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Conserved domains on  [gi|489081004|ref|WP_002990938|]
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iron-hydroxamate ABC transporter substrate-binding protein [Streptococcus pyogenes]

Protein Classification

iron-hydroxamate ABC transporter substrate-binding protein( domain architecture ID 10100137)

iron-hydroxamate ABC transporter substrate-binding protein functions as the initial receptor in the ABC transport of iron(3+)-hydroxamate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FeuA cd01138
Periplasmic binding protein FeuA. These proteins have predicted to function as initial ...
 46-291 7.99e-83

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: 250.33  E-value: 7.99e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489081004  46 YYGDIPKQPKRVVSLASTYTGYLKkLDMNLVGVTSYDKKNPILAKTV--KKAKQVTATDLEAITTLKPDLIVVGST-EEN 122
Cdd:cd01138    1 GEVEIPAKPKRIVALSGETEGLAL-LGIKPVGAASIGGKNPYYKKKTlaKVVGIVDEPNLEKVLELKPDLIIVSSKqEEN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489081004 123 IKQLAEIAPVISIEYRKRDYLQVLSDFGRIFNKEGKAKKWLKDWKTKTAAYEKEVKAVTGDKATFTIMGLyEKDVYLFGK 202
Cdd:cd01138   80 YEKLSKIAPTVPVSYNSSDWEEQLKEIGKLLNKEDEAEKWLADYKQKAKEAKEKIKKKLGNDKSVAVLRG-RKQIYVFGE 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489081004 203 DWGRGGEVIHQAFHYDAPEKVKTEVFKQGYLSLSQEVLPDYIGDYVVVAAEDDKTGSALYES-KLWQSIPAVKKHHVIKV 281
Cdd:cd01138  159 DGRGGGPILYADLGLKAPEKVKEIEDKPGYAAISLEVLPEFDADYIFLLFFTGPEAKADFESlPIWKNLPAVKNNHVYIV 238

                        250
                 ....*....|
gi 489081004 282 NANVFYFTDP 291
Cdd:cd01138  239 DAWVFYFADG 248
 
Name Accession Description Interval E-value
FeuA cd01138
Periplasmic binding protein FeuA. These proteins have predicted to function as initial ...
 46-291 7.99e-83

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: 250.33  E-value: 7.99e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489081004  46 YYGDIPKQPKRVVSLASTYTGYLKkLDMNLVGVTSYDKKNPILAKTV--KKAKQVTATDLEAITTLKPDLIVVGST-EEN 122
Cdd:cd01138    1 GEVEIPAKPKRIVALSGETEGLAL-LGIKPVGAASIGGKNPYYKKKTlaKVVGIVDEPNLEKVLELKPDLIIVSSKqEEN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489081004 123 IKQLAEIAPVISIEYRKRDYLQVLSDFGRIFNKEGKAKKWLKDWKTKTAAYEKEVKAVTGDKATFTIMGLyEKDVYLFGK 202
Cdd:cd01138   80 YEKLSKIAPTVPVSYNSSDWEEQLKEIGKLLNKEDEAEKWLADYKQKAKEAKEKIKKKLGNDKSVAVLRG-RKQIYVFGE 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489081004 203 DWGRGGEVIHQAFHYDAPEKVKTEVFKQGYLSLSQEVLPDYIGDYVVVAAEDDKTGSALYES-KLWQSIPAVKKHHVIKV 281
Cdd:cd01138  159 DGRGGGPILYADLGLKAPEKVKEIEDKPGYAAISLEVLPEFDADYIFLLFFTGPEAKADFESlPIWKNLPAVKNNHVYIV 238

                        250
                 ....*....|
gi 489081004 282 NANVFYFTDP 291
Cdd:cd01138  239 DAWVFYFADG 248
FecB COG4594
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and ...
 19-307 5.10e-37

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


Pssm-ID: 443650 [Multi-domain]  Cd Length: 316  Bit Score: 134.28  E-value: 5.10e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489081004  19 ACGNQATNHSNTASKSLSPMPQIA-GVTyygDIPKQPKRVVSLASTYTGYLKKLDMNLVGVTSYDKKNPILAKTVKKAKQ 97
Cdd:COG4594   19 ACGSSSSDSSSSEAAAGARTVKHAmGET---TIPGTPKRVVVLEWSFADALLALGVTPVGIADDNDYDRWVPYLRDLIKG 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489081004  98 VT------ATDLEAITTLKPDLIVVGST--EENIKQLAEIAPVISIEYRKRDYLQVLSDF---GRIFNKEGKAKKWLKDW 166
Cdd:COG4594   96 VTsvgtrsQPNLEAIAALKPDLIIADKSrhEAIYDQLSKIAPTVLFKSRNGDYQENLESFktiAKALGKEEEAEAVLADH 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489081004 167 KTKTAAYEKEVK-AVTGDKATFTIMglYEKDVYLFGKDWGRGGeVIHQA-FHYdAPEKVKTEVFkqGYLSLSQEVLPDYI 244
Cdd:COG4594  176 DQRIAEAKAKLAaADKGKKVAVGQF--RADGLRLYTPNSFAGS-VLAALgFEN-PPKQSKDNGY--GYSEVSLEQLPALD 249

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489081004 245 GDYVVVAAEDDKT-GSALYESKLWQSIPAVKKHHVIKVNANV-FYFTDPLSLEYQLESLREAILS 307
Cdd:COG4594  250 PDVLFIATYDDPSiLKEWKNNPLWKNLKAVKNGRVYEVDGDLwTRGRGPLAAELMADDLVEILLK 314
Peripla_BP_2 pfam01497
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ...
 58-279 7.54e-21

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: 88.96  E-value: 7.54e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489081004   58 VSLASTYTGYLKKLDM--NLVGVTSYDKKNPIL--AKTVKKAKQVTATDLEAITTLKPDLIVVGS---TEENIKQLAEIA 130
Cdd:pfam01497   1 AALSPAYTEILYALGAtdSIVGVDAYTRDPLKAdaVAAIVKVGAYGEINVERLAALKPDLVILSTgylTDEAEELLSLII 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489081004  131 PVISIEYRK--RDYLQVLSDFGRIFNKEGKAKKWLKDWKTKTAAYEKEVKAVTgDKATFTIMGLYEKDVYLFGkDWGRGG 208
Cdd:pfam01497  81 PTVIFESSStgESLKEQIKQLGELLGLEDEAEELVAEIDSALAAAKKAVPSLT-RKPVLVFGGADGGGYVVAG-SNTYIG 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489081004  209 EVIHQA-FHYDAPEKVKtevfkQGYLSLSQEVLPDYIGDYVVVAAEDDKTGS---ALYESKLWQSIPAVKKHHVI 279
Cdd:pfam01497 159 DLLRILgIENIAAELSG-----SEYAPISFEAILSSNPDVIIVSGRDSFTKTgpeFVAANPLWAGLPAVKNGRVY 228
fecB PRK11411
iron-dicitrate transporter substrate-binding subunit; Provisional
 50-284 4.89e-17

iron-dicitrate transporter substrate-binding subunit; Provisional


Pssm-ID: 183123 [Multi-domain]  Cd Length: 303  Bit Score: 79.72  E-value: 4.89e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489081004  50 IPKQPKRVVSLASTYTGYLKKLDMNLVGVTSYDKKNPILAKTVKKAKQVTAT------DLEAITTLKPDLIVVGSTEEN- 122
Cdd:PRK11411  35 LEKTPQRIVVLELSFVDALAAVGVSPVGVADDNDAKRILPEVRAHLKPWQSVgtrsqpSLEAIAALKPDLIIADSSRHAg 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489081004 123 -IKQLAEIAPVISIEYRKRDY---LQVLSDFGRIFNKEGKAKKWLKDWKTKTAAYEKEVKAvtGDKATFTI-----MGLY 193
Cdd:PRK11411 115 vYIALQKIAPTLLLKSRNETYqenLQSAAIIGEVLGKKREMQARIEQHKERMAQFASQLPK--GTRVAFGTsreqqFNLH 192

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489081004 194 EKDVYlfgkdwgrGGEVIhQAFHYDAPEKVKTEvfkQGYLSLSQEVLPDYIGDYVVVAAEDDKTGSALYESK-LWQSIPA 272
Cdd:PRK11411 193 SPESY--------TGSVL-AALGLNVPKAPMNG---AAMPSISLEQLLALNPDWLLVAHYRQESIVKRWQQDpLWQMLTA 260

                        250
                 ....*....|..
gi 489081004 273 VKKHHVIKVNAN 284
Cdd:PRK11411 261 AKKQQVASVDSN 272
 
Name Accession Description Interval E-value
FeuA cd01138
Periplasmic binding protein FeuA. These proteins have predicted to function as initial ...
 46-291 7.99e-83

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: 250.33  E-value: 7.99e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489081004  46 YYGDIPKQPKRVVSLASTYTGYLKkLDMNLVGVTSYDKKNPILAKTV--KKAKQVTATDLEAITTLKPDLIVVGST-EEN 122
Cdd:cd01138    1 GEVEIPAKPKRIVALSGETEGLAL-LGIKPVGAASIGGKNPYYKKKTlaKVVGIVDEPNLEKVLELKPDLIIVSSKqEEN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489081004 123 IKQLAEIAPVISIEYRKRDYLQVLSDFGRIFNKEGKAKKWLKDWKTKTAAYEKEVKAVTGDKATFTIMGLyEKDVYLFGK 202
Cdd:cd01138   80 YEKLSKIAPTVPVSYNSSDWEEQLKEIGKLLNKEDEAEKWLADYKQKAKEAKEKIKKKLGNDKSVAVLRG-RKQIYVFGE 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489081004 203 DWGRGGEVIHQAFHYDAPEKVKTEVFKQGYLSLSQEVLPDYIGDYVVVAAEDDKTGSALYES-KLWQSIPAVKKHHVIKV 281
Cdd:cd01138  159 DGRGGGPILYADLGLKAPEKVKEIEDKPGYAAISLEVLPEFDADYIFLLFFTGPEAKADFESlPIWKNLPAVKNNHVYIV 238

                        250
                 ....*....|
gi 489081004 282 NANVFYFTDP 291
Cdd:cd01138  239 DAWVFYFADG 248
FecB COG4594
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and ...
 19-307 5.10e-37

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


Pssm-ID: 443650 [Multi-domain]  Cd Length: 316  Bit Score: 134.28  E-value: 5.10e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489081004  19 ACGNQATNHSNTASKSLSPMPQIA-GVTyygDIPKQPKRVVSLASTYTGYLKKLDMNLVGVTSYDKKNPILAKTVKKAKQ 97
Cdd:COG4594   19 ACGSSSSDSSSSEAAAGARTVKHAmGET---TIPGTPKRVVVLEWSFADALLALGVTPVGIADDNDYDRWVPYLRDLIKG 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489081004  98 VT------ATDLEAITTLKPDLIVVGST--EENIKQLAEIAPVISIEYRKRDYLQVLSDF---GRIFNKEGKAKKWLKDW 166
Cdd:COG4594   96 VTsvgtrsQPNLEAIAALKPDLIIADKSrhEAIYDQLSKIAPTVLFKSRNGDYQENLESFktiAKALGKEEEAEAVLADH 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489081004 167 KTKTAAYEKEVK-AVTGDKATFTIMglYEKDVYLFGKDWGRGGeVIHQA-FHYdAPEKVKTEVFkqGYLSLSQEVLPDYI 244
Cdd:COG4594  176 DQRIAEAKAKLAaADKGKKVAVGQF--RADGLRLYTPNSFAGS-VLAALgFEN-PPKQSKDNGY--GYSEVSLEQLPALD 249

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489081004 245 GDYVVVAAEDDKT-GSALYESKLWQSIPAVKKHHVIKVNANV-FYFTDPLSLEYQLESLREAILS 307
Cdd:COG4594  250 PDVLFIATYDDPSiLKEWKNNPLWKNLKAVKNGRVYEVDGDLwTRGRGPLAAELMADDLVEILLK 314
FepB COG0614
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ...
 56-305 3.74e-33

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


Pssm-ID: 440379 [Multi-domain]  Cd Length: 264  Bit Score: 122.80  E-value: 3.74e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489081004  56 RVVSLASTYTGYLKKLDM--NLVGVTS--YDKKNPILAKTVKKAKQVTATDLEAITTLKPDLIVV---GSTEENIKQLAE 128
Cdd:COG0614    2 RIVSLSPSATELLLALGAgdRLVGVSDwgYCDYPELELKDLPVVGGTGEPNLEAILALKPDLVLAsssGNDEEDYEQLEK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489081004 129 I-APVISIEYRK-RDYLQVLSDFGRIFNKEGKAKKWLKDWKTKTAAYEKEVKAVTgDKATFTIMGLYEKDVYLFGKDWGR 206
Cdd:COG0614   82 IgIPVVVLDPRSlEDLYESIRLLGELLGREERAEALIAEYEARLAAVRARLAGAE-ERPTVLYEIWSGDPLYTAGGGSFI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489081004 207 GgEVIHQA-FHYDAPEKvktevfKQGYLSLSQEVL----PDYI--GDYVVVAAEDDKTGSALYESKLWQSIPAVKKHHVI 279
Cdd:COG0614  161 G-ELLELAgGRNVAADL------GGGYPEVSLEQVlaldPDVIilSGGGYDAETAEEALEALLADPGWQSLPAVKNGRVY 233

                        250       260
                 ....*....|....*....|....*.
gi 489081004 280 KVNANVFYFTDPLSLeYQLESLREAI 305
Cdd:COG0614  234 VVPGDLLSRPGPRLL-LALEDLAKAL 258
FhuD cd01146
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ...
 52-293 9.07e-33

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: 121.62  E-value: 9.07e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489081004  52 KQPKRVVSLASTYTGYLKKLDMNLVGVTSYDKKNPILAKTVKKAKQVT------ATDLEAITTLKPDLIVV--GSTEENI 123
Cdd:cd01146    1 AKPQRIVALDWGALETLLALGVKPVGVADTAGYKPWIPEPALPLEGVVdvgtrgQPNLEAIAALKPDLILGsaSRHDEIY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489081004 124 KQLAEIAPVISIEYRKRDY--LQVLSDFGRIFNKEGKAKKWLKDWKTKTAayekEVKAVTGDKA--TFTIMGLYEKD-VY 198
Cdd:cd01146   81 DQLSQIAPTVLLDSSPWLAewKENLRLIAKALGKEEEAEKLLAEYDQRLA----ELRQKLPDKGpkPVSVVRFSDAGsIR 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489081004 199 LFGKDwGRGGEVIHQA-FHYdaPEKVKTeVFKQGYLSLSQEVLPDYIGDYVVV-AAEDDKTGSALYESKLWQSIPAVKKH 276
Cdd:cd01146  157 LYGPN-SFAGSVLEDLgLQN--PWAQET-TNDSGFATISLERLAKADADVLFVfTYEDEELAQALQANPLWQNLPAVKNG 232

                        250
                 ....*....|....*..
gi 489081004 277 HVIKVNANVFYFTDPLS 293
Cdd:cd01146  233 RVYVVDDVWWFFGGGLS 249
FatB cd01140
Siderophore binding protein FatB. These proteins have been shown to function as ABC-type ...
 50-289 6.09e-21

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: 90.01  E-value: 6.09e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489081004  50 IPKQPKRVVSLASTYTGYLKKLDMNLVGVTSyDKKNPILAKTVKKAKQVTA-----TDLEAITTLKPDLIVV-GSTEENI 123
Cdd:cd01140    8 VPKNPEKVVVFDVGALDTLDALGVKVVGVPK-SSTLPEYLKKYKDDKYANVgtlfePDLEAIAALKPDLIIIgGRLAEKY 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489081004 124 KQLAEIAPVISIEYRKRDYLQVL----SDFGRIFNKEGKAKKWLKDWKtktaAYEKEVKAVTGDKATFTIMGLYEKDVYL 199
Cdd:cd01140   87 DELKKIAPTIDLGADLKNYLESVkqniETLGKIFGKEEEAKELVAEID----ASIAEAKSAAKGKKKALVVLVNGGKLSA 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489081004 200 FGKDwGRGGeVIHQAFhyDAPEKVKTEVFKQGYLSLSQEVL----PDYIgdYVV----VAAEDDKTGSALYESKLWQSIP 271
Cdd:cd01140  163 FGPG-SRFG-WLHDLL--GFEPADENIKASSHGQPVSFEYIleanPDWL--FVIdrgaAIGAEGSSAKEVLDNDLVKNTT 236

                        250
                 ....*....|....*...
gi 489081004 272 AVKKHHVIKVNANVFYFT 289
Cdd:cd01140  237 AWKNGKVIYLDPDLWYLS 254
Peripla_BP_2 pfam01497
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ...
 58-279 7.54e-21

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: 88.96  E-value: 7.54e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489081004   58 VSLASTYTGYLKKLDM--NLVGVTSYDKKNPIL--AKTVKKAKQVTATDLEAITTLKPDLIVVGS---TEENIKQLAEIA 130
Cdd:pfam01497   1 AALSPAYTEILYALGAtdSIVGVDAYTRDPLKAdaVAAIVKVGAYGEINVERLAALKPDLVILSTgylTDEAEELLSLII 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489081004  131 PVISIEYRK--RDYLQVLSDFGRIFNKEGKAKKWLKDWKTKTAAYEKEVKAVTgDKATFTIMGLYEKDVYLFGkDWGRGG 208
Cdd:pfam01497  81 PTVIFESSStgESLKEQIKQLGELLGLEDEAEELVAEIDSALAAAKKAVPSLT-RKPVLVFGGADGGGYVVAG-SNTYIG 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489081004  209 EVIHQA-FHYDAPEKVKtevfkQGYLSLSQEVLPDYIGDYVVVAAEDDKTGS---ALYESKLWQSIPAVKKHHVI 279
Cdd:pfam01497 159 DLLRILgIENIAAELSG-----SEYAPISFEAILSSNPDVIIVSGRDSFTKTgpeFVAANPLWAGLPAVKNGRVY 228
CeuA COG4607
ABC-type enterochelin transport system, periplasmic component [Inorganic ion transport and ...
 1-305 3.45e-20

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


Pssm-ID: 443657 [Multi-domain]  Cd Length: 310  Bit Score: 88.70  E-value: 3.45e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489081004   1 MKKLTLLLTLCLTTITLIACGNQATNHSNTASKSlspmpQIAGVTYYGD--IPKQPKRVVSL--ASTYTgyLKKLDMNLV 76
Cdd:COG4607    1 MKKTLLAALALAAALALAACGSSSAAAASAAAAE-----TVTVEHALGTveVPKNPKRVVVFdnGALDT--LDALGVEVA 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489081004  77 GVTSydkknPILAKTVKKAKQVTAT--------DLEAITTLKPDLIVVGS-TEENIKQLAEIAPVISIEYRKRDYLQVLS 147
Cdd:COG4607   74 GVPK-----GLLPDYLSKYADDKYAnvgtlfepDLEAIAALKPDLIIIGGrSAKKYDELSKIAPTIDLTVDGEDYLESLK 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489081004 148 D----FGRIFNKEGKAKKWLKDWKTKTAAYEkevKAVTGDKATFTIMGlYEKDVYLFGKDwGRGGeVIHQAFHY-DAPEK 222
Cdd:COG4607  149 RntetLGEIFGKEDEAEELVADLDAKIAALK---AAAAGKGTALIVLT-NGGKISAYGPG-SRFG-PIHDVLGFkPADED 222

