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Conserved domains on  [gi|1201074194|gb|ARW55691|]
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putative ABC transporter substrate-binding lipoprotein YvrC [Bacillus licheniformis]

Protein Classification

ABC transporter substrate-binding protein( domain architecture ID 10100144)

uncharacterized ABC transporter substrate-binding protein, which functions as the initial receptor in ABC transport of metal ions or other substrates, and as asurface adhesin in some eubacterial species

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YvrC cd01143
Periplasmic binding protein YvrC. These proteins are predicted to function as initial ...
 56-256 2.98e-77

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: 234.48  E-value: 2.98e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201074194  56 KEPKKIVSLMPSNTEITYALGLGKKVVGVTDFDTYPKEVKNVEKIGGM-EFNTEKIISLNPDLVLAHASSMQSAeegLKQ 134
Cdd:cd01143     1 KEPERIVSLSPSITEILFALGAGDKIVGVDTYSNYPKEVRKKPKVGSYsNPNVEKIVALKPDLVIVSSSSLAEL---LEK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201074194 135 LKDAGITVVTVNDAASFEETYRSIEMIGKAAGAEDQAASLVKSMKSDLAGIKEKAAAISKadqKKVFVEVSPaPDIYTTG 214
Cdd:cd01143    78 LKDAGIPVVVLPAASSLDEIYDQIELIGKITGAEEEAEKLVKEMKQKIDKVKDKGKTIKK---SKVYIEVSL-GGPYTAG 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1201074194 215 KGTFMNEMLEAIHAENAASAQKGWAKITEEAIVKLNPDAIVT 256
Cdd:cd01143   154 KNTFINELIRLAGAKNIAADSGGWPQVSPEEILKANPDVIIL 195
 
Name Accession Description Interval E-value
YvrC cd01143
Periplasmic binding protein YvrC. These proteins are predicted to function as initial ...
 56-256 2.98e-77

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: 234.48  E-value: 2.98e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201074194  56 KEPKKIVSLMPSNTEITYALGLGKKVVGVTDFDTYPKEVKNVEKIGGM-EFNTEKIISLNPDLVLAHASSMQSAeegLKQ 134
Cdd:cd01143     1 KEPERIVSLSPSITEILFALGAGDKIVGVDTYSNYPKEVRKKPKVGSYsNPNVEKIVALKPDLVIVSSSSLAEL---LEK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201074194 135 LKDAGITVVTVNDAASFEETYRSIEMIGKAAGAEDQAASLVKSMKSDLAGIKEKAAAISKadqKKVFVEVSPaPDIYTTG 214
Cdd:cd01143    78 LKDAGIPVVVLPAASSLDEIYDQIELIGKITGAEEEAEKLVKEMKQKIDKVKDKGKTIKK---SKVYIEVSL-GGPYTAG 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1201074194 215 KGTFMNEMLEAIHAENAASAQKGWAKITEEAIVKLNPDAIVT 256
Cdd:cd01143   154 KNTFINELIRLAGAKNIAADSGGWPQVSPEEILKANPDVIIL 195
FepB COG0614
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ...
 60-315 2.73e-76

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


Pssm-ID: 440379 [Multi-domain]  Cd Length: 264  Bit Score: 234.51  E-value: 2.73e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201074194  60 KIVSLMPSNTEITYALGLGKKVVGVTD--FDTYPK-EVKNVEKIGGM-EFNTEKIISLNPDLVLAHASSMQsaEEGLKQL 135
Cdd:COG0614     2 RIVSLSPSATELLLALGAGDRLVGVSDwgYCDYPElELKDLPVVGGTgEPNLEAILALKPDLVLASSSGND--EEDYEQL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201074194 136 KDAGITVVTVnDAASFEETYRSIEMIGKAAGAEDQAASLVKSMKSDLAGIKEKAAAIskADQKKVFVEVSPAPDIYTTGK 215
Cdd:COG0614    80 EKIGIPVVVL-DPRSLEDLYESIRLLGELLGREERAEALIAEYEARLAAVRARLAGA--EERPTVLYEIWSGDPLYTAGG 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201074194 216 GTFMNEMLEAIHAENAAS-AQKGWAKITEEAIVKLNPDAIVTTNG-------ESAVSEIKKRSGWSGVKAVKNNEVYDVD 287
Cdd:COG0614   157 GSFIGELLELAGGRNVAAdLGGGYPEVSLEQVLALDPDVIILSGGgydaetaEEALEALLADPGWQSLPAVKNGRVYVVP 236

                         250       260
                  ....*....|....*....|....*...
gi 1201074194 288 PDLVTRPGPRLIKGVEELAEHIYPDVFK 315
Cdd:COG0614   237 GDLLSRPGPRLLLALEDLAKALHPELFA 264
btuF PRK09534
corrinoid ABC transporter substrate-binding protein; Reviewed
 16-306 1.14e-40

corrinoid ABC transporter substrate-binding protein; Reviewed


Pssm-ID: 236552 [Multi-domain]  Cd Length: 359  Bit Score: 145.05  E-value: 1.14e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201074194  16 GVLSGCGQAQKPADEQKQEKAAEAFPVTIKDASGQEVKIEKEPKKIVSLMPSNTEITYALGLGKKVVGVTDFDTY---PK 92
Cdd:PRK09534   18 MTAAGGALAPAPAAQHADADRACSFPVTETDATGTEITLDERPERVVTLNPSAAQTMWELGARDRVVGVTQYASYldgAE 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201074194  93 EVKNVEKIGGMEFNTEKIISLNPDLVLAHASsmqSAEEGLKQLKDAGITVVTVNDAASFEETYRSIEMIGKAAGAEDQAA 172
Cdd:PRK09534   98 ERTNVSGGQPFGVNVEAVVGLDPDLVLAPNA---VAGDTVTRLREAGITVFHFPAATSIEDVAEKTATIGRLTGNCEAAA 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201074194 173 SLVKSMKSDLAGIKEKAAAISkaDQKKVFVevsPAPDIYTTGKGTFMNEMLEAIHAENAASAQK--GWAKITEEAIVKLN 250
Cdd:PRK09534  175 ETNAEMRDRVDAVEDRTADVD--DRPRVLY---PLGDGYTAGGNTFIGALIEAAGGHNVAADATtdGYPQLSEEVIVQQD 249

