKNGRVYEVDGDLWTRGrgplAAELMADDLVEILLK 314
FhuD cd01146
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ...
 55-293 4.91e-37

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: 132.41  E-value: 4.91e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410802043  55 TPKRIVAL-QNVSEMEI-LGVKPVGTTDY-----YITTYPKATKGTESVGN-DKPSIEKIANLKPDLIIISDY-QKDLLE 125
Cdd:cd01146     2 KPQRIVALdWGALETLLaLGVKPVGVADTagykpWIPEPALPLEGVVDVGTrGQPNLEAIAALKPDLILGSASrHDEIYD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410802043 126 NLEKVAP-VYISHFGDTPD--KQLSNIANLLNKKSEKEKWDKDYAKSSKEAKATLKDAGveNEKAAVIQFYG-KEIYVHD 201
Cdd:cd01146    82 QLSQIAPtVLLDSSPWLAEwkENLRLIAKALGKEEEAEKLLAEYDQRLAELRQKLPDKG--PKPVSVVRFSDaGSIRLYG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410802043 202 AKVFDG-LFSGAGFT--PTDGAKANKETKAISSEAIPEyaAGADRLFILmpTDGNEDSVNEML-NGVWKDIPAVKKNQVY 277
Cdd:cd01146   160 PNSFAGsVLEDLGLQnpWAQETTNDSGFATISLERLAK--ADADVLFVF--TYEDEELAQALQaNPLWQNLPAVKNGRVY 235

                         250
                  ....*....|....*...
gi 1410802043 278 KVDNTKW--SDYSAAAQL 293
Cdd:cd01146   236 VVDDVWWffGGGLSAARL 253
CeuA COG4607
ABC-type enterochelin transport system, periplasmic component [Inorganic ion transport and ...
 6-303 2.92e-29

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


Pssm-ID: 443657 [Multi-domain]  Cd Length: 310  Bit Score: 113.35  E-value: 2.92e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410802043   6 KWAAILMTVLLAVVLTACGNSSDKDSSKEkEAATKTVTDTMDrKVEVPTTPKRIVALQN--VSEMEILGVKPVGTTDYYI 83
Cdd:COG4607     3 KTLLAALALAAALALAACGSSSAAAASAA-AAETVTVEHALG-TVEVPKNPKRVVVFDNgaLDTLDALGVEVAGVPKGLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410802043  84 TTY--PKATKGTESVGNDK-PSIEKIANLKPDLIIISDYQKDLLENLEKVAP-VYIS----HFGDTPDKQLSNIANLLNK 155
Cdd:COG4607    81 PDYlsKYADDKYANVGTLFePDLEAIAALKPDLIIIGGRSAKKYDELSKIAPtIDLTvdgeDYLESLKRNTETLGEIFGK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410802043 156 KSEKEKWDKDYAKSSKEAKATLKDAGveneKAAVIQFYGKEIYVHDAK-VFDGLFSGAGFTPTD-GAKANKETKAISSEA 233
Cdd:COG4607   161 EDEAEELVADLDAKIAALKAAAAGKG----TALIVLTNGGKISAYGPGsRFGPIHDVLGFKPADeDIEASTHGQAISFEF 236

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1410802043 234 I----PEYaagadrLFIL---MPTDGNEDSVNEML-NGVWKDIPAVKKNQVYKVDNTKWsdYSAAAQLYQMEDAVKQI 303
Cdd:COG4607   237 IaeanPDW------LFVIdrdAAIGGEGPAAKQVLdNELVKQTTAWKNGQIVYLDPDAW--YLAGGGIQSLTEMLDEV 306
FepB COG0614
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ...
 58-303 8.30e-29

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


Pssm-ID: 440379 [Multi-domain]  Cd Length: 264  Bit Score: 111.24  E-value: 8.30e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410802043  58 RIVALqNVSEMEI---LGVKP--VGTTDYYITTYPKAT-KGTESVGNDK-PSIEKIANLKPDLIIISDY--QKDLLENLE 128
Cdd:COG0614     2 RIVSL-SPSATELllaLGAGDrlVGVSDWGYCDYPELElKDLPVVGGTGePNLEAILALKPDLVLASSSgnDEEDYEQLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410802043 129 KV-APVYISHFGDTPD--KQLSNIANLLNKKSEKEKWDKDYAKSSKEAKATLKDAGvENEKAAVIQFYGKEIYVHDAKVF 205
Cdd:COG0614    81 KIgIPVVVLDPRSLEDlyESIRLLGELLGREERAEALIAEYEARLAAVRARLAGAE-ERPTVLYEIWSGDPLYTAGGGSF 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410802043 206 -DGLFSGAGFTPTdGAKANKETKAISSEAIPEYAagADRLFIL---MPTDGNEDSVNEMLNG-VWKDIPAVKKNQVYKVD 280
Cdd:COG0614   160 iGELLELAGGRNV-AADLGGGYPEVSLEQVLALD--PDVIILSgggYDAETAEEALEALLADpGWQSLPAVKNGRVYVVP 236

                         250       260
                  ....*....|....*....|...
gi 1410802043 281 NTKWSDYSAAAqLYQMEDAVKQI 303
Cdd:COG0614   237 GDLLSRPGPRL-LLALEDLAKAL 258
FatB cd01140
Siderophore binding protein FatB. These proteins have been shown to function as ABC-type ...
 49-304 1.00e-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: 1.00e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410802043  49 KVEVPTTPKRIVALqNVSEMEI---LGVKPVGTTD-----YYITTYPKATkgTESVGNDK-PSIEKIANLKPDLIIISDY 119
Cdd:cd01140     5 ETKVPKNPEKVVVF-DVGALDTldaLGVKVVGVPKsstlpEYLKKYKDDK--YANVGTLFePDLEAIAALKPDLIIIGGR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410802043 120 QKDLLENLEKVAP-VYIS----HFGDTPDKQLSNIANLLNKKSEKEKWDKDYAKSSKEAKATLKdagvENEKAAVIQFYG 194
Cdd:cd01140    82 LAEKYDELKKIAPtIDLGadlkNYLESVKQNIETLGKIFGKEEEAKELVAEIDASIAEAKSAAK----GKKKALVVLVNG 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410802043 195 KEIYVHDAKVFDG-LFSGAGFTPTD-GAKANKETKAISSEAIPEyaAGADRLFIL---MPTDGNEDSVNEML-NGVWKDI 268
Cdd:cd01140   158 GKLSAFGPGSRFGwLHDLLGFEPADeNIKASSHGQPVSFEYILE--ANPDWLFVIdrgAAIGAEGSSAKEVLdNDLVKNT 235

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1410802043 269 PAVKKNQVYKVDNTKWsdYSAAAQLYQMEDAVKQIT 304
Cdd:cd01140   236 TAWKNGKVIYLDPDLW--YLSGGGLESLKQMIDDLK 269
Peripla_BP_2 pfam01497
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ...
 75-277 1.23e-16

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: 77.41  E-value: 1.23e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410802043  75 PVGTTDYYITTYPKATKGTESVGNDKPSIEKIANLKPDLIIIS-DYQKDLLENLEKV-APVYISHFGDTPDK---QLSNI 149
Cdd:pfam01497  22 GVDAYTRDPLKADAVAAIVKVGAYGEINVERLAALKPDLVILStGYLTDEAEELLSLiIPTVIFESSSTGESlkeQIKQL 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410802043 150 ANLLNKKSEKEKWDKDYAKSSKEAKatlKDAGVENEKAAVIQFYGKE---IYVHDAKVFDGLFSGAGFTPTDGAKANKET 226
Cdd:pfam01497 102 GELLGLEDEAEELVAEIDSALAAAK---KAVPSLTRKPVLVFGGADGggyVVAGSNTYIGDLLRILGIENIAAELSGSEY 178

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1410802043 227 KAISSEAIPEYAagADRLFILMPTDGNEDSVNEML-NGVWKDIPAVKKNQVY 277
Cdd:pfam01497 179 APISFEAILSSN--PDVIIVSGRDSFTKTGPEFVAaNPLWAGLPAVKNGRVY 228
fecB PRK11411
iron-dicitrate transporter substrate-binding subunit; Provisional
 37-285 1.65e-12