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489081004 223 VKTEVFKQgylSLSQEVL----PDYIgdYVV----VAAEDDKTGSALYESKLWQSIPAVKKHHVIKVNANVFYFT--DPL 292
Cdd:COG4607  223 IEASTHGQ---AISFEFIaeanPDWL--FVIdrdaAIGGEGPAAKQVLDNELVKQTTAWKNGQIVYLDPDAWYLAggGIQ 297

                        330
                 ....*....|...
gi 489081004 293 SLEYQLESLREAI 305
Cdd:COG4607  298 SLTEMLDEVADAL 310
FepB COG4592
ABC-type Fe2+-enterobactin transport system, periplasmic component [Inorganic ion transport ...
 19-286 8.56e-19

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


Pssm-ID: 443649 [Multi-domain]  Cd Length: 330  Bit Score: 85.00  E-value: 8.56e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489081004  19 ACGNQATNHSNTASKSLSPMP-QIagVTYYGD--IPKQPKRVVSLASTYTGYLKKLDMNLVG-VTSY-----DKKNPILA 89
Cdd:COG4592   21 GCSSADSTASGTSTAAAGGWPrTV--TTEKGTvtLPAKPQRIVSTSVTLTGSLLAIDAPVVAsGATTpnnvtDDQGFFRQ 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489081004  90 -KTVKKAKQVTAT------DLEAITTLKPDLIVVG-----STEENIKQLAEIAPVISIEYRKRDYLQVLSDFGRIFNKEG 157
Cdd:COG4592   99 wADVAKERGVKRLyiglepNAEAIAAAAPDLIIGSatggdSALDLYDQLSAIAPTLVVNYDDKSWQELATQLGEATGHEA 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489081004 158 KAKKwlkdwktKTAAYEKEVKAVtgdKATFT-------IMGLYEKDVYLFGKDWGRGGEVIHQ-AFHYD-APEKVKTEVf 228
Cdd:COG4592  179 QADA-------VIAAFDARVAEV---KAAITlppqpvsALVYNEDGGANLWTPESAQGQLLQAlGFTLApLPAELATST- 247

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489081004 229 KQGY----LSLSQEVLPDYI-GDYVVVAAEDDKTGSALYESKLWQSIPAVKKHHVIKVNANVF 286
Cdd:COG4592  248 SQGKrgdiVQLSGENLAAALtGPTLFLFAADDKDVDALKADPLLAHLPAVQAGRVYALGPDSF 310
fecB PRK11411
iron-dicitrate transporter substrate-binding subunit; Provisional
 50-284 4.89e-17

iron-dicitrate transporter substrate-binding subunit; Provisional


Pssm-ID: 183123 [Multi-domain]  Cd Length: 303  Bit Score: 79.72  E-value: 4.89e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489081004  50 IPKQPKRVVSLASTYTGYLKKLDMNLVGVTSYDKKNPILAKTVKKAKQVTAT------DLEAITTLKPDLIVVGSTEEN- 122
Cdd:PRK11411  35 LEKTPQRIVVLELSFVDALAAVGVSPVGVADDNDAKRILPEVRAHLKPWQSVgtrsqpSLEAIAALKPDLIIADSSRHAg 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489081004 123 -IKQLAEIAPVISIEYRKRDY---LQVLSDFGRIFNKEGKAKKWLKDWKTKTAAYEKEVKAvtGDKATFTI-----MGLY 193
Cdd:PRK11411 115 vYIALQKIAPTLLLKSRNETYqenLQSAAIIGEVLGKKREMQARIEQHKERMAQFASQLPK--GTRVAFGTsreqqFNLH 192

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489081004 194 EKDVYlfgkdwgrGGEVIhQAFHYDAPEKVKTEvfkQGYLSLSQEVLPDYIGDYVVVAAEDDKTGSALYESK-LWQSIPA 272
Cdd:PRK11411 193 SPESY--------TGSVL-AALGLNVPKAPMNG---AAMPSISLEQLLALNPDWLLVAHYRQESIVKRWQQDpLWQMLTA 260

                        250
                 ....*....|..
gi 489081004 273 VKKHHVIKVNAN 284
Cdd:PRK11411 261 AKKQQVASVDSN 272
TroA-like cd00636
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function ...
 55-187 5.76e-17

Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function in the ABC transport of ferric siderophores and metal ions such as Mn2+, Fe3+, Cu2+ and/or Zn2+. Their ligand binding site is formed in the interface between two globular domains linked by a single helix. Many of these proteins also possess a low complexity region containing a metal-binding histidine-rich motif (repetitive HDH sequence). The TroA-like proteins differ in their fold and ligand-binding mechanism from the PBPI and PBPII proteins, but are structurally similar, however, to the beta-subunit of the nitrogenase molybdenum-iron protein MoFe. Most TroA-like proteins are encoded by ABC-type operons and appear to function as periplasmic components of ABC transporters in metal ion uptake.