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1201074194 251 PDAIVTTNGESAVSEikkRSGWSGVKAVKNNEVYDVDPDLVTRPGPRLIKGVEELA 306
Cdd:PRK09534  250 PDVIVVATASALVAE---TEPYASTTAGETGNVVTVNVNHINQPAPRIVESMATMA 302
Peripla_BP_2 pfam01497
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ...
 62-289 1.57e-36

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: 130.95  E-value: 1.57e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201074194  62 VSLMPSNTEITYALGLGKKVVGVTDFDTYPKEVKNVEKI----GGMEFNTEKIISLNPDLVLAhaSSMQSAEEGLKQLKd 137
Cdd:pfam01497   1 AALSPAYTEILYALGATDSIVGVDAYTRDPLKADAVAAIvkvgAYGEINVERLAALKPDLVIL--STGYLTDEAEELLS- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201074194 138 AGITVVTVNDAASFEETYRSIEMIGKAAGAEDQAASLVKSMKSDLAGIKEKaaaISKADQKKVFV-EVSPAPDIYTTGKG 216
Cdd:pfam01497  78 LIIPTVIFESSSTGESLKEQIKQLGELLGLEDEAEELVAEIDSALAAAKKA---VPSLTRKPVLVfGGADGGGYVVAGSN 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1201074194 217 TFMNEMLEAIHAENAASA--QKGWAKITEEAIVKLNPDAIVTTNGESAVSE----IKKRSGWSGVKAVKNNEVYDVDPD 289
Cdd:pfam01497 155 TYIGDLLRILGIENIAAElsGSEYAPISFEAILSSNPDVIIVSGRDSFTKTgpefVAANPLWAGLPAVKNGRVYTLPSD 233
IsdE TIGR03659
heme ABC transporter, heme-binding protein isdE; This family of ABC substrate-binding proteins ...
 45-290 5.69e-20

heme ABC transporter, heme-binding protein isdE; This family of ABC substrate-binding proteins is observed primarily in close proximity with proteins localized to the cell wall and bearing the NEAT (NEAr Transporter, pfam05031) heme-binding domain. IsdE has been shown to bind heme and is involved in the process of scavenging heme for the purpose of obtaining iron.


Pssm-ID: 274706 [Multi-domain]  Cd Length: 289  Bit Score: 87.71  E-value: 5.69e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201074194  45 KDASGQEVKIEKEPKkIVSLMPSNTEITYALGLgkKVVGV-TDFDTYPKEVKNVEKIGG-MEFNTEKIISLNPDLVLaha 122
Cdd:TIGR03659  23 KEKSKVSNKKSKEER-IVATSVAVTEILDKLDL--DLVGVpTSQKTLPKRYKDVPEVGNpMSPDMEKIKSLKPTVVL--- 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201074194 123 sSMQSAEEGLK-QLKDAGITVVTVNdAASFEETYRSIEMIGKAAGAEDQAASLVKSMKSDLAGIKEKAAaiskaDQKKVF 201
Cdd:TIGR03659  97 -SVTTLEEDLGpKFKQLGVEATFLN-LTSVDGMKKSITELGEKYGREEQAEKLVKEINEKEAEVKKKVK-----GKKKPK 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201074194 202 VEV---SPAPDIYTTGKgTFMNEMLEAIHAENAASAQKG-WAKITEEAIVKLNPDAIV-TTNG--ESAV----SEIKKRS 270
Cdd:TIGR03659 170 VLIlmgVPGSYLVATEN-SYIGDLVKLAGGENVYKGNKQeYLSSNTEYLLKANPDIILrAAHGmpDEVKkmfdEEFKTND 248

                         250       260
                  ....*....|....*....|
gi 1201074194 271 GWSGVKAVKNNEVYDVDPDL 290
Cdd:TIGR03659 249 IWKHFEAVKNNRVYDLDEEL 268
TroA_like NF038402
helical backbone metal receptor;
60-169 2.05e-05

helical backbone metal receptor;


Pssm-ID: 439691  Cd Length: 219  Bit Score: 44.92  E-value: 2.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201074194  60 KIVSLMPSNTEiTYALGLGKKVVGVTDFDTYPKEVkNVEKIGGMEF-NTEKIISLNPDLVLAhassmqSAEEG----LKQ 134
Cdd:NF038402    1 RVVSLVPSLTE-AIAATAPELLVGATDWCTHPADL-DVARVRGTKNpDRAAIAALRPDLVVA------NQEENreldVDR 72

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1201074194 135 LKDAGITV-VTVNDaaSFEETYRSIE-MIGKAAGAED 169
Cdd:NF038402   73 LRAAGVPVwVTRIE--TVDEALASLRrLFTEALGVPV 107
 
Name Accession Description Interval E-value
YvrC cd01143
Periplasmic binding protein YvrC. These proteins are predicted to function as initial ...
 56-256 2.98e-77

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: 234.48  E-value: 2.98e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201074194  56 KEPKKIVSLMPSNTEITYALGLGKKVVGVTDFDTYPKEVKNVEKIGGM-EFNTEKIISLNPDLVLAHASSMQSAeegLKQ 134
Cdd:cd01143     1 KEPERIVSLSPSITEILFALGAGDKIVGVDTYSNYPKEVRKKPKVGSYsNPNVEKIVALKPDLVIVSSSSLAEL---LEK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201074194 135 LKDAGITVVTVNDAASFEETYRSIEMIGKAAGAEDQAASLVKSMKSDLAGIKEKAAAISKadqKKVFVEVSPaPDIYTTG 214
Cdd:cd01143    78 LKDAGIPVVVLPAASSLDEIYDQIELIGKITGAEEEAEKLVKEMKQKIDKVKDKGKTIKK---SKVYIEVSL-GGPYTAG 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1201074194 215 KGTFMNEMLEAIHAENAASAQKGWAKITEEAIVKLNPDAIVT 256
Cdd:cd01143   154 KNTFINELIRLAGAKNIAADSGGWPQVSPEEILKANPDVIIL 195
FepB COG0614
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ...
 60-315 2.73e-76

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


Pssm-ID: 440379 [Multi-domain]  Cd Length: 264  Bit Score: 234.51  E-value: 2.73e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201074194  60 KIVSLMPSNTEITYALGLGKKVVGVTD--FDTYPK-EVKNVEKIGGM-EFNTEKIISLNPDLVLAHASSMQsaEEGLKQL 135
Cdd:COG0614     2 RIVSLSPSATELLLALGAGDRLVGVSDwgYCDYPElELKDLPVVGGTgEPNLEAILALKPDLVLASSSGND--EEDYEQL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201074194 136 KDAGITVVTVnDAASFEETYRSIEMIGKAAGAEDQAASLVKSMKSDLAGIKEKAAAIskADQKKVFVEVSPAPDIYTTGK 215
Cdd:COG0614    80 EKIGIPVVVL-DPRSLEDLYESIRLLGELLGREERAEALIAEYEARLAAVRARLAGA--EERPTVLYEIWSGDPLYTAGG 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201074194 216 GTFMNEMLEAIHAENAAS-AQKGWAKITEEAIVKLNPDAIVTTNG-------ESAVSEIKKRSGWSGVKAVKNNEVYDVD 287
Cdd:COG0614   157 GSFIGELLELAGGRNVAAdLGGGYPEVSLEQVLALDPDVIILSGGgydaetaEEALEALLADPGWQSLPAVKNGRVYVVP 236

                         250       260
                  ....*....|....*....|....*...
gi 1201074194 288 PDLVTRPGPRLIKGVEELAEHIYPDVFK 315
Cdd:COG0614   237 GDLLSRPGPRLLLALEDLAKALHPELFA 264
ChuT COG4558
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism] ...
 58-312 1.62e-67

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


Pssm-ID: 443619 [Multi-domain]  Cd Length: 285  Bit Score: 212.74  E-value: 1.62e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201074194  58 PKKIVSLMPSNTEITYALGLGKKVVGVTDFDTYPKEVKNVEKIGGM-EFNTEKIISLNPDLVLAHASSMQSaeEGLKQLK 136
Cdd:COG4558    27 AERIVSLGGSVTEIVYALGAGDRLVGVDTTSTYPAAAKALPDVGYMrQLSAEGILSLKPTLVLASEGAGPP--EVLDQLR 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201074194 137 DAGITVVTVNDAASFEETYRSIEMIGKAAGAEDQAASLVKSMKSDLAGIKEKAAAISKAdqKKVFVEVSPAPDIYTT-GK 215
Cdd:COG4558   105 AAGVPVVVVPAAPSLEGVLAKIRAVAAALGVPEAGEALAARLEADLAALAARVAAIGKP--PRVLFLLSRGGGRPMVaGR 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201074194 216 GTFMNEMLEAIHAENAASAQKGWAKITEEAIVKLNPDAIVTTN--GESA--VSEIKKRSGWSGVKAVKNNEVYDVDPDLV 291
Cdd:COG4558   183 GTAADALIRLAGGVNAAAGFEGYKPLSAEALIAAAPDVILVMTrgLESLggVDGLLALPGLAQTPAGKNKRIVAMDDLLL 262

                         250       260
                  ....*....|....*....|.
gi 1201074194 292 TRPGPRLIKGVEELAEHIYPD 312
Cdd:COG4558   263 LGFGPRTPQAALALAQALYPA 283
BtuF cd01144
Cobalamin binding protein BtuF. These proteins have been shown to function as initial ...
 59-307 4.09e-57

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: 184.43  E-value: 4.09e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201074194  59 KKIVSLMPSNTEITYALGLGKKVVGVTDFDTYPKEVKNVEKIGGM-EFNTEKIISLNPDLVLAHASSmqSAEEGLKQLKD 137
Cdd:cd01144     1 MRIVSLAPSATELLYALGLGDQLVGVTDYCDYPPEAKKLPRVGGFyQLDLERVLALKPDLVIAWDDC--NVCAVVDQLRA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201074194 138 AGITVVtVNDAASFEETYRSIEMIGKAAGAEDQAASLVKSMKSDLAGIKEKAAAISkadQKKVFVEVSPAPdIYTTGKGT 217
Cdd:cd01144    79 AGIPVL-VSEPQTLDDILADIRRLGTLAGRPARAEELAEALRRRLAALRKQYASKP---PPRVFYQEWIDP-LMTAGGDW 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201074194 218 FmNEMLEAIHAENAASAQ-KGWAKITEEAIVKLNPDAIVTTNGESAVSE--IKKRSGWSGVKAVKNNEVYDVDPDLVTRP 294
Cdd:cd01144   154 V-PELIALAGGVNVFADAgERSPQVSWEDVLAANPDVIVLSPCGFGFTPaiLRKEPAWQALPAVRNGRVYAVDGNWYFRP 232

                         250
                  ....*....|...
gi 1201074194 295 GPRLIKGVEELAE 307
Cdd:cd01144   233 SPRLVDGLEQLAA 245
HutB cd01149
Hemin binding protein HutB. These proteins have been shown to function as initial receptors ...
 58-288 2.43e-42

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: 146.26  E-value: 2.43e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201074194  58 PKKIVSLMPSNTEITYALGLGKKVVGVTDFDTYPKEVKNVEKIGGM-EFNTEKIISLNPDLVLAHASSmqSAEEGLKQLK 136
Cdd:cd01149     1 PERIVSLGGSVTEIVYALGAGDRLVGVDSTSTYPEAAAKLPDVGYMrQLSAEGVLSLKPTLVIASDEA--GPPEALDQLR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201074194 137 DAGITVVTVNDAASFEETYRSIEMIGKAAGAEDQAASLVKSMKSDLAGIKEKAAAISKadQKKV-FVEVSPAPDIYTTGK 215
Cdd:cd01149    79 AAGVPVVTVPSTPTLDGLLTKIRQVAQALGVPEKGEALAQEVRQRLAALRKTVAAHKK--PPRVlFLLSHGGGAAMAAGR 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1201074194 216 GTFMNEMLEAIHAENAASAQKGWAKITEEAIVKLNPDAIVTTN----GESAVSEIKKRSGWSGVKAVKNNEVYDVDP 288
Cdd:cd01149   157 NTAADAIIALAGAVNAAAGFRGYKPLSAEALIAAQPDVILVMSrgldAVGGVDGLLKLPGLAQTPAGRNKRILAMDD 233
TroA_e cd01142
Periplasmic binding protein TroA_e. These proteins are predicted to function as initial ...
 36-315 1.11e-41