iron-dicitrate transporter substrate-binding subunit; Provisional


Pssm-ID: 183123 [Multi-domain]  Cd Length: 303  Bit Score: 66.62  E-value: 1.65e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410802043  37 AATKTVTDTMDrKVEVPTTPKRIVALQN--VSEMEILGVKPVGTTD-----YYITTYPKATKGTESVG-NDKPSIEKIAN 108
Cdd:PRK11411   21 AFAVTVQDEQG-TFTLEKTPQRIVVLELsfVDALAAVGVSPVGVADdndakRILPEVRAHLKPWQSVGtRSQPSLEAIAA 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410802043 109 LKPDLiIISDYQKD--LLENLEKVAPVYI--SHfGDTPDKQLSN---IANLLNKKSEKEKWDKDYAKSSKEAKATLKDA- 180
Cdd:PRK11411  100 LKPDL-IIADSSRHagVYIALQKIAPTLLlkSR-NETYQENLQSaaiIGEVLGKKREMQARIEQHKERMAQFASQLPKGt 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410802043 181 ----GVENEKaaviQF--YGKEIYVhdakvfDGLFSGAGFTPTDGAKANKETKAISSEAIpeYAAGADRLFILMPTDGN- 253
Cdd:PRK11411  178 rvafGTSREQ----QFnlHSPESYT------GSVLAALGLNVPKAPMNGAAMPSISLEQL--LALNPDWLLVAHYRQESi 245

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1410802043 254 -EDSVNEMLngvWKDIPAVKKNQVYKVDNTKWS 285
Cdd:PRK11411  246 vKRWQQDPL---WQMLTAAKKQQVASVDSNTWA 275
FepB COG4592
ABC-type Fe2+-enterobactin transport system, periplasmic component [Inorganic ion transport ...
 8-293 1.82e-12

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


Pssm-ID: 443649 [Multi-domain]  Cd Length: 330  Bit Score: 66.89  E-value: 1.82e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410802043   8 AAILMTVLLAVVLTACGNSSDKDSSK---EKEAATKTVTDtmDR-KVEVPTTPKRIVALqNVSemeILG--------VKP 75
Cdd:COG4592     7 AAAAALLAAALLLAGCSSADSTASGTstaAAGGWPRTVTT--EKgTVTLPAKPQRIVST-SVT---LTGsllaidapVVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410802043  76 VGTTDYYITTYPK---------ATK-GTESV-GNDKPSIEKIANLKPDLIIIS----DYQKDLLENLEKVAPVYISHFGD 140
Cdd:COG4592    81 SGATTPNNVTDDQgffrqwadvAKErGVKRLyIGLEPNAEAIAAAAPDLIIGSatggDSALDLYDQLSAIAPTLVVNYDD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410802043 141 TPDKQLSN-IANLLNKKSEKEKWDKDYAKSSKEAKATLKdagVENEKAAVIQFYGkeiyvhDAKVF--------DGLFSG 211
Cdd:COG4592   161 KSWQELATqLGEATGHEAQADAVIAAFDARVAEVKAAIT---LPPQPVSALVYNE------DGGANlwtpesaqGQLLQA 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410802043 212 AGFT----PTDGAKANKETKA-----ISSEAIPEYAAGaDRLFILmptDGNEDSVNEML-NGVWKDIPAVKKNQVYKVDN 281
Cdd:COG4592   232 LGFTlaplPAELATSTSQGKRgdivqLSGENLAAALTG-PTLFLF---AADDKDVDALKaDPLLAHLPAVQAGRVYALGP 307

                         330
                  ....*....|....*
gi 1410802043 282 tkWS---DYSAAAQL 293
Cdd:COG4592   308 --DSfrlDYYSASNL 320
TroA-like cd00636
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function ...
 57-179 2.62e-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: 63.35  E-value: 2.62e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410802043  57 KRIVALQNvSEMEIL-----GVKPVGTTDY--YITTYPKATKGTESVGNDK-PSIEKIANLKPDLIIISD-YQKDLLENL 127
Cdd:cd00636     1 KRVVALDP-GATELLlalggDDKPVGVADPsgYPPEAKALLEKVPDVGHGYePNLEKIAALKPDLIIANGsGLEAWLDKL 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1410802043 128 EKVA-PVYISHFGDTPD-----KQLSNIANLLNKKSEKEKWDKDYAKSSKEAKATLKD 179
Cdd:cd00636    80 SKIAiPVVVVDEASELSlenikESIRLIGKALGKEENAEELIAELDARLAELRAKLAK 137
TroA_e cd01142
Periplasmic binding protein TroA_e. These proteins are predicted to function as initial ...
 36-295 5.95e-11