Pssm-ID: 238347 [Multi-domain]  Cd Length: 148  Bit Score: 76.44  E-value: 5.76e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489081004  55 KRVVSLASTYTGYLKKL--DMNLVGVTSYDKKNPILAKTVKKAKQVTAT---DLEAITTLKPDLIVVGST--EENIKQLA 127
Cdd:cd00636    1 KRVVALDPGATELLLALggDDKPVGVADPSGYPPEAKALLEKVPDVGHGyepNLEKIAALKPDLIIANGSglEAWLDKLS 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489081004 128 EIA-PVISIEYR----KRDYLQVLSDFGRIFNKEGKAKKWLKDWKTKTAAYEKEVKAVTGDKATF 187
Cdd:cd00636   81 KIAiPVVVVDEAselsLENIKESIRLIGKALGKEENAEELIAELDARLAELRAKLAKIPKKKVSL 145
PRK10957 PRK10957
iron-enterobactin transporter periplasmic binding protein; Provisional
 50-286 1.15e-15

iron-enterobactin transporter periplasmic binding protein; Provisional


Pssm-ID: 236806 [Multi-domain]  Cd Length: 317  Bit Score: 76.17  E-value: 1.15e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489081004  50 IPKQPKRVVSLASTYTGYLKKLDMNLV--GVTSydkKNPILAK---------TVKKAKQV-----TATDLEAITTLKPDL 113
Cdd:PRK10957  40 LESKPQRIVSTSVTLTGTLLAIDAPVIasGATT---PNTRVADdqgffrqwsDVAKERGVevlyiGEPDAEAVAAQMPDL 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489081004 114 IVVG-----STEENIKQLAEIAPVISIEYRKRDYLQVLSDFGRIFNKEGKAK-------KWLKDWKTKTAAYEKEVKAV- 180
Cdd:PRK10957 117 IVISatggdSALALYDQLSAIAPTLVIDYDDKSWQELATQLGEATGLEKQAAaviaqfdAQLAEVKAKITLPPQPVSALv 196

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489081004 181 -TGDKATFTImglyekdvylfGKDWGRGGEVIHQ-AFHY-DAPEKVKTEVfKQGYLS----LSQEVLPDYI-GDYVVVAA 252
Cdd:PRK10957 197 yNGAGHSANL-----------WTPESAQGQLLEQlGFTLaELPAGLQAST-SQGKRHdiiqLGGENLAAGLnGETLFLFA 264

                        250       260       270
                 ....*....|....*....|....*....|....
gi 489081004 253 EDDKTGSALYESKLWQSIPAVKKHHVIKVNANVF 286
Cdd:PRK10957 265 GDDKDADAFLADPLLANLPAVQNKQVYALGTDTF 298
TroA_e cd01142
Periplasmic binding protein TroA_e. These proteins are predicted to function as initial ...
 50-295 3.84e-13

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: 68.54  E-value: 3.84e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489081004  50 IPKQPKRVVSL--ASTYTGYLKKLDMNLVGVTSYDKKNPILAKTV----KKAKQVTATDL--EAITTLKPDLIVVGST-- 119
Cdd:cd01142   20 IPDEVKRIAALwgAGNAVVAALGGGKLIVATTSTVQQEPWLYRLApsleNVATGGTGNDVniEELLALKPDVVIVWSTdg 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489081004 120 EENIKQLAEIAPVISIEY-RKRDYLQVLSDFGRIFNKEGKAKKWLKDWKTKTAAYEKEVKAVTGDKatftimglyEKDVY 198
Cdd:cd01142  100 KEAGKAVLRLLNALSLRDaELEEVKLTIALLGELLGRQEKAEALVAYFDDNLAYVAARTKKLPDSE---------RPRVY 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489081004 199 LFGKDWG--RGGEVIHQAFHYDA-PEKVKTEVFKQGYLSLSQEVL----PDyigdyVVVAAEDDKTGsALYESKLWQSIP 271
Cdd:cd01142  171 YAGPDPLttDGTGSITNSWIDLAgGINVASEATKKGSGEVSLEQLlkwnPD-----VIIVGNADTKA-AILADPRWQNLR 244

                        250       260
                 ....*....|....*....|....
gi 489081004 272 AVKKHHVIKVNANVFYFTDPLSLE 295
Cdd:cd01142  245 AVKNGRVYVNPEGAFWWDRPSAEE 268
YvrC cd01143
Periplasmic binding protein YvrC. These proteins are predicted to function as initial ...
 52-203 8.05e-12