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: 145.96  E-value: 1.11e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201074194  36 AAEAFPVTIKDASGQEVKIEKEPKKIVSLMPSNTEITYALGLGKKVVGVTD---FDTYPKEV----KNVEKIG-GMEFNT 107
Cdd:cd01142     2 AATAATRTITDMAGRKVTIPDEVKRIAALWGAGNAVVAALGGGKLIVATTStvqQEPWLYRLapslENVATGGtGNDVNI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201074194 108 EKIISLNPDLVLAHASsmqSAEEGLKQlKDAGITVVTVnDAASFEETYRSIEMIGKAAGAEDQAASLVKSMKSDLAGIKE 187
Cdd:cd01142    82 EELLALKPDVVIVWST---DGKEAGKA-VLRLLNALSL-RDAELEEVKLTIALLGELLGRQEKAEALVAYFDDNLAYVAA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201074194 188 KAAAISKADQKKVFVEvspAPDIYTT-GKGTFMNEMLEAIHAENAASA--QKGWAKITEEAIVKLNPDAIVTTNGESAVs 264
Cdd:cd01142   157 RTKKLPDSERPRVYYA---GPDPLTTdGTGSITNSWIDLAGGINVASEatKKGSGEVSLEQLLKWNPDVIIVGNADTKA- 232

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1201074194 265 EIKKRSGWSGVKAVKNNEVYdVDPDLV---TRPGPRLIKGVEELAEHIYPDVFK 315
Cdd:cd01142   233 AILADPRWQNLRAVKNGRVY-VNPEGAfwwDRPSAEEALLGLWLAKTLYPERFT 285
btuF PRK09534
corrinoid ABC transporter substrate-binding protein; Reviewed
 16-306 1.14e-40

corrinoid ABC transporter substrate-binding protein; Reviewed


Pssm-ID: 236552 [Multi-domain]  Cd Length: 359  Bit Score: 145.05  E-value: 1.14e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201074194  16 GVLSGCGQAQKPADEQKQEKAAEAFPVTIKDASGQEVKIEKEPKKIVSLMPSNTEITYALGLGKKVVGVTDFDTY---PK 92
Cdd:PRK09534   18 MTAAGGALAPAPAAQHADADRACSFPVTETDATGTEITLDERPERVVTLNPSAAQTMWELGARDRVVGVTQYASYldgAE 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201074194  93 EVKNVEKIGGMEFNTEKIISLNPDLVLAHASsmqSAEEGLKQLKDAGITVVTVNDAASFEETYRSIEMIGKAAGAEDQAA 172
Cdd:PRK09534   98 ERTNVSGGQPFGVNVEAVVGLDPDLVLAPNA---VAGDTVTRLREAGITVFHFPAATSIEDVAEKTATIGRLTGNCEAAA 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201074194 173 SLVKSMKSDLAGIKEKAAAISkaDQKKVFVevsPAPDIYTTGKGTFMNEMLEAIHAENAASAQK--GWAKITEEAIVKLN 250
Cdd:PRK09534  175 ETNAEMRDRVDAVEDRTADVD--DRPRVLY---PLGDGYTAGGNTFIGALIEAAGGHNVAADATtdGYPQLSEEVIVQQD 249

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1201074194 251 PDAIVTTNGESAVSEikkRSGWSGVKAVKNNEVYDVDPDLVTRPGPRLIKGVEELA 306
Cdd:PRK09534  250 PDVIVVATASALVAE---TEPYASTTAGETGNVVTVNVNHINQPAPRIVESMATMA 302
TroA_a cd01148
Metal binding protein TroA_a. These proteins are predicted to function as initial receptors ...
 40-306 1.28e-37

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: 135.16  E-value: 1.28e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201074194  40 FPVTIkDASGQEVKIEKEPKKIVSLMPSNTEITYALGLGKKVVGVT-----DFDTYPKEVKNVEKIGGMEFNTEKIISLN 114
Cdd:cd01148     1 YPLTV-ENCGRSVTFDKAPQRVVSNDQNTTEMMLALGLQDRMVGTAgidnkDLPELKAKYDKVPELAKKYPSKETVLAAR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201074194 115 PDLVLAHASSMQSAEEGL--KQLKDAGI-------TVVTVNDAASFEETYRSIEMIGKAAGAEDQAASLVKSMKSDLAGI 185
Cdd:cd01148    80 PDLVFGGWSYGFDKGGLGtpDSLAELGIktyilpeSCGQRRGEATLDDVYNDIRNLGKIFDVEDRADKLVADLKARLAEI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201074194 186 KEKAAAISKAdqKKVFVEVSPAPDIYTTGKGTFMNEMLEAIHAENA-ASAQKGWAKITEEAIVKLNPDAIV------TTN 258
Cdd:cd01148   160 SAKVKGDGKK--VAVFVYDSGEDKPFTSGRGGIPNAIITAAGGRNVfADVDESWTTVSWETVIARNPDVIViidygdQNA 237

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1201074194 259 GESAVSEIKKRSGWSGVKAVKNNEVYDVDPDLVTrPGPRLIKGVEELA 306
Cdd:cd01148   238 AEQKIKFLKENPALKNVPAVKNNRFIVLPLAEAT-PGIRNVDAIEKLA 284
HemV-2 cd01147
Metal binding protein HemV-2. These proteins are predicted to function as initial receptors ...
 54-286 7.02e-37

Metal binding protein HemV-2. These proteins are predicted to function as initial receptors in ABC transport of metal ions. They belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind the metal ion in the cleft between these domains. In addition, these proteins sometimes have a low complexity region containing a metal-binding histidine-rich motif (repetitive HDH sequence).


