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Conserved domains on  [gi|446671700|ref|WP_000749046|]
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ABC transporter substrate-binding protein [Staphylococcus aureus]

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 ...
 37-236 2.00e-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: 234.09  E-value: 2.00e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671700  37 SPYHRIVSLMPSNTEILYELGLGKYIVGVSTVDDYPKDVKEGKKQFDALNLNKEELLKAKPDLILAHESQKATankVLSS 116
Cdd:cd01143    1 KEPERIVSLSPSITEILFALGAGDKIVGVDTYSNYPKEVRKKPKVGSYSNPNVEKIVALKPDLVIVSSSSLAE---LLEK 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671700 117 LEKQGIKVVYVKDAQSIDETYNTFKQIGKLTHHDKQAEQLVEETKDNIDKVIDSIPAyHKKSKVFIEVSSkPEIYTAGKH 196
Cdd:cd01143   78 LKDAGIPVVVLPAASSLDEIYDQIELIGKITGAEEEAEKLVKEMKQKIDKVKDKGKT-IKKSKVYIEVSL-GGPYTAGKN 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 446671700 197 TFFNDMLEKLEAQNVYSDINGWNPVTKESIIKKNPDILIS 236
Cdd:cd01143  156 TFINELIRLAGAKNIAADSGGWPQVSPEEILKANPDVIIL 195
 
Name Accession Description Interval E-value
YvrC cd01143
Periplasmic binding protein YvrC. These proteins are predicted to function as initial ...
 37-236 2.00e-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: 234.09  E-value: 2.00e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671700  37 SPYHRIVSLMPSNTEILYELGLGKYIVGVSTVDDYPKDVKEGKKQFDALNLNKEELLKAKPDLILAHESQKATankVLSS 116
Cdd:cd01143    1 KEPERIVSLSPSITEILFALGAGDKIVGVDTYSNYPKEVRKKPKVGSYSNPNVEKIVALKPDLVIVSSSSLAE---LLEK 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671700 117 LEKQGIKVVYVKDAQSIDETYNTFKQIGKLTHHDKQAEQLVEETKDNIDKVIDSIPAyHKKSKVFIEVSSkPEIYTAGKH 196
Cdd:cd01143   78 LKDAGIPVVVLPAASSLDEIYDQIELIGKITGAEEEAEKLVKEMKQKIDKVKDKGKT-IKKSKVYIEVSL-GGPYTAGKN 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 446671700 197 TFFNDMLEKLEAQNVYSDINGWNPVTKESIIKKNPDILIS 236
Cdd:cd01143  156 TFINELIRLAGAKNIAADSGGWPQVSPEEILKANPDVIIL 195
FepB COG0614
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ...
 41-293 6.02e-67

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


Pssm-ID: 440379 [Multi-domain]  Cd Length: 264  Bit Score: 209.85  E-value: 6.02e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671700  41 RIVSLMPSNTEILYELGLGKYIVGVS--TVDDYPKDVKEGKKQF-DALNLNKEELLKAKPDLILAHESQkaTANKVLSSL 117
Cdd:COG0614    2 RIVSLSPSATELLLALGAGDRLVGVSdwGYCDYPELELKDLPVVgGTGEPNLEAILALKPDLVLASSSG--NDEEDYEQL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671700 118 EKQGIKVVYVkDAQSIDETYNTFKQIGKLTHHDKQAEQLVEETKDNIDKVIDSIPAYHKKSKVFIEVSSKPEIYTAGKHT 197
Cdd:COG0614   80 EKIGIPVVVL-DPRSLEDLYESIRLLGELLGREERAEALIAEYEARLAAVRARLAGAEERPTVLYEIWSGDPLYTAGGGS 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671700 198 FFNDMLEKLEAQNVYSDIN-GWNPVTKESIIKKNPDILI----STEAKTRSDYMDIIKKRGGFNKINAVKNTRIEVVNGD 272
Cdd:COG0614  159 FIGELLELAGGRNVAADLGgGYPEVSLEQVLALDPDVIIlsggGYDAETAEEALEALLADPGWQSLPAVKNGRVYVVPGD 238

                        250       260
                 ....*....|....*....|.
gi 446671700 273 EVSRPGPRIDEGLKELRDAIY 293
Cdd:COG0614  239 LLSRPGPRLLLALEDLAKALH 259
Peripla_BP_2 pfam01497
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ...
 43-266 1.56e-28