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: 61.99  E-value: 5.95e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410802043  36 EAATKTVTDTMDRKVEVPTTPKRIVALQ--NVSEMEILG---------VKPVGTTDYYiTTYPKATKGTESVGNDKPSIE 104
Cdd:cd01142     4 TAATRTITDMAGRKVTIPDEVKRIAALWgaGNAVVAALGggklivattSTVQQEPWLY-RLAPSLENVATGGTGNDVNIE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410802043 105 KIANLKPDLII-ISDYQKDLLENLEKVAPVYISHFGDTPDKQLS--NIANLLNKKSEKEKWDKDYAKSSKEAKATLKDAG 181
Cdd:cd01142    83 ELLALKPDVVIvWSTDGKEAGKAVLRLLNALSLRDAELEEVKLTiaLLGELLGRQEKAEALVAYFDDNLAYVAARTKKLP 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410802043 182 vENEKAAViqFYGKEiyvhDAKVFDGlfSG---------AGFTPTDGAKANKETKAISSEAIpeYAAGADRLFIlmptdG 252
Cdd:cd01142   163 -DSERPRV--YYAGP----DPLTTDG--TGsitnswidlAGGINVASEATKKGSGEVSLEQL--LKWNPDVIIV-----G 226

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1410802043 253 NEDSVNEML-NGVWKDIPAVKKNQVYKV-DNTKWSDYSAAAQLYQ 295
Cdd:cd01142   227 NADTKAAILaDPRWQNLRAVKNGRVYVNpEGAFWWDRPSAEEALL 271
YvrC cd01143
Periplasmic binding protein YvrC. These proteins are predicted to function as initial ...
 56-180 7.50e-10

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: 57.29  E-value: 7.50e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410802043  56 PKRIVALQNvSEMEIL-----GVKPVGTTDYyiTTYPKATKGTESVGN-DKPSIEKIANLKPDLII-ISDYQKDLLENLE 128
Cdd:cd01143     3 PERIVSLSP-SITEILfalgaGDKIVGVDTY--SNYPKEVRKKPKVGSySNPNVEKIVALKPDLVIvSSSSLAELLEKLK 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1410802043 129 KVA-PVYISHFGDTPD---KQLSNIANLLNKKSEKEKWDKDYAKSSKEAKATLKDA 180
Cdd:cd01143    80 DAGiPVVVLPAASSLDeiyDQIELIGKITGAEEEAEKLVKEMKQKIDKVKDKGKTI 135
BtuF cd01144
Cobalamin binding protein BtuF. These proteins have been shown to function as initial ...
 57-280 1.91e-09

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: 56.92  E-value: 1.91e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410802043  57 KRIVALQNvSEMEIL-----GVKPVGTTDYyiTTYPKATKGTESVGNDK-PSIEKIANLKPDLIIISDY--QKDLLENLE 128
Cdd:cd01144     1 MRIVSLAP-SATELLyalglGDQLVGVTDY--CDYPPEAKKLPRVGGFYqLDLERVLALKPDLVIAWDDcnVCAVVDQLR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410802043 129 K-VAPVYISHFGDTPD--KQLSNIANLLNKKSEKEKWDKDYaksskEAKAtlkdAGVENEKAAVIQfygkeiyvhdAKVF 205
Cdd:cd01144    78 AaGIPVLVSEPQTLDDilADIRRLGTLAGRPARAEELAEAL-----RRRL----AALRKQYASKPP----------PRVF 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410802043 206 -----DGLFSGAGFTPTD----------GAKANKETKAISSEAIPeyAAGADRLfILMPTDGNEDSVNEMLNGVWKDIPA 270
Cdd:cd01144   139 yqewiDPLMTAGGDWVPElialaggvnvFADAGERSPQVSWEDVL--AANPDVI-VLSPCGFGFTPAILRKEPAWQALPA 215

                         250
                  ....*....|
gi 1410802043 271 VKKNQVYKVD 280
Cdd:cd01144   216 VRNGRVYAVD 225
ChuT COG4558
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism] ...
 54-280 5.49e-09