Pssm-ID: 238567 [Multi-domain]  Cd Length: 262  Bit Score: 132.84  E-value: 7.02e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201074194  54 IEKEPKKIVSLMPSNTEITYALGLGKKVVGVTDFDT---------YPKEVKNVEKIGGMEF----NTEKIISLNPDLVLA 120
Cdd:cd01147     1 VPKPVERVVAAGPGALRLLYALAAPDKIVGVDDAEKsdegrpyflASPELKDLPVIGRGGRgntpNYEKIAALKPDVVID 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201074194 121 haSSMQSAEEGLKQL-KDAGITVVTVNDAASFEETYRSIEMIGKAAGAEDQAASLVKSMKSDLAGIKEKAAAISKADQKK 199
Cdd:cd01147    81 --VGSDDPTSIADDLqKKTGIPVVVLDGGDSLEDTPEQIRLLGKVLGKEERAEELISFIESILADVEERTKDIPDEEKPT 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201074194 200 VFVEVSP---APDIYTTGKGTfmNEMLEAIHAENAASAQ--KGWAKITEEAIVKLNPDAIVTTNG---ESAVSEIKKRSG 271
Cdd:cd01147   159 VYFGRIGtkgAAGLESGLAGS--IEVFELAGGINVADGLggGGLKEVSPEQILLWNPDVIFLDTGsfyLSLEGYAKNRPF 236

                         250
                  ....*....|....*
gi 1201074194 272 WSGVKAVKNNEVYDV 286
Cdd:cd01147   237 WQSLKAVKNGRVYLL 251
Peripla_BP_2 pfam01497
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ...
 62-289 1.57e-36

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: 130.95  E-value: 1.57e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201074194  62 VSLMPSNTEITYALGLGKKVVGVTDFDTYPKEVKNVEKI----GGMEFNTEKIISLNPDLVLAhaSSMQSAEEGLKQLKd 137
Cdd:pfam01497   1 AALSPAYTEILYALGATDSIVGVDAYTRDPLKADAVAAIvkvgAYGEINVERLAALKPDLVIL--STGYLTDEAEELLS- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201074194 138 AGITVVTVNDAASFEETYRSIEMIGKAAGAEDQAASLVKSMKSDLAGIKEKaaaISKADQKKVFV-EVSPAPDIYTTGKG 216
Cdd:pfam01497  78 LIIPTVIFESSSTGESLKEQIKQLGELLGLEDEAEELVAEIDSALAAAKKA---VPSLTRKPVLVfGGADGGGYVVAGSN 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1201074194 217 TFMNEMLEAIHAENAASA--QKGWAKITEEAIVKLNPDAIVTTNGESAVSE----IKKRSGWSGVKAVKNNEVYDVDPD 289
Cdd:pfam01497 155 TYIGDLLRILGIENIAAElsGSEYAPISFEAILSSNPDVIIVSGRDSFTKTgpefVAANPLWAGLPAVKNGRVYTLPSD 233
FecB COG4594
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and ...
 14-293 1.45e-35

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


Pssm-ID: 443650 [Multi-domain]  Cd Length: 316  Bit Score: 130.43  E-value: 1.45e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201074194  14 AAGVLSGCGQAqkpaDEQKQEKAAEAFPVTIKDASGqEVKIEKEPKKIVSLMPSNTEitYALGLGKKVVGVTDFDTYP-- 91
Cdd:COG4594    13 ALLLLAACGSS----SSDSSSSEAAAGARTVKHAMG-ETTIPGTPKRVVVLEWSFAD--ALLALGVTPVGIADDNDYDrw 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201074194  92 -----KEVKNVEKIG-GMEFNTEKIISLNPDLVLAhassMQSAEEGL-KQLKDAGITVVTVNDAASFEETYRSIEMIGKA 164
Cdd:COG4594    86 vpylrDLIKGVTSVGtRSQPNLEAIAALKPDLIIA----DKSRHEAIyDQLSKIAPTVLFKSRNGDYQENLESFKTIAKA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201074194 165 AGAEDQAASLVKSMKSDLAGIKEKAAAisKADQKKVFVEVSPAPDIYTTGKGTFMNEMLEAIHAENAASAQK----GWAK 240
Cdd:COG4594   162 LGKEEEAEAVLADHDQRIAEAKAKLAA--ADKGKKVAVGQFRADGLRLYTPNSFAGSVLAALGFENPPKQSKdngyGYSE 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1201074194 241 ITEEAIVKLNPD-AIVTTNG-ESAVSEIKKRSGWSGVKAVKNNEVYDVDPDLVTR 293
Cdd:COG4594   240 VSLEQLPALDPDvLFIATYDdPSILKEWKNNPLWKNLKAVKNGRVYEVDGDLWTR 294
FhuD cd01146
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ...
 56-296 3.81e-30

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: 114.69  E-value: 3.81e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201074194  56 KEPKKIVSLMPSNTEItyALGLGKKVVGVTDFDTYPK-------EVKNVEKIGG-MEFNTEKIISLNPDLVLAHASSMQS 127
Cdd:cd01146     1 AKPQRIVALDWGALET--LLALGVKPVGVADTAGYKPwipepalPLEGVVDVGTrGQPNLEAIAALKPDLILGSASRHDE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201074194 128 AEEGLKQLkdAgiTVVTVNDAASFEETYRSIEMIGKAAGAEDQAASLVKSMKSDLAGIKEKaaaISKADQKKV-FVEVSP 206
Cdd:cd01146    79 IYDQLSQI--A--PTVLLDSSPWLAEWKENLRLIAKALGKEEEAEKLLAEYDQRLAELRQK---LPDKGPKPVsVVRFSD 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201074194 207 APDIYTTGKGTFMNEMLEAIHAENAASAQK----GWAKITEEAIVKLNPDAIV--TTNGESAVSEIKKRSGWSGVKAVKN 280
Cdd:cd01146   152 AGSIRLYGPNSFAGSVLEDLGLQNPWAQETtndsGFATISLERLAKADADVLFvfTYEDEELAQALQANPLWQNLPAVKN 231

                         250
                  ....*....|....*.
gi 1201074194 281 NEVYDVDPDLVTRPGP 296
Cdd:cd01146   232 GRVYVVDDVWWFFGGG 247
PRK03379 PRK03379
vitamin B12-transporter protein BtuF; Provisional
 60-305 6.59e-30

vitamin B12-transporter protein BtuF; Provisional


Pssm-ID: 179575 [Multi-domain]  Cd Length: 260  Bit Score: 114.01  E-value: 6.59e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201074194  60 KIVSLMPSNTEITYALGLGKkvVGVTDFDTYPKEVKNVEKIG---GMefNTEKIISLNPDLVLAHASSmqSAEEGLKQLK 136
Cdd:PRK03379   19 RVITLSPANTELAFAAGITP--VGVSSYSDYPPQAKKIEQVAtwqGM--NLERIVALKPDLVLAWRGG--NAERQVDQLA 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201074194 137 DAGITVVTVnDAASFEETYRSIEMIGKAAGAEDQAASLVKSMKSDLAGIKEKAAAISKadqKKVFVEVSPAPdIYTTGKG 216
Cdd:PRK03379   93 SLGIKVMWV-DATSIEQIANALRQLAPWSPQPEKAEQAAQSLLQQYAALKAQYADKPK---KRVFLQFGTNP-LFTSGKH 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201074194 217 TFMNEMLEAIHAENA-ASAQKGWAKITEEAIVKLNPDAIVTTNGESAVSEIKKRsgWSGVKAVKnneVYDVDPDLVTRPG 295
Cdd:PRK03379  168 SIQSQVLSLCGGENIfADSRVPWPQVSREQVLARKPQAIVITGGPDQIPKIKQF--WGPQLKIP---VIPLNSDWFERAS 242

                         250
                  ....*....|
gi 1201074194 296 PRLIKGVEEL 305
Cdd:PRK03379  243 PRIILAAQQL 252
TroA-like cd00636
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function ...
 59-205 3.53e-26

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: 101.10  E-value: 3.53e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201074194  59 KKIVSLMPSNTEITYALGLGKKVVGVTDFDTYPKEVKNVEK-----IGGMEFNTEKIISLNPDLVLAHASSMQSAEEGLK 133
Cdd:cd00636     1 KRVVALDPGATELLLALGGDDKPVGVADPSGYPPEAKALLEkvpdvGHGYEPNLEKIAALKPDLIIANGSGLEAWLDKLS 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1201074194 134 QLkDAGITVVTVNDAASFEETYRSIEMIGKAAGAEDQAASLVKSMKSDLAGIKEKAAAISKadqKKVFVEVS 205
Cdd:cd00636    81 KI-AIPVVVVDEASELSLENIKESIRLIGKALGKEENAEELIAELDARLAELRAKLAKIPK---KKVSLVVG 148
TroA_f cd01139
Periplasmic binding protein TroA_f. These proteins are predicted to function as initial ...
 42-316 1.50e-25

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: 104.31  E-value: 1.50e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201074194  42 VTIKDASGQEVKIEKEPKKIVsLMPSntEITYALGLGK------KVVG------VTDFDTYPK------EVKNVEKIGGM 103
Cdd:cd01139     1 ITVTDVAGRKVTLDAPVERVL-LGEG--RQLYALALLEgenpfaRIVGwggdlkKGDPDTYAKykekfpEIADIPLIGST 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201074194 104 ---EFNTEKIISLNPDLVLAHaSSMQSAEEG---LKQLKDAGITVVTVN-DAASFEETYRSIEMIGKAAGAEDQAASLVK 176
Cdd:cd01139    78 yngDFSVEKVLTLKPDLVILN-IWAKTTAEEsgiLEKLEQAGIPVVFVDfRQKPLKNTTPSMRLLGKALGREERAEEFIE 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201074194 177 SMKSDLAGIKEKAAAISKadQK-KVFVEVSP-APDIY--TTGKGTFmNEMLEAIHAENAASAQKG--WAKITEEAIVKLN 250
Cdd:cd01139   157 FYQERIDRIRDRLAKINE--PKpKVFIELGAgGPEECcsTYGNGNW-GELVDAAGGDNIADGLIPgtSGELNAEYVIAAN 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201074194 251 PDAIVTTNG---------------------ESAVSEIKKRSGWSGVKAVKNNEVYDVDPDLVTRpgPRLIKGVEELAEHI 309
Cdd:cd01139   234 PEIIIATGGnwakdpsgvslgpdgttadakESLLRALLKRPGWSSLQAVKNGRVYALWHQFYRS--PYNFVALEAFAKWL 311


                  ....*..
gi 1201074194 310 YPDVFKK 316
Cdd:cd01139   312 YPELFKD 318
FatB cd01140
Siderophore binding protein FatB. These proteins have been shown to function as ABC-type ...
 51-290 6.41e-24

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: 98.48  E-value: 6.41e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201074194  51 EVKIEKEPKKIVSLMPSNTEITYALGLgkKVVGVTDFDTYPKEVKNV-----EKIGG-MEFNTEKIISLNPDLVLAHASS 124
Cdd:cd01140     5 ETKVPKNPEKVVVFDVGALDTLDALGV--KVVGVPKSSTLPEYLKKYkddkyANVGTlFEPDLEAIAALKPDLIIIGGRL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201074194 125 MQSAEEGLKqlkDAGITVVTVNDAASFEETYRSIEMIGKAAGAEDQAASLVKSMKSDLAGIKEKAAAiskadQKKVFVEV 204
Cdd:cd01140    83 AEKYDELKK---IAPTIDLGADLKNYLESVKQNIETLGKIFGKEEEAKELVAEIDASIAEAKSAAKG-----KKKALVVL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201074194 205 SPAPDIYTTGKGTFMNEMLEAIHAENAASAQKGWAK---ITEEAIVKLNPD--------AIVTTNGESAVsEIKKRSGWS 273
Cdd:cd01140   155 VNGGKLSAFGPGSRFGWLHDLLGFEPADENIKASSHgqpVSFEYILEANPDwlfvidrgAAIGAEGSSAK-EVLDNDLVK 233

                         250
                  ....*....|....*..
gi 1201074194 274 GVKAVKNNEVYDVDPDL 290
Cdd:cd01140   234 NTTAWKNGKVIYLDPDL 250
CeuA COG4607
ABC-type enterochelin transport system, periplasmic component [Inorganic ion transport and ...
 1-289 2.09e-23

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


Pssm-ID: 443657 [Multi-domain]  Cd Length: 310  Bit Score: 97.56  E-value: 2.09e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201074194   1 MKKFgLLLLSLLLAAGVLSGCGQaqkpaDEQKQEKAAEAFPVTIKDASGqEVKIEKEPKKIVSLMPSNTEITYALGLgkK 80
Cdd:COG4607     1 MKKT-LLAALALAAALALAACGS-----SSAAAASAAAAETVTVEHALG-TVEVPKNPKRVVVFDNGALDTLDALGV--E 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201074194  81 VVGVTDfDTYPKEVK-----NVEKIGGM-EFNTEKIISLNPDLVLAHASSMQSAEEgLKQLkdAGITVVTVNDAASFEET 154
Cdd:COG4607    72 VAGVPK-GLLPDYLSkyaddKYANVGTLfEPDLEAIAALKPDLIIIGGRSAKKYDE-LSKI--APTIDLTVDGEDYLESL 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201074194 155 YRSIEMIGKAAGAEDQAASLVKSMKSDLAGIKEKAAAiskaDQKKVFVEVSpAPDIYTTGKGT---FMNEML---EAihA 228
Cdd:COG4607   148 KRNTETLGEIFGKEDEAEELVADLDAKIAALKAAAAG----KGTALIVLTN-GGKISAYGPGSrfgPIHDVLgfkPA--D 220

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1201074194 229 ENAASAQKGWAkITEEAIVKLNPD--------AIVTTNGESAV----SEIKKrsgwsGVKAVKNNEVYDVDPD 289
Cdd:COG4607   221 EDIEASTHGQA-ISFEFIAEANPDwlfvidrdAAIGGEGPAAKqvldNELVK-----QTTAWKNGQIVYLDPD 287
FeuA cd01138
Periplasmic binding protein FeuA. These proteins have predicted to function as initial ...
 51-289 2.22e-22

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: 93.55  E-value: 2.22e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201074194  51 EVKIEKEPKKIVSLMPSNTEityALGLGKKVVGVTDFDT----YPKEVKNVEKIGGMEFNTEKIISLNPDLVLAhassMQ 126
Cdd:cd01138     2 EVEIPAKPKRIVALSGETEG---LALLGIKPVGAASIGGknpyYKKKTLAKVVGIVDEPNLEKVLELKPDLIIV----SS 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201074194 127 SAEEGLKQLKDAGITVVTVNDAASFEETyrsIEMIGKAAGAEDQAASLVKSMKSDLAGIKEKaaaISKADQKKVFVEVSP 206
Cdd:cd01138    75 KQEENYEKLSKIAPTVPVSYNSSDWEEQ---LKEIGKLLNKEDEAEKWLADYKQKAKEAKEK---IKKKLGNDKSVAVLR 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201074194 207 APD--------------IYTTGKGTFMNEMLEAIhaenaaSAQKGWAKITEEAIVKLNPDAIVTTN--GESAVSEIKKRS 270
Cdd:cd01138   149 GRKqiyvfgedgrgggpILYADLGLKAPEKVKEI------EDKPGYAAISLEVLPEFDADYIFLLFftGPEAKADFESLP 222

                         250
                  ....*....|....*....
gi 1201074194 271 GWSGVKAVKNNEVYDVDPD 289
Cdd:cd01138   223 IWKNLPAVKNNHVYIVDAW 241
IsdE TIGR03659
heme ABC transporter, heme-binding protein isdE; This family of ABC substrate-binding proteins ...
 45-290 5.69e-20

heme ABC transporter, heme-binding protein isdE; This family of ABC substrate-binding proteins is observed primarily in close proximity with proteins localized to the cell wall and bearing the NEAT (NEAr Transporter, pfam05031) heme-binding domain. IsdE has been shown to bind heme and is involved in the process of scavenging heme for the purpose of obtaining iron.


Pssm-ID: 274706 [Multi-domain]  Cd Length: 289  Bit Score: 87.71  E-value: 5.69e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201074194  45 KDASGQEVKIEKEPKkIVSLMPSNTEITYALGLgkKVVGV-TDFDTYPKEVKNVEKIGG-MEFNTEKIISLNPDLVLaha 122
Cdd:TIGR03659  23 KEKSKVSNKKSKEER-IVATSVAVTEILDKLDL--DLVGVpTSQKTLPKRYKDVPEVGNpMSPDMEKIKSLKPTVVL--- 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201074194 123 sSMQSAEEGLK-QLKDAGITVVTVNdAASFEETYRSIEMIGKAAGAEDQAASLVKSMKSDLAGIKEKAAaiskaDQKKVF 201
Cdd:TIGR03659  97 -SVTTLEEDLGpKFKQLGVEATFLN-LTSVDGMKKSITELGEKYGREEQAEKLVKEINEKEAEVKKKVK-----GKKKPK 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201074194 202 VEV---SPAPDIYTTGKgTFMNEMLEAIHAENAASAQKG-WAKITEEAIVKLNPDAIV-TTNG--ESAV----SEIKKRS 270
Cdd:TIGR03659 170 VLIlmgVPGSYLVATEN-SYIGDLVKLAGGENVYKGNKQeYLSSNTEYLLKANPDIILrAAHGmpDEVKkmfdEEFKTND 248

                         250       260
                  ....*....|....*....|
gi 1201074194 271 GWSGVKAVKNNEVYDVDPDL 290
Cdd:TIGR03659 249 IWKHFEAVKNNRVYDLDEEL 268
fecB PRK11411
iron-dicitrate transporter substrate-binding subunit; Provisional
 36-307 1.19e-13