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: 109.38  E-value: 1.56e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671700   43 VSLMPSNTEILYELGLGKYIVGVS--TVDDYPKDVKEGKKQFDA-LNLNKEELLKAKPDLILAHESQKATANkvlSSLEK 119
Cdd:pfam01497   1 AALSPAYTEILYALGATDSIVGVDayTRDPLKADAVAAIVKVGAyGEINVERLAALKPDLVILSTGYLTDEA---EELLS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671700  120 QGIKVVYVKDAQSIDETYNTFKQIGKLTHHDKQAEQLVEETKDNIDKVIDSIPAYHKKSKVFIEVSSKPEIYTAGKHTFF 199
Cdd:pfam01497  78 LIIPTVIFESSSTGESLKEQIKQLGELLGLEDEAEELVAEIDSALAAAKKAVPSLTRKPVLVFGGADGGGYVVAGSNTYI 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671700  200 NDMLEKLEAQNVYSDIN--GWNPVTKESIIKKNPDILI-STEAKTRSDYMDIIKKRGGFNKINAVKNTRI 266
Cdd:pfam01497 158 GDLLRILGIENIAAELSgsEYAPISFEAILSSNPDVIIvSGRDSFTKTGPEFVAANPLWAGLPAVKNGRV 227
PRK03379 PRK03379
vitamin B12-transporter protein BtuF; Provisional
 41-281 1.43e-26

vitamin B12-transporter protein BtuF; Provisional


Pssm-ID: 179575 [Multi-domain]  Cd Length: 260  Bit Score: 104.77  E-value: 1.43e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671700  41 RIVSLMPSNTEILYELGLGKyiVGVSTVDDYPKDVKEGKKQFDALNLNKEELLKAKPDLILAHesQKATANKVLSSLEKQ 120
Cdd:PRK03379  19 RVITLSPANTELAFAAGITP--VGVSSYSDYPPQAKKIEQVATWQGMNLERIVALKPDLVLAW--RGGNAERQVDQLASL 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671700 121 GIKVVYVkDAQSIDETYNTFKQIGKLTHHDKQAEQLVEETKDNIDKVIDSIPAYHKKsKVFIEVSSKPeIYTAGKHTFFN 200
Cdd:PRK03379  95 GIKVMWV-DATSIEQIANALRQLAPWSPQPEKAEQAAQSLLQQYAALKAQYADKPKK-RVFLQFGTNP-LFTSGKHSIQS 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671700 201 DMLEKLEAQNVYSDIN-GWNPVTKESIIKKNPDILISTeaktrsdymdiikkrGGFNKINAVKN-----TRIEV--VNGD 272
Cdd:PRK03379 172 QVLSLCGGENIFADSRvPWPQVSREQVLARKPQAIVIT---------------GGPDQIPKIKQfwgpqLKIPVipLNSD 236


                 ....*....
gi 446671700 273 EVSRPGPRI 281
Cdd:PRK03379 237 WFERASPRI 245
 
Name Accession Description Interval E-value
YvrC cd01143
Periplasmic binding protein YvrC. These proteins are predicted to function as initial ...
 37-236 2.00e-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: 234.09  E-value: 2.00e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671700  37 SPYHRIVSLMPSNTEILYELGLGKYIVGVSTVDDYPKDVKEGKKQFDALNLNKEELLKAKPDLILAHESQKATankVLSS 116
Cdd:cd01143    1 KEPERIVSLSPSITEILFALGAGDKIVGVDTYSNYPKEVRKKPKVGSYSNPNVEKIVALKPDLVIVSSSSLAE---LLEK 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671700 117 LEKQGIKVVYVKDAQSIDETYNTFKQIGKLTHHDKQAEQLVEETKDNIDKVIDSIPAyHKKSKVFIEVSSkPEIYTAGKH 196
Cdd:cd01143   78 LKDAGIPVVVLPAASSLDEIYDQIELIGKITGAEEEAEKLVKEMKQKIDKVKDKGKT-IKKSKVYIEVSL-GGPYTAGKN 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 446671700 197 TFFNDMLEKLEAQNVYSDINGWNPVTKESIIKKNPDILIS 236
Cdd:cd01143  156 TFINELIRLAGAKNIAADSGGWPQVSPEEILKANPDVIIL 195
FepB COG0614
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ...
 41-293 6.02e-67

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


Pssm-ID: 440379 [Multi-domain]  Cd Length: 264  Bit Score: 209.85  E-value: 6.02e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671700  41 RIVSLMPSNTEILYELGLGKYIVGVS--TVