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Conserved domains on  [gi|446655191|ref|WP_000732537|]
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MULTISPECIES: ABC transporter substrate-binding protein [Enterobacterales]

Protein Classification

ABC transporter substrate-binding protein( domain architecture ID 10100164)

TroA family ABC transporter substrate-binding protein functions in the ABC transport of ferric siderophores and/or metal ions such as Mn2+, Fe3+, Cu2+, and Zn2+

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TroA_a cd01148
Metal binding protein TroA_a. These proteins are predicted to function as initial receptors ...
 22-309 7.65e-144

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: 406.72  E-value: 7.65e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655191  22 FPVTIESCGTPVTFAGPPKRAVINDLNMSEMAFALHLQDRIVGLTGISgwYKMTPEFKKAMGSIPELAPKYPTLETLLAA 101
Cdd:cd01148    1 YPLTVENCGRSVTFDKAPQRVVSNDQNTTEMMLALGLQDRMVGTAGID--NKDLPELKAKYDKVPELAKKYPSKETVLAA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655191 102 EPDFFFAGWNYGMKVGGEVTPDTLSKYGIKTFVLSESCVFttaHKNKATMDLLYNDVLTLGKIFGKRNDAQSLVSGWKKR 181
Cdd:cd01148   79 RPDLVFGGWSYGFDKGGLGTPDSLAELGIKTYILPESCGQ---RRGEATLDDVYNDIRNLGKIFDVEDRADKLVADLKAR 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655191 182 LNELPKPAAGT-RPLKVFVYDSGEDKPFTSGKYAMPTAIIEAAGGKNVMEAVDTSWGTTSWESVAATEPDFIILLDYQTG 260
Cdd:cd01148  156 LAEISAKVKGDgKKVAVFVYDSGEDKPFTSGRGGIPNAIITAAGGRNVFADVDESWTTVSWETVIARNPDVIVIIDYGDQ 235

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 446655191 261 SGADALRHFLENHPLMKLTPAVQHHRYLKLQYAELTPGPANVDAVEKLA 309
Cdd:cd01148  236 NAAEQKIKFLKENPALKNVPAVKNNRFIVLPLAEATPGIRNVDAIEKLA 284
 
Name Accession Description Interval E-value
TroA_a cd01148
Metal binding protein TroA_a. These proteins are predicted to function as initial receptors ...
 22-309 7.65e-144

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: 406.72  E-value: 7.65e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655191  22 FPVTIESCGTPVTFAGPPKRAVINDLNMSEMAFALHLQDRIVGLTGISgwYKMTPEFKKAMGSIPELAPKYPTLETLLAA 101
Cdd:cd01148    1 YPLTVENCGRSVTFDKAPQRVVSNDQNTTEMMLALGLQDRMVGTAGID--NKDLPELKAKYDKVPELAKKYPSKETVLAA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655191 102 EPDFFFAGWNYGMKVGGEVTPDTLSKYGIKTFVLSESCVFttaHKNKATMDLLYNDVLTLGKIFGKRNDAQSLVSGWKKR 181
Cdd:cd01148   79 RPDLVFGGWSYGFDKGGLGTPDSLAELGIKTYILPESCGQ---RRGEATLDDVYNDIRNLGKIFDVEDRADKLVADLKAR 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655191 182 LNELPKPAAGT-RPLKVFVYDSGEDKPFTSGKYAMPTAIIEAAGGKNVMEAVDTSWGTTSWESVAATEPDFIILLDYQTG 260
Cdd:cd01148  156 LAEISAKVKGDgKKVAVFVYDSGEDKPFTSGRGGIPNAIITAAGGRNVFADVDESWTTVSWETVIARNPDVIVIIDYGDQ 235

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 446655191 261 SGADALRHFLENHPLMKLTPAVQHHRYLKLQYAELTPGPANVDAVEKLA 309
Cdd:cd01148  236 NAAEQKIKFLKENPALKNVPAVKNNRFIVLPLAEATPGIRNVDAIEKLA 284
FepB COG0614
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ...
 41-314 5.93e-57

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


Pssm-ID: 440379 [Multi-domain]  Cd Length: 264  Bit Score: 184.82  E-value: 5.93e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655191  41 RAVINDLNMSEMAFALHLQDRIVGLTGISgwYKMTPEFkkAMGSIPELA-PKYPTLETLLAAEPDFFFAGWNYGmkvgGE 119
Cdd:COG0614    2 RIVSLSPSATELLLALGAGDRLVGVSDWG--YCDYPEL--ELKDLPVVGgTGEPNLEAILALKPDLVLASSSGN----DE 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655191 120 VTPDTLSKYGIKTFVLSEScvfttahknkaTMDLLYNDVLTLGKIFGKRNDAQSLVSGWKKRLNEL-PKPAAGTRPLKVF 198
Cdd:COG0614   74 EDYEQLEKIGIPVVVLDPR-----------SLEDLYESIRLLGELLGREERAEALIAEYEARLAAVrARLAGAEERPTVL 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655191 199 VYDSGEDKPFTSGKYAMPTAIIEAAGGKNVMEAVDTSWGTTSWESVAATEPDFIILLDY-QTGSGADALRHFLENHPLMK 277
Cdd:COG0614  143 YEIWSGDPLYTAGGGSFIGELLELAGGRNVAADLGGGYPEVSLEQVLALDPDVIILSGGgYDAETAEEALEALLADPGWQ 222

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 446655191 278 LTPAVQHHRYLKL-QYAELTPGPANVDAVEKLARAMYP 314
Cdd:COG0614  223 SLPAVKNGRVYVVpGDLLSRPGPRLLLALEDLAKALHP 260
F420-O_ABCperi TIGR03868
proposed F420-0 ABC transporter, periplasmic F420-0 binding protein; This small clade of ...
 23-312 1.06e-56

proposed F420-0 ABC transporter, periplasmic F420-0 binding protein; This small clade of ABC-type transporter periplasmic binding protein components is found as a three gene cassette along with a permease (TIGR03869) and an ATPase (TIGR03873). The organisms containing this cassette are all Actinobacteria and all contain numerous genes requiring the coenzyme F420. This model was defined based on five such organisms, four of which are lacking all F420 biosynthetic capability save the final side-chain polyglutamate attachment step (via the gene cofE: TIGR01916). In Jonesia denitrificans DSM 20603 and marine actinobacterium PHSC20C1 this cassette is in an apparent operon with the cofE gene and, in PHSC20C1, also with a F420-dependent glucose-6-phosphate dehydrogenase (TIGR03554). Based on these observations we propose that this periplasmic binding protein is a component of an F420-0 (that is, F420 lacking only the polyglutamate tail) transporter.


Pssm-ID: 274826 [Multi-domain]  Cd Length: 287  Bit Score: 185.04  E-value: 1.06e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655191   23 PVTIESCGTPVTFAGPPKRAVINDLNMSEMAFALHLQDRIVGLTGISGwyKMTPEFKKAMGSIPELAPKYPTLETLLAAE 102
Cdd:TIGR03868   1 PVTVDNCGTDVTFDSAPQRVVTIKSSTTELLLALGLGDRIVGTAFPDG--PVPAEWATDAAAVPPLSERVPSPEAVLETE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655191  103 PDFFFAGWNYGMKVGGEVTPDTLSKYGIKTFVLSESCVFTTAHKNKATMDLLYNDVLTLGKIFGKRNDAQSLVSGWKKRL 182
Cdd:TIGR03868  79 PDLVYAGWESNLTAEGAGERADLASLGVNTYVAPSACKEDGYQPDPLTFDDVFAEITEVGTIFDVPDAAASLVAEQRAQL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655191  183 NELPKPAAGtrpLKVFVYDSGEDKPFTSGKYAMPTAIIEAAGGKNVMEAVDTSWGTTSWESVAATEPDFIILLDYQTGSg 262
Cdd:TIGR03868 159 AAIEPDDRG---LTALWYSSGSDTPFVGAGIGAPQMVMDTAGLTNIAADVHDTWTPMSWEAVVDADPDVIVLVDSAWNS- 234

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 446655191  263 ADALRHFLENHPLMKLTPAVQHHRYLKLQYAELTPGPANVDAVEKLARAM 312
Cdd:TIGR03868 235 AEKKIEVLESNPATSNLTAVQEQRYVVVPFAATEAGVRNVDAAASLADQL 284
Peripla_BP_2 pfam01497
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ...
 51-286 1.54e-18

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: 82.80  E-value: 1.54e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655191   51 EMAFALHLQDRIVGltgISGWYKMtPEFKKAMGSIPEL-APKYPTLETLLAAEPDFFFAGWNYGMkvggEVTPDTLSKyG 129
Cdd:pfam01497   9 EILYALGATDSIVG---VDAYTRD-PLKADAVAAIVKVgAYGEINVERLAALKPDLVILSTGYLT----DEAEELLSL-I 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655191  130 IKTFVLSESCVFttahknkatmDLLYNDVLTLGKIFGKRNDAQSLVSGWKKRLNELPKPAAGTRPLKVFVYDSGEDKPFT 209
Cdd:pfam01497  80 IPTVIFESSSTG----------ESLKEQIKQLGELLGLEDEAEELVAEIDSALAAAKKAVPSLTRKPVLVFGGADGGGYV 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655191  210 -SGKYAMPTAIIEAAGGKNVMEAVDTS-WGTTSWESVAATEPDFIILLDY--QTGSGADalrhFLENHPLMKLTPAVQHH 285
Cdd:pfam01497 150 vAGSNTYIGDLLRILGIENIAAELSGSeYAPISFEAILSSNPDVIIVSGRdsFTKTGPE----FVAANPLWAGLPAVKNG 225


                  .
gi 446655191  286 R 286
Cdd:pfam01497 226 R 226
PRK03379 PRK03379
vitamin B12-transporter protein BtuF; Provisional
 50-254 1.73e-05

vitamin B12-transporter protein BtuF; Provisional


Pssm-ID: 179575 [Multi-domain]  Cd Length: 260  Bit Score: 45.45  E-value: 1.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655191  50 SEMAFAlhlqdriVGLT--GISGWYKMTPEFKKamgsIPELAP-KYPTLETLLAAEPDFFFAgWNYGmkvGGEVTPDTLS 126
Cdd:PRK03379  28 TELAFA-------AGITpvGVSSYSDYPPQAKK----IEQVATwQGMNLERIVALKPDLVLA-WRGG---NAERQVDQLA 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655191 127 KYGIKTFVLSEScvfttahknkaTMDLLYNDVLTLGKIFGKRNDAQSLVSGWKKRLNELPKPAAGTRPLKVFVyDSGEDK 206
Cdd:PRK03379  93 SLGIKVMWVDAT-----------SIEQIANALRQLAPWSPQPEKAEQAAQSLLQQYAALKAQYADKPKKRVFL-QFGTNP 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 446655191 207 PFTSGKYAMPTAIIEAAGGKNVMEAVDTSWGTTSWESVAATEPDFIIL 254
Cdd:PRK03379 161 LFTSGKHSIQSQVLSLCGGENIFADSRVPWPQVSREQVLARKPQAIVI 208
 
Name Accession Description Interval E-value
TroA_a cd01148
Metal binding protein TroA_a. These proteins are predicted to function as initial receptors ...
 22-309 7.65e-144

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: 406.72  E-value: 7.65e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655191  22 FPVTIESCGTPVTFAGPPKRAVINDLNMSEMAFALHLQDRIVGLTGISgwYKMTPEFKKAMGSIPELAPKYPTLETLLAA 101
Cdd:cd01148    1 YPLTVENCGRSVTFDKAPQRVVSNDQNTTEMMLALGLQDRMVGTAGID--NKDLPELKAKYDKVPELAKKYPSKETVLAA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655191 102 EPDFFFAGWNYGMKVGGEVTPDTLSKYGIKTFVLSESCVFttaHKNKATMDLLYNDVLTLGKIFGKRNDAQSLVSGWKKR 181
Cdd:cd01148   79 RPDLVFGGWSYGFDKGGLGTPDSLAELGIKTYILPESCGQ---RRGEATLDDVYNDIRNLGKIFDVEDRADKLVADLKAR 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655191 182 LNELPKPAAGT-RPLKVFVYDSGEDKPFTSGKYAMPTAIIEAAGGKNVMEAVDTSWGTTSWESVAATEPDFIILLDYQTG 260
Cdd:cd01148  156 LAEISAKVKGDgKKVAVFVYDSGEDKPFTSGRGGIPNAIITAAGGRNVFADVDESWTTVSWETVIARNPDVIVIIDYGDQ 235

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 446655191 261 SGADALRHFLENHPLMKLTPAVQHHRYLKLQYAELTPGPANVDAVEKLA 309
Cdd:cd01148  236 NAAEQKIKFLKENPALKNVPAVKNNRFIVLPLAEATPGIRNVDAIEKLA 284
FepB COG0614
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ...
 41-314 5.93e-57

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


Pssm-ID: 440379 [Multi-domain]  Cd Length: 264  Bit Score: 184.82  E-value: 5.93e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655191  41 RAVINDLNMSEMAFALHLQDRIVGLTGISgwYKMTPEFkkAMGSIPELA-PKYPTLETLLAAEPDFFFAGWNYGmkvgGE 119
Cdd:COG0614    2 RIVSLSPSATELLLALGAGDRLVGVSDWG--YCDYPEL--ELKDLPVVGgTGEPNLEAILALKPDLVLASSSGN----DE 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655191 120 VTPDTLSKYGIKTFVLSEScvfttahknkaTMDLLYNDVLTLGKIFGKRNDAQSLVSGWKKRLNEL-PKPAAGTRPLKVF 198
Cdd:COG0614   74 EDYEQLEKIGIPVVVLDPR-----------SLEDLYESIRLLGELLGREERAEALIAEYEARLAAVrARLAGAEERPTVL 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655191 199 VYDSGEDKPFTSGKYAMPTAIIEAAGGKNVMEAVDTSWGTTSWESVAATEPDFIILLDY-QTGSGADALRHFLENHPLMK 277
Cdd:COG0614  143 YEIWSGDPLYTAGGGSFIGELLELAGGRNVAADLGGGYPEVSLEQVLALDPDVIILSGGgYDAETAEEALEALLADPGWQ 222

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 446655191 278 LTPAVQHHRYLKL-QYAELTPGPANVDAVEKLARAMYP 314
Cdd:COG0614  223 SLPAVKNGRVYVVpGDLLSRPGPRLLLALEDLAKALHP 260
F420-O_ABCperi TIGR03868
proposed F420-0 ABC transporter, periplasmic F420-0 binding protein; This small clade of ...
 23-312 1.06e-56

proposed F420-0 ABC transporter, periplasmic F420-0 binding protein; This small clade of ABC-type transporter periplasmic binding protein components is found as a three gene cassette along with a permease (TIGR03869) and an ATPase (TIGR03873). The organisms containing this cassette are all Actinobacteria and all contain numerous genes requiring the coenzyme F420. This model was defined based on five such organisms, four of which are lacking all F420 biosynthetic capability save the final side-chain polyglutamate attachment step (via the gene cofE: TIGR01916). In Jonesia denitrificans DSM 20603 and marine actinobacterium PHSC20C1 this cassette is in an apparent operon with the cofE gene and, in PHSC20C1, also with a F420-dependent glucose-6-phosphate dehydrogenase (TIGR03554). Based on these observations we propose that this periplasmic binding protein is a component of an F420-0 (that is, F420 lacking only the polyglutamate tail) transporter.


Pssm-ID: 274826 [Multi-domain]  Cd Length: 287  Bit Score: 185.04  E-value: 1.06e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655191   23 PVTIESCGTPVTFAGPPKRAVINDLNMSEMAFALHLQDRIVGLTGISGwyKMTPEFKKAMGSIPELAPKYPTLETLLAAE 102
Cdd:TIGR03868   1 PVTVDNCGTDVTFDSAPQRVVTIKSSTTELLLALGLGDRIVGTAFPDG--PVPAEWATDAAAVPPLSERVPSPEAVLETE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655191  103 PDFFFAGWNYGMKVGGEVTPDTLSKYGIKTFVLSESCVFTTAHKNKATMDLLYNDVLTLGKIFGKRNDAQSLVSGWKKRL 182
Cdd:TIGR03868  79 PDLVYAGWESNLTAEGAGERADLASLGVNTYVAPSACKEDGYQPDPLTFDDVFAEITEVGTIFDVPDAAASLVAEQRAQL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655191  183 NELPKPAAGtrpLKVFVYDSGEDKPFTSGKYAMPTAIIEAAGGKNVMEAVDTSWGTTSWESVAATEPDFIILLDYQTGSg 262
Cdd:TIGR03868 159 AAIEPDDRG---LTALWYSSGSDTPFVGAGIGAPQMVMDTAGLTNIAADVHDTWTPMSWEAVVDADPDVIVLVDSAWNS- 234

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 446655191  263 ADALRHFLENHPLMKLTPAVQHHRYLKLQYAELTPGPANVDAVEKLARAM 312
Cdd:TIGR03868 235 AEKKIEVLESNPATSNLTAVQEQRYVVVPFAATEAGVRNVDAAASLADQL 284
ChuT COG4558
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism] ...
 1-317 3.25e-30

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


Pssm-ID: 443619 [Multi-domain]  Cd Length: 285  Bit Score: 115.67  E-value: 3.25e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655191   1 MKKLFISLLavLSASVASAADFPVTIEScgtpvtfagpPKRAVINDLNMSEMAFALHLQDRIVGLTGISGWykmtpefkk 80
Cdd:COG4558    1 MKRLALALL--LLALAALAAGASVAAAA----------AERIVSLGGSVTEIVYALGAGDRLVGVDTTSTY--------- 59

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655191  81 amgsiPELAPKYPTL--------ETLLAAEPDFFFAGWNygmkVGGEVTPDTLSKYGIKTFVLSEscvfttahknKATMD 152
Cdd:COG4558   60 -----PAAAKALPDVgymrqlsaEGILSLKPTLVLASEG----AGPPEVLDQLRAAGVPVVVVPA----------APSLE 120

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655191 153 LLYNDVLTLGKIFGKRNDAQSLVSGWKKRLNELPK-PAAGTRPLKV-FVYDSGEDKPFTSGKYAMPTAIIEAAGGKNVME 230
Cdd:COG4558  121 GVLAKIRAVAAALGVPEAGEALAARLEADLAALAArVAAIGKPPRVlFLLSRGGGRPMVAGRGTAADALIRLAGGVNAAA 200

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655191 231 AVDtSWGTTSWESVAATEPDFIILLD--YQTGSGADAlrhfLENHPLMKLTPAVQHHRYLKLQYAELT-PGPANVDAVEK 307
Cdd:COG4558  201 GFE-GYKPLSAEALIAAAPDVILVMTrgLESLGGVDG----LLALPGLAQTPAGKNKRIVAMDDLLLLgFGPRTPQAALA 275

                        330
                 ....*....|
gi 446655191 308 LARAMYPSTA 317
Cdd:COG4558  276 LAQALYPAAA 285
BtuF cd01144
Cobalamin binding protein BtuF. These proteins have been shown to function as initial ...
 49-310 5.44e-22

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: 92.75  E-value: 5.44e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655191  49 MSEMAFALHLQDRIVGLTGISGWykmtPEFKKAMGSIpeLAPKYPTLETLLAAEPDFFFAgWNygmkvGGEVTP--DTLS 126
Cdd:cd01144   10 ATELLYALGLGDQLVGVTDYCDY----PPEAKKLPRV--GGFYQLDLERVLALKPDLVIA-WD-----DCNVCAvvDQLR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655191 127 KYGIKTFVLsescvfttahkNKATMDLLYNDVLTLGKIFGKRNDAQSLVSGWKKRLNELPKPAAGTRPLKVFvYDSGEDK 206
Cdd:cd01144   78 AAGIPVLVS-----------EPQTLDDILADIRRLGTLAGRPARAEELAEALRRRLAALRKQYASKPPPRVF-YQEWIDP 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655191 207 PFTSGKyAMPTAIIEAAGGKNVMEAVDTSWGTTSWESVAATEPDFIILLDYQTGSGADALRhfleNHPLMKLTPAVQHHR 286
Cdd:cd01144  146 LMTAGG-DWVPELIALAGGVNVFADAGERSPQVSWEDVLAANPDVIVLSPCGFGFTPAILR----KEPAWQALPAVRNGR 220

                        250       260       270
                 ....*....|....*....|....*....|..
gi 446655191 287 --------YLKlqyaeltPGPANVDAVEKLAR 310
Cdd:cd01144  221 vyavdgnwYFR-------PSPRLVDGLEQLAA 245
YvrC cd01143
Periplasmic binding protein YvrC. These proteins are predicted to function as initial ...
 37-254 2.77e-20

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: 86.56  E-value: 2.77e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655191  37 GPPKRAVINDLNMSEMAFALHLQDRIVGLTGISGWYKMTPEfKKAMGSIPElapkyPTLETLLAAEPDFFFAgwNYGMKv 116
Cdd:cd01143    1 KEPERIVSLSPSITEILFALGAGDKIVGVDTYSNYPKEVRK-KPKVGSYSN-----PNVEKIVALKPDLVIV--SSSSL- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655191 117 gGEVTpDTLSKYGIKTFVLsescvfttahKNKATMDLLYNDVLTLGKIFGKRNDAQSLVSGWKKRLNELPKPAAGTRPLK 196
Cdd:cd01143   72 -AELL-EKLKDAGIPVVVL----------PAASSLDEIYDQIELIGKITGAEEEAEKLVKEMKQKIDKVKDKGKTIKKSK 139

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446655191 197 VFvYDSGEDKPFTSGKYAMPTAIIEAAGGKNVMEAVdTSWGTTSWESVAATEPDFIIL 254
Cdd:cd01143  140 VY-IEVSLGGPYTAGKNTFINELIRLAGAKNIAADS-GGWPQVSPEEILKANPDVIIL 195
TroA_e cd01142
Periplasmic binding protein TroA_e. These proteins are predicted to function as initial ...
 17-316 4.00e-20

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: 88.18  E-value: 4.00e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655191  17 ASAADFPVTIEScGTPVTFAGPPKRAVINDLNMSEMAFALHLQDRIVGLTGISGWykmTPEFKKAMGSIPELAPKY---- 92
Cdd:cd01142    3 ATAATRTITDMA-GRKVTIPDEVKRIAALWGAGNAVVAALGGGKLIVATTSTVQQ---EPWLYRLAPSLENVATGGtgnd 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655191  93 PTLETLLAAEPDFFFAgWNYGMKVGGEVTPDTLSKYGIKTFVLSEScvfttahKNKATMdllyndvltLGKIFGKRNDAQ 172
Cdd:cd01142   79 VNIEELLALKPDVVIV-WSTDGKEAGKAVLRLLNALSLRDAELEEV-------KLTIAL---------LGELLGRQEKAE 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655191 173 SLVSGWKKRLNELpkpAAGTRPL----KVFVYDSGEDKPFTSGKYAMPTAIIEAAGGKNVM-EAVDTSWGTTSWESVAAT 247
Cdd:cd01142  142 ALVAYFDDNLAYV---AARTKKLpdseRPRVYYAGPDPLTTDGTGSITNSWIDLAGGINVAsEATKKGSGEVSLEQLLKW 218

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446655191 248 EPDFIILldyQTGSGADALRhfleNHPLMKLTPAVQHHR-YLKLQYAELTPGPANVDAVEK--LARAMYPST 316
Cdd:cd01142  219 NPDVIIV---GNADTKAAIL----ADPRWQNLRAVKNGRvYVNPEGAFWWDRPSAEEALLGlwLAKTLYPER 283
TroA-like cd00636
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function ...
 40-202 1.21e-19

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: 83.76  E-value: 1.21e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655191  40 KRAVINDLNMSEMAFALHLQDRIVGLTGISGWYKMTPEFKKAMGSIPELapKYPTLETLLAAEPDFFFAGWNYGmkvggE 119
Cdd:cd00636    1 KRVVALDPGATELLLALGGDDKPVGVADPSGYPPEAKALLEKVPDVGHG--YEPNLEKIAALKPDLIIANGSGL-----E 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655191 120 VTPDTLSKYGIKTFVLSESCVFTtahknkatMDLLYNDVLTLGKIFGKRNDAQSLVSGWKKRLNELPKPAAGTRPLKVFV 199
Cdd:cd00636   74 AWLDKLSKIAIPVVVVDEASELS--------LENIKESIRLIGKALGKEENAEELIAELDARLAELRAKLAKIPKKKVSL 145


                 ...
gi 446655191 200 YDS 202
Cdd:cd00636  146 VVG 148
Peripla_BP_2 pfam01497
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ...
 51-286 1.54e-18

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: 82.80  E-value: 1.54e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655191   51 EMAFALHLQDRIVGltgISGWYKMtPEFKKAMGSIPEL-APKYPTLETLLAAEPDFFFAGWNYGMkvggEVTPDTLSKyG 129
Cdd:pfam01497   9 EILYALGATDSIVG---VDAYTRD-PLKADAVAAIVKVgAYGEINVERLAALKPDLVILSTGYLT----DEAEELLSL-I 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655191  130 IKTFVLSESCVFttahknkatmDLLYNDVLTLGKIFGKRNDAQSLVSGWKKRLNELPKPAAGTRPLKVFVYDSGEDKPFT 209
Cdd:pfam01497  80 IPTVIFESSSTG----------ESLKEQIKQLGELLGLEDEAEELVAEIDSALAAAKKAVPSLTRKPVLVFGGADGGGYV 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655191  210 -SGKYAMPTAIIEAAGGKNVMEAVDTS-WGTTSWESVAATEPDFIILLDY--QTGSGADalrhFLENHPLMKLTPAVQHH 285
Cdd:pfam01497 150 vAGSNTYIGDLLRILGIENIAAELSGSeYAPISFEAILSSNPDVIIVSGRdsFTKTGPE----FVAANPLWAGLPAVKNG 225


                  .
gi 446655191  286 R 286
Cdd:pfam01497 226 R 226
HutB cd01149
Hemin binding protein HutB. These proteins have been shown to function as initial receptors ...
 39-288 1.87e-16

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: 76.92  E-value: 1.87e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655191  39 PKRAVINDLNMSEMAFALHLQDRIVGLTGISGWykmtpefkkamgsiPELAPKYPTL--------ETLLAAEPDFFFAgw 110
Cdd:cd01149    1 PERIVSLGGSVTEIVYALGAGDRLVGVDSTSTY--------------PEAAAKLPDVgymrqlsaEGVLSLKPTLVIA-- 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655191 111 NYGMkvGGEVTPDTLSKYGIKTFVLSEScvfttahknkATMDLLYNDVLTLGKIFGKRNDAQSLVSGWKKRLNELPK-PA 189
Cdd:cd01149   65 SDEA--GPPEALDQLRAAGVPVVTVPST----------PTLDGLLTKIRQVAQALGVPEKGEALAQEVRQRLAALRKtVA 132

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655191 190 AGTRPLKV-FVYDSGEDKPFTSGKYAMPTAIIEAAGGKNVMEAVDtSWGTTSWESVAATEPDFIILLDyqTGSGADALRH 268
Cdd:cd01149  133 AHKKPPRVlFLLSHGGGAAMAAGRNTAADAIIALAGAVNAAAGFR-GYKPLSAEALIAAQPDVILVMS--RGLDAVGGVD 209

                        250       260
                 ....*....|....*....|
gi 446655191 269 FLENHPLMKLTPAVQHHRYL 288
Cdd:cd01149  210 GLLKLPGLAQTPAGRNKRIL 229
FhuD cd01146
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ...
 37-290 3.45e-13

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: 68.08  E-value: 3.45e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655191  37 GPPKRAVINDLNMSEMAFALHLQdrIVGLTGISGWYKMTPEFKKAMGSIPELAPKY-PTLETLLAAEPDFFFAGWNYGMK 115
Cdd:cd01146    1 AKPQRIVALDWGALETLLALGVK--PVGVADTAGYKPWIPEPALPLEGVVDVGTRGqPNLEAIAALKPDLILGSASRHDE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655191 116 VggevtPDTLSKygIKTFVLSEScvFTTAHKNKATmdllyndVLTLGKIFGKRNDAQSLVSGWKKRLNELPKPAAGTRPL 195
Cdd:cd01146   79 I-----YDQLSQ--IAPTVLLDS--SPWLAEWKEN-------LRLIAKALGKEEEAEKLLAEYDQRLAELRQKLPDKGPK 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655191 196 KVFVYD-SGEDKPFTSGKYAMPTAIIEAAG---GKNVMEAVDTSWGTTSWESVAATEPDFIILLDYQTGSGADAlrhfLE 271
Cdd:cd01146  143 PVSVVRfSDAGSIRLYGPNSFAGSVLEDLGlqnPWAQETTNDSGFATISLERLAKADADVLFVFTYEDEELAQA----LQ 218

                        250
                 ....*....|....*....
gi 446655191 272 NHPLMKLTPAVQHHRYLKL 290
Cdd:cd01146  219 ANPLWQNLPAVKNGRVYVV 237
HemV-2 cd01147
Metal binding protein HemV-2. These proteins are predicted to function as initial receptors ...
 22-286 3.23e-11

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: 62.74  E-value: 3.23e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655191  22 FPVTIEScgtpVTFAGPPkravindlnMSEMAFALHLQDRIVGLTGIsgwyKMTPEFKKAMGSIPELApKYPTL------ 95
Cdd:cd01147    1 VPKPVER----VVAAGPG---------ALRLLYALAAPDKIVGVDDA----EKSDEGRPYFLASPELK-DLPVIgrggrg 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655191  96 -----ETLLAAEPDFFFAGWNYGmkvgGEVTPDTLS-KYGIKTFVLSESCVFTTahknkatmdlLYNDVLTLGKIFGKRN 169
Cdd:cd01147   63 ntpnyEKIAALKPDVVIDVGSDD----PTSIADDLQkKTGIPVVVLDGGDSLED----------TPEQIRLLGKVLGKEE 128

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655191 170 DAQSLVSGWKKRLNEL----PKPAAGTRPlKVFVYDSGEDKP--FTSG--KYAMPtaiIEAAGGKNVMEAVDTSWGTT-S 240
Cdd:cd01147  129 RAEELISFIESILADVeertKDIPDEEKP-TVYFGRIGTKGAagLESGlaGSIEV---FELAGGINVADGLGGGGLKEvS 204

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 446655191 241 WESVAATEPDFIILldyQTGSGADALRHFLENHPLMKLTPAVQHHR 286
Cdd:cd01147  205 PEQILLWNPDVIFL---DTGSFYLSLEGYAKNRPFWQSLKAVKNGR 247
FecB COG4594
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and ...
 1-286 4.24e-10

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


Pssm-ID: 443650 [Multi-domain]  Cd Length: 316  Bit Score: 59.93  E-value: 4.24e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655191   1 MKKLFISLLAVLSASVASA-------------ADFPVTIE-SCGTpVTFAGPPKRAVINDLNMSEMAFALHLQDriVGLT 66
Cdd:COG4594    1 MKKLLLLLILLLALLLLAAcgssssdsssseaAAGARTVKhAMGE-TTIPGTPKRVVVLEWSFADALLALGVTP--VGIA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655191  67 GISGWYKMTPEFKKAM------GSIPElapkyPTLETLLAAEPDFFFAGwnygmKVGGEVTPDTLSKygIKTFVLSEScv 140
Cdd:COG4594   78 DDNDYDRWVPYLRDLIkgvtsvGTRSQ-----PNLEAIAALKPDLIIAD-----KSRHEAIYDQLSK--IAPTVLFKS-- 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655191 141 fttahkNKATMDLLYNDVLTLGKIFGKRNDAQSLVSGWKKRLNEL-PKPAAGTRPLKVFVYDSGEDKPFTSGKYAMPTAI 219
Cdd:COG4594  144 ------RNGDYQENLESFKTIAKALGKEEEAEAVLADHDQRIAEAkAKLAAADKGKKVAVGQFRADGLRLYTPNSFAGSV 217

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655191 220 IEAAGGKNVMEAVDT-SWG--TTSWESVAATEPDFIILLDYQTGSGADALrhflENHPLMKLTPAVQHHR 286
Cdd:COG4594  218 LAALGFENPPKQSKDnGYGysEVSLEQLPALDPDVLFIATYDDPSILKEW----KNNPLWKNLKAVKNGR 283
FatB cd01140
Siderophore binding protein FatB. These proteins have been shown to function as ABC-type ...
 32-313 2.25e-09

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: 57.27  E-value: 2.25e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655191  32 PVTFAGPPKRAVINDLNMSEMAFALHLqdRIVGLTGISGwykmTPEFKKAM--GSIPEL-APKYPTLETLLAAEPDFFFA 108
Cdd:cd01140    5 ETKVPKNPEKVVVFDVGALDTLDALGV--KVVGVPKSST----LPEYLKKYkdDKYANVgTLFEPDLEAIAALKPDLIII 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655191 109 GwnygmkvggevtpDTLSKYGIKTFVLSESCVFTTAHKNkaTMDLLYNDVLTLGKIFGKRNDAQSLVSGWKKRLNELPKP 188
Cdd:cd01140   79 G-------------GRLAEKYDELKKIAPTIDLGADLKN--YLESVKQNIETLGKIFGKEEEAKELVAEIDASIAEAKSA 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655191 189 AAGTRPLKVFVYDSGEDKPFTSGKYAMPtaIIEAAGGKNVMEAVDTS-WGTT-SWESVAATEPDFIILLD--YQTGSGAD 264
Cdd:cd01140  144 AKGKKKALVVLVNGGKLSAFGPGSRFGW--LHDLLGFEPADENIKASsHGQPvSFEYILEANPDWLFVIDrgAAIGAEGS 221

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446655191 265 ALRHFLENhPLMKLTPAVQHHR--YLKLQYAELTPGpaNVDAVEKLARAMY 313
Cdd:cd01140  222 SAKEVLDN-DLVKNTTAWKNGKviYLDPDLWYLSGG--GLESLKQMIDDLK 269
CeuA COG4607
ABC-type enterochelin transport system, periplasmic component [Inorganic ion transport and ...
 1-283 7.99e-09

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


Pssm-ID: 443657 [Multi-domain]  Cd Length: 310  Bit Score: 55.96  E-value: 7.99e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655191   1 MKKLFISLLAVLSASV------------ASAADFPVTIESCGTPVTFAGPPKRAVINDLNMSEMAFALHlqdriVGLTGI 68
Cdd:COG4607    1 MKKTLLAALALAAALAlaacgsssaaaaSAAAAETVTVEHALGTVEVPKNPKRVVVFDNGALDTLDALG-----VEVAGV 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655191  69 SGwyKMTPEFKKA--------MGSIPElapkyPTLETLLAAEPDFFFagwnygmkVGGEVTP--DTLSKYGiKTFVLSES 138
Cdd:COG4607   76 PK--GLLPDYLSKyaddkyanVGTLFE-----PDLEAIAALKPDLII--------IGGRSAKkyDELSKIA-PTIDLTVD 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655191 139 cvfttahkNKATMDLLYNDVLTLGKIFGKRNDAQSLVSGWKKRLNELpKPAAgTRPLKVFV--YDSGEDKPFTSG-KYAM 215
Cdd:COG4607  140 --------GEDYLESLKRNTETLGEIFGKEDEAEELVADLDAKIAAL-KAAA-AGKGTALIvlTNGGKISAYGPGsRFGP 209

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446655191 216 ptaIIEAAGGKNVMEAVDTSwgtT-----SWESVAATEPDFIILLDY--QTGSGADALRHFLENhPLMKLTPAVQ 283
Cdd:COG4607  210 ---IHDVLGFKPADEDIEAS---ThgqaiSFEFIAEANPDWLFVIDRdaAIGGEGPAAKQVLDN-ELVKQTTAWK 277
TroA_f cd01139
Periplasmic binding protein TroA_f. These proteins are predicted to function as initial ...
 30-315 4.82e-07

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


Pssm-ID: 238559 [Multi-domain]  Cd Length: 342  Bit Score: 50.77  E-value: 4.82e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655191  30 GTPVTFAGPPKRAVINDLNMSEMAFALH---LQDRIVGLTGisGWYKMTPEFKKAMGSI-PELApKYPT----------L 95
Cdd:cd01139    8 GRKVTLDAPVERVLLGEGRQLYALALLEgenPFARIVGWGG--DLKKGDPDTYAKYKEKfPEIA-DIPLigstyngdfsV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655191  96 ETLLAAEPDF-FFAGWNYGMKVGGEVTPdTLSKYGIKTfvlsescVFTTAHknkatMDLLYN---DVLTLGKIFGKRNDA 171
Cdd:cd01139   85 EKVLTLKPDLvILNIWAKTTAEESGILE-KLEQAGIPV-------VFVDFR-----QKPLKNttpSMRLLGKALGREERA 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655191 172 QSLVSGWKKRLNELPKPAAGTRPLKVFVY----DSGEDKPFTSGKYAMPTAIIEAAGGKNVMEA-VDTSWGTTSWESVAA 246
Cdd:cd01139  152 EEFIEFYQERIDRIRDRLAKINEPKPKVFielgAGGPEECCSTYGNGNWGELVDAAGGDNIADGlIPGTSGELNAEYVIA 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655191 247 TEPDFIIL---------------LDYQTGSGADALRHFLENHPLMKLTPAVQHHRYLKLqYAELTPGPANVDAVEKLARA 311
Cdd:cd01139  232 ANPEIIIAtggnwakdpsgvslgPDGTTADAKESLLRALLKRPGWSSLQAVKNGRVYAL-WHQFYRSPYNFVALEAFAKW 310


                 ....
gi 446655191 312 MYPS 315
Cdd:cd01139  311 LYPE 314
PRK03379 PRK03379
vitamin B12-transporter protein BtuF; Provisional
 50-254 1.73e-05

vitamin B12-transporter protein BtuF; Provisional


Pssm-ID: 179575 [Multi-domain]  Cd Length: 260  Bit Score: 45.45  E-value: 1.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655191  50 SEMAFAlhlqdriVGLT--GISGWYKMTPEFKKamgsIPELAP-KYPTLETLLAAEPDFFFAgWNYGmkvGGEVTPDTLS 126
Cdd:PRK03379  28 TELAFA-------AGITpvGVSSYSDYPPQAKK----IEQVATwQGMNLERIVALKPDLVLA-WRGG---NAERQVDQLA 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446655191 127 KYGIKTFVLSEScvfttahknkaTMDLLYNDVLTLGKIFGKRNDAQSLVSGWKKRLNELPKPAAGTRPLKVFVyDSGEDK 206
Cdd:PRK03379  93 SLGIKVMWVDAT-----------SIEQIANALRQLAPWSPQPEKAEQAAQSLLQQYAALKAQYADKPKKRVFL-QFGTNP 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 446655191 207 PFTSGKYAMPTAIIEAAGGKNVMEAVDTSWGTTSWESVAATEPDFIIL 254
Cdd:PRK03379 161 LFTSGKHSIQSQVLSLCGGENIFADSRVPWPQVSREQVLARKPQAIVI 208
 
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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