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


Pssm-ID: 443619 [Multi-domain]  Cd Length: 285  Bit Score: 55.97  E-value: 5.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410802043  54 TTPKRIVAL-QNVSEmeI---LGVKP--VGTTDYyiTTYPKATKGTESVGNDK-PSIEKIANLKPDLIIISD--YQKDLL 124
Cdd:COG4558    25 AAAERIVSLgGSVTE--IvyaLGAGDrlVGVDTT--STYPAAAKALPDVGYMRqLSAEGILSLKPTLVLASEgaGPPEVL 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410802043 125 ENLEKVA-PVYISHFGDTPD---KQLSNIANLLNKKSE----KEKWDKDYAKSSKEAKATLKDAgveneKAAViqfygke 196
Cdd:COG4558   101 DQLRAAGvPVVVVPAAPSLEgvlAKIRAVAAALGVPEAgealAARLEADLAALAARVAAIGKPP-----RVLF------- 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410802043 197 IYVHDAKVF---------DGLFSGAGFtpTDGAKANKETKAISSEAIPeyAAGADrlFILMPTDGNEDSVNemLNGVWK- 266
Cdd:COG4558   169 LLSRGGGRPmvagrgtaaDALIRLAGG--VNAAAGFEGYKPLSAEALI--AAAPD--VILVMTRGLESLGG--VDGLLAl 240

                         250
                  ....*....|....*...
gi 1410802043 267 ----DIPAVKKNQVYKVD 280
Cdd:COG4558   241 pglaQTPAGKNKRIVAMD 258
PRK10957 PRK10957
iron-enterobactin transporter periplasmic binding protein; Provisional
 9-293 9.70e-08

iron-enterobactin transporter periplasmic binding protein; Provisional


Pssm-ID: 236806 [Multi-domain]  Cd Length: 317  Bit Score: 52.67  E-value: 9.70e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410802043   9 AILMTVLLAVVLTACGNSSDKDSSkekEAATKTVTDTmDRKVEVPTTPKRIVAlqnvSEMEILGV-----KPV----GTT 79
Cdd:PRK10957    1 PLYRLALLLLGLLLSGIAAAQASA---AGWPRTVTDS-RGSVTLESKPQRIVS----TSVTLTGTllaidAPViasgATT 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410802043  80 DYYITTYPK----------ATKGTESVGNDKPSIEKIANLKPDLIIIS----DYQKDLLENLEKVAPVYISHFGDtpdKQ 145
Cdd:PRK10957   73 PNTRVADDQgffrqwsdvaKERGVEVLYIGEPDAEAVAAQMPDLIVISatggDSALALYDQLSAIAPTLVIDYDD---KS 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410802043 146 LSNIANLLNKKSEKEKwdkdyaksskEAKATLK--DAGVENEKAA---------VIQFYGKEiyvHDAKVF--DG----L 208
Cdd:PRK10957  150 WQELATQLGEATGLEK----------QAAAVIAqfDAQLAEVKAKitlppqpvsALVYNGAG---HSANLWtpESaqgqL 216

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410802043 209 FSGAGFT----PTDGAKANKETKA-----ISSEAIPEyAAGADRLFILMPTDGNEDSVneMLNGVWKDIPAVKKNQVYKV 279
Cdd:PRK10957  217 LEQLGFTlaelPAGLQASTSQGKRhdiiqLGGENLAA-GLNGETLFLFAGDDKDADAF--LADPLLANLPAVQNKQVYAL 293

                         330
                  ....*....|....*
gi 1410802043 280 DNTKWS-DYSAAAQL 293
Cdd:PRK10957  294 GTDTFRlDYYSATQL 308
PRK14048 PRK14048
ferrichrome/ferrioxamine B periplasmic transporter; Provisional
 41-179 2.33e-07

ferrichrome/ferrioxamine B periplasmic transporter; Provisional


Pssm-ID: 172540 [Multi-domain]  Cd Length: 374  Bit Score: 51.44  E-value: 2.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410802043  41 TVTDTMDRKVEVPTTPKRIVALQ--NVSEMEILGVKPVGTT---------------DYYITTYPKATKGTESVGNDKP-- 101
Cdd:PRK14048   33 TVTDAVGREVTIPAPPKAVLLGSgfNLIALSLIHPDPVSLLagwsgdmkgdnpeiyESFLRKFPELADVPLIDDGSGPgl 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410802043 102 SIEKIANLKPDLIIISDYQKD------LLENLEKVA-PVYISHFGDTPDKQLSNIANLLNKKSEKEKWDKDYAKSSKEAK 174
Cdd:PRK14048  113 SFETILTLKADLAILANWQADteagqrAIEYLESIGvPVIVVDFNNEALKNTPDNMRLLGKVFEREEQAEDFARFYEERL 192