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: 63.07  E-value: 8.05e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489081004  52 KQPKRVVSL--ASTYTGYLKKLDMNLVGVTSYDKKNPILAKTVKKaKQVTATDLEAITTLKPDLIVV--GSTEENIKQLA 127
Cdd:cd01143    1 KEPERIVSLspSITEILFALGAGDKIVGVDTYSNYPKEVRKKPKV-GSYSNPNVEKIVALKPDLVIVssSSLAELLEKLK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489081004 128 EIA-PVISIeYRKRDYLQVLSDF---GRIFNKEGKAKKWLKDWKTKTAAYEKEVKAVTGDKATFTImglYEKDVYLFGKD 203
Cdd:cd01143   80 DAGiPVVVL-PAASSLDEIYDQIeliGKITGAEEEAEKLVKEMKQKIDKVKDKGKTIKKSKVYIEV---SLGGPYTAGKN 155
TroA_a cd01148
Metal binding protein TroA_a. These proteins are predicted to function as initial receptors ...
 52-284 2.63e-11

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: 63.13  E-value: 2.63e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489081004  52 KQPKRVVSLASTYTGYLKKLDM--NLVGVTSYDKK-NPILAKTVKKAKQVTATD--LEAITTLKPDLIVVGS-------- 118
Cdd:cd01148   16 KAPQRVVSNDQNTTEMMLALGLqdRMVGTAGIDNKdLPELKAKYDKVPELAKKYpsKETVLAARPDLVFGGWsygfdkgg 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489081004 119 -------TEENIKQLAEIAPVISI--EYRKRDYLQVLSDFGRIFNKEGKAKKWLKDWKTKTAAYEKEVKAVTGDKATFT- 188
Cdd:cd01148   96 lgtpdslAELGIKTYILPESCGQRrgEATLDDVYNDIRNLGKIFDVEDRADKLVADLKARLAEISAKVKGDGKKVAVFVy 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489081004 189 IMGlyEKDVYLFGKDwGRGGEVIHQAFHYDAPEKVKTEVFKQGYLSLSQEVlPDYI--GDYVVVAAEDDKTGsALYESKL 266
Cdd:cd01148  176 DSG--EDKPFTSGRG-GIPNAIITAAGGRNVFADVDESWTTVSWETVIARN-PDVIviIDYGDQNAAEQKIK-FLKENPA 250

                        250
                 ....*....|....*...
gi 489081004 267 WQSIPAVKKHHVIKVNAN 284
Cdd:cd01148  251 LKNVPAVKNNRFIVLPLA 268
BtuF cd01144
Cobalamin binding protein BtuF. These proteins have been shown to function as initial ...
 55-287 5.33e-11

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: 61.55  E-value: 5.33e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489081004  55 KRVVSLA--STYTGYLKKLDMNLVGVTSYDKKnPILAKTVKKAKQVTATDLEAITTLKPDLIVV---GSTEENIKQLAEI 129
Cdd:cd01144    1 MRIVSLApsATELLYALGLGDQLVGVTDYCDY-PPEAKKLPRVGGFYQLDLERVLALKPDLVIAwddCNVCAVVDQLRAA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489081004 130 A-PVISIEYRK-RDYLQVLSDFGRIFNKEGKAKKWLKDWKTKTAAYEKEVKAVTGDKATFTImglYEKDVYLFGKDW--- 204
Cdd:cd01144   80 GiPVLVSEPQTlDDILADIRRLGTLAGRPARAEELAEALRRRLAALRKQYASKPPPRVFYQE---WIDPLMTAGGDWvpe 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489081004 205 ---GRGGeviHQAFhYDAPEKVktevfkqGYLSLSqEVL---PDyigdyVVVAAEddkTGSALYESKL-----WQSIPAV 273
Cdd:cd01144  157 liaLAGG---VNVF-ADAGERS-------PQVSWE-DVLaanPD-----VIVLSP---CGFGFTPAILrkepaWQALPAV 216

                        250
                 ....*....|....
gi 489081004 274 KKHHVIKVNANVFY 287
Cdd:cd01144  217 RNGRVYAVDGNWYF 230
HemV-2 cd01147
Metal binding protein HemV-2. These proteins are predicted to function as initial receptors ...
 102-286 2.26e-07

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: 51.18  E-value: 2.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489081004 102 DLEAITTLKPDLIVVG------STEENIKQLAEIaPVISIEYRK-----RDYLQVLsdfGRIFNKEGKAKKwLKDWKTKt 170
Cdd:cd01147   66 NYEKIAALKPDVVIDVgsddptSIADDLQKKTGI-PVVVLDGGDsledtPEQIRLL---GKVLGKEERAEE-LISFIES- 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489081004 171 aaYEKEVKAVTGD-----KATFTIMGLYEKdvYLFGKDWGRGGEVihQAFHYDAPEKVKTEVFKQGYLSLSQEVL----P 241
Cdd:cd01147  140 --ILADVEERTKDipdeeKPTVYFGRIGTK--GAAGLESGLAGSI--EVFELAGGINVADGLGGGGLKEVSPEQIllwnP 213