iron-dicitrate transporter substrate-binding subunit; Provisional


Pssm-ID: 183123 [Multi-domain]  Cd Length: 303  Bit Score: 70.09  E-value: 1.19e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201074194  36 AAEAFPVTIKDASGqEVKIEKEPKKIVSLmpsntEITYALGL---GKKVVGVTDfDTYPKEV-KNV-EKIG-----GM-- 103
Cdd:PRK11411   18 SSHAFAVTVQDEQG-TFTLEKTPQRIVVL-----ELSFVDALaavGVSPVGVAD-DNDAKRIlPEVrAHLKpwqsvGTrs 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201074194 104 EFNTEKIISLNPDLVLAHASSMQSAEEGLKQLKDagiTVVTVNDAASFEETYRSIEMIGKAAGAEDQaaslvksMKSDLA 183
Cdd:PRK11411   91 QPSLEAIAALKPDLIIADSSRHAGVYIALQKIAP---TLLLKSRNETYQENLQSAAIIGEVLGKKRE-------MQARIE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201074194 184 GIKEKAAAISK--ADQKKVFVEVSPAPDIYTTGKGTFMNEMLEA--IHAENAASAQKGWAKITEEAIVKLNPDAIVTTN- 258
Cdd:PRK11411  161 QHKERMAQFASqlPKGTRVAFGTSREQQFNLHSPESYTGSVLAAlgLNVPKAPMNGAAMPSISLEQLLALNPDWLLVAHy 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1201074194 259 -GESAVSEIKKRSGWSGVKAVKNNEVYDVDPDLVTRpgPRLIKGVEELAE 307
Cdd:PRK11411  241 rQESIVKRWQQDPLWQMLTAAKKQQVASVDSNTWAR--MRGIFAAERIAK 288
PRK10957 PRK10957
iron-enterobactin transporter periplasmic binding protein; Provisional
 14-188 4.58e-12

iron-enterobactin transporter periplasmic binding protein; Provisional


Pssm-ID: 236806 [Multi-domain]  Cd Length: 317  Bit Score: 65.76  E-value: 4.58e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201074194  14 AAGVLSGCGQAqkpadeqkqEKAAEAFPVTIKDASGqEVKIEKEPKKIVSLMPSNTEITyaLGLGKKVVG---------V 84
Cdd:PRK10957   10 LGLLLSGIAAA---------QASAAGWPRTVTDSRG-SVTLESKPQRIVSTSVTLTGTL--LAIDAPVIAsgattpntrV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201074194  85 TD---FDTYPKEV---KNVEKIGGMEFNTEKIISLNPDLVLAHASSMQSAEEGLKQLKDAGITVVTVNDAASFEETYRsi 158
Cdd:PRK10957   78 ADdqgFFRQWSDVakeRGVEVLYIGEPDAEAVAAQMPDLIVISATGGDSALALYDQLSAIAPTLVIDYDDKSWQELAT-- 155

                         170       180       190
                  ....*....|....*....|....*....|
gi 1201074194 159 eMIGKAAGAEDQAASLVKSMKSDLAGIKEK 188
Cdd:PRK10957  156 -QLGEATGLEKQAAAVIAQFDAQLAEVKAK 184
TroA_d cd01141
Periplasmic binding protein TroA_d. These proteins are predicted to function as initial ...
 54-195 1.17e-11

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


Pssm-ID: 238561 [Multi-domain]  Cd Length: 186  Bit Score: 62.44  E-value: 1.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201074194  54 IEKEPKKIVSLMPSNTEITYALGLGKKVVGVTDFDTY---PKEVKNVEKIGGMEF--NTEKIISLNPDLVLahASSMQSA 128
Cdd:cd01141     4 IKVPPKRIVVLSPTHVDLLLALDKADKIVGVSASAYDlntPAVKERIDIQVGPTGslNVELIVALKPDLVI--LYGGFQA 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1201074194 129 EEGLKQLKDAGITVVTVNDaasFEETYRSIEMIGKAA-----GAEDQAASLVKSMKSDLAGIKEKAAAISKA 195
Cdd:cd01141    82 QTILDKLEQLGIPVLYVNE---YPSPLGRAEWIKFAAafygvGKEDKADEAFAQIAGRYRDLAKKVSNLNKP 150
PRK14048 PRK14048
ferrichrome/ferrioxamine B periplasmic transporter; Provisional
 36-308 2.11e-09

ferrichrome/ferrioxamine B periplasmic transporter; Provisional


Pssm-ID: 172540 [Multi-domain]  Cd Length: 374  Bit Score: 57.99  E-value: 2.11e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201074194  36 AAEAFPVTIKDASGQEVKIEKEPKKI------------------VSLMP--------SNTEItYALGLGKkvvgvtdfdt 89
Cdd:PRK14048   26 AEVQWPMTVTDAVGREVTIPAPPKAVllgsgfnlialslihpdpVSLLAgwsgdmkgDNPEI-YESFLRK---------- 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201074194  90 YPK--EVKNVEKIGGMEFNTEKIISLNPDLVLAHASSMQSAE--EGLKQLKDAGITVVTV--NDAAsFEETYRSIEMIGK 163
Cdd:PRK14048   95 FPElaDVPLIDDGSGPGLSFETILTLKADLAILANWQADTEAgqRAIEYLESIGVPVIVVdfNNEA-LKNTPDNMRLLGK 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201074194 164 AAGAEDQAASLVKSMKSDLAGIKEKAAAISKADqKKVFVEVSPAPD----IY-TTGKGTFMNEMLEAIHAENAASAQKGw 238
Cdd:PRK14048  174 VFEREEQAEDFARFYEERLARIRDRVAKHSEPG-PTVLMEAFPAADrccwAYgRGGLGEFIALTGSRNIAEGALPRPGG- 251

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201074194 239 aKITEEAIVKLNPDAIVTTNgesavSEIKKRSGWSGVKAVKNNEVYDVDPDLVTRPGPRLIKGVEELAEH 308
Cdd:PRK14048  252 -MMNAEAIMAENPDVYIATS-----SPGGKYSGFSIGPGVSAEEAETTLANVVDKPVMASIAAVRDGRVH 315
TroA_like NF038402
helical backbone metal receptor;
60-169 2.05e-05

helical backbone metal receptor;


Pssm-ID: 439691  Cd Length: 219  Bit Score: 44.92  E-value: 2.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201074194  60 KIVSLMPSNTEiTYALGLGKKVVGVTDFDTYPKEVkNVEKIGGMEF-NTEKIISLNPDLVLAhassmqSAEEG----LKQ 134
Cdd:NF038402    1 RVVSLVPSLTE-AIAATAPELLVGATDWCTHPADL-DVARVRGTKNpDRAAIAALRPDLVVA------NQEENreldVDR 72

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1201074194 135 LKDAGITV-VTVNDaaSFEETYRSIE-MIGKAAGAED 169
Cdd:NF038402   73 LRAAGVPVwVTRIE--TVDEALASLRrLFTEALGVPV 107
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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