                  ....*
gi 1410802043 175 ATLKD 179
Cdd:PRK14048  193 ARIRD 197
HemV-2 cd01147
Metal binding protein HemV-2. These proteins are predicted to function as initial receptors ...
 97-279 7.56e-06

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: 46.56  E-value: 7.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410802043  97 GNDKPSIEKIANLKPDLIII--SDYQKDLLENLEK------VAPVYISHFGDTPDkQLSNIANLLNKKSEKEKWdKDYAK 168
Cdd:cd01147    61 RGNTPNYEKIAALKPDVVIDvgSDDPTSIADDLQKktgipvVVLDGGDSLEDTPE-QIRLLGKVLGKEERAEEL-ISFIE 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410802043 169 SS-KEAKATLKDAGvENEKAAV----IQFYGKEIYVHDAKVFDGLFSGAGFTPTDGAKANKETKAISSEAI----PEYaa 239
Cdd:cd01147   139 SIlADVEERTKDIP-DEEKPTVyfgrIGTKGAAGLESGLAGSIEVFELAGGINVADGLGGGGLKEVSPEQIllwnPDV-- 215

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1410802043 240 gadrlfILMPTDGNEDSVNEMLNG--VWKDIPAVKKNQVYKV 279
Cdd:cd01147   216 ------IFLDTGSFYLSLEGYAKNrpFWQSLKAVKNGRVYLL 251
TroA_f cd01139
Periplasmic binding protein TroA_f. These proteins are predicted to function as initial ...
 40-277 1.08e-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: 46.53  E-value: 1.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410802043  40 KTVTDTMDRKVEVPTTPKRIValqnVSEMEIL-------GVKPV------------GTTDY---YITTYPKATK--GTES 95
Cdd:cd01139     1 ITVTDVAGRKVTLDAPVERVL----LGEGRQLyalalleGENPFarivgwggdlkkGDPDTyakYKEKFPEIADipLIGS 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410802043  96 VGNDKPSIEKIANLKPDLIIIS------DYQKDLLENLEKVA-PVYISHFGDTPDKQLSNIANLLNKKSEKEKWDKDYAK 168
Cdd:cd01139    77 TYNGDFSVEKVLTLKPDLVILNiwakttAEESGILEKLEQAGiPVVFVDFRQKPLKNTTPSMRLLGKALGREERAEEFIE 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410802043 169 ---------SSKEAKATLKDAGVENEKAAVIQF-----YGKEIYVHDAKVFDGLFSGAGFTPTDGAKANKEtKAISSEai 234
Cdd:cd01139   157 fyqeridriRDRLAKINEPKPKVFIELGAGGPEeccstYGNGNWGELVDAAGGDNIADGLIPGTSGELNAE-YVIAAN-- 233

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1410802043 235 PEYAAGADRLFILMPTDGN-------EDSVNEMLNG-----VWKDIPAVKKNQVY 277
Cdd:cd01139   234 PEIIIATGGNWAKDPSGVSlgpdgttADAKESLLRAllkrpGWSSLQAVKNGRVY 288
TroA_d cd01141
Periplasmic binding protein TroA_d. These proteins are predicted to function as initial ...
 54-144 5.78e-04

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: 40.10  E-value: 5.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1410802043  54 TTPKRIVALQNVSEMEILGV----KPVGTTDYYITTY-PK-ATKGTESVGND-KPSIEKIANLKPDLIIISD--YQKDLL 124
Cdd:cd01141     6 VPPKRIVVLSPTHVDLLLALdkadKIVGVSASAYDLNtPAvKERIDIQVGPTgSLNVELIVALKPDLVILYGgfQAQTIL 85

                          90       100
                  ....*....|....*....|..
gi 1410802043 125 ENLEK--VAPVYISHFGDTPDK 144
Cdd:cd01141    86 DKLEQlgIPVLYVNEYPSPLGR 107
 
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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