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 489081004 242 DYIgdYVVVAAEDDKTGSALYESKLWQSIPAVKKHHVIKVNANVF 286
Cdd:cd01147  214 DVI--FLDTGSFYLSLEGYAKNRPFWQSLKAVKNGRVYLLPALPF 256
TroA_d cd01141
Periplasmic binding protein TroA_d. These proteins are predicted to function as initial ...
 54-166 4.27e-06

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: 46.26  E-value: 4.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489081004  54 PKRVVSLASTYTGYLKKLD--MNLVGVT--SYDKKNPILAKTVKKA-KQVTATDLEAITTLKPDLIVVG------STEEN 122
Cdd:cd01141    8 PKRIVVLSPTHVDLLLALDkaDKIVGVSasAYDLNTPAVKERIDIQvGPTGSLNVELIVALKPDLVILYggfqaqTILDK 87

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 489081004 123 IKQLAEIAPVISIEYRKRDYLQVLSDFGRIFN--KEGKAKKWLKDW 166
Cdd:cd01141   88 LEQLGIPVLYVNEYPSPLGRAEWIKFAAAFYGvgKEDKADEAFAQI 133
ChuT COG4558
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism] ...
 54-283 2.06e-05

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


Pssm-ID: 443619 [Multi-domain]  Cd Length: 285  Bit Score: 45.18  E-value: 2.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489081004  54 PKRVVSLASTYTGYLKKLDM--NLVGVTSYDKkNPILAKTVKK---AKQVTAtdlEAITTLKPDLIVVGST---EENIKQ 125
Cdd:COG4558   27 AERIVSLGGSVTEIVYALGAgdRLVGVDTTST-YPAAAKALPDvgyMRQLSA---EGILSLKPTLVLASEGagpPEVLDQ 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489081004 126 L--AEIaPVISI--EYRKRDYLQVLSDFGRIFNKEGKAKKWLKDWKTKTAAYEKEVKAVTGDKATFTIMGLYEKDVYLFG 201
Cdd:COG4558  103 LraAGV-PVVVVpaAPSLEGVLAKIRAVAAALGVPEAGEALAARLEADLAALAARVAAIGKPPRVLFLLSRGGGRPMVAG 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489081004 202 KDWGrGGEVIHQAFHYDAPEKVKtevfkqGYLSLSQEVL----PDYIgdyVVVAAEDDKTGSAlyeSKLWQ-----SIPA 272
Cdd:COG4558  182 RGTA-ADALIRLAGGVNAAAGFE------GYKPLSAEALiaaaPDVI---LVMTRGLESLGGV---DGLLAlpglaQTPA 248

                        250
                 ....*....|.
gi 489081004 273 VKKHHVIKVNA 283
Cdd:COG4558  249 GKNKRIVAMDD 259
HutB cd01149
Hemin binding protein HutB. These proteins have been shown to function as initial receptors ...
 54-282 3.86e-04

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: 41.10  E-value: 3.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489081004  54 PKRVVSLASTYTGYLKKLDM--NLVGV--TSYDKKNPILAKTVKKAKQVTAtdlEAITTLKPDLiVVGSTE----ENIKQ 125
Cdd:cd01149    1 PERIVSLGGSVTEIVYALGAgdRLVGVdsTSTYPEAAAKLPDVGYMRQLSA---EGVLSLKPTL-VIASDEagppEALDQ 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489081004 126 LAEIA-PVISI--EYRKRDYLQVLSDFGRIFNKEGKAKKWLKDWKTKTAAYEKEVKAVTGDKATFTIMGLYEKDVYLFGK 202
Cdd:cd01149   77 LRAAGvPVVTVpsTPTLDGLLTKIRQVAQALGVPEKGEALAQEVRQRLAALRKTVAAHKKPPRVLFLLSHGGGAAMAAGR 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489081004 203 DWGRGGeVIHQAFHYDAPEKVktevfkQGYLSLSQEVL----PDYIgdyVVVAAEDDKTGS--ALYESKLWQSIPAVKKH 276
Cdd:cd01149  157 NTAADA-IIALAGAVNAAAGF------RGYKPLSAEALiaaqPDVI---LVMSRGLDAVGGvdGLLKLPGLAQTPAGRNK 226


                 ....*.
gi 489081004 277 HVIKVN 282
Cdd:cd01149  227 RILAMD 232
PRK03379 PRK03379
vitamin B12-transporter protein BtuF; Provisional
 56-127 2.70e-03

vitamin B12-transporter protein BtuF; Provisional


Pssm-ID: 179575 [Multi-domain]  Cd Length: 260  Bit Score: 38.51  E-value: 2.70e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489081004  56 RVVSLASTYTGYLKKLDMNLVGVTSYDKKNPilakTVKKAKQVTA---TDLEAITTLKPDLIVV---GSTEENIKQLA 127
Cdd:PRK03379  19 RVITLSPANTELAFAAGITPVGVSSYSDYPP----QAKKIEQVATwqgMNLERIVALKPDLVLAwrgGNAERQVDQLA 92
 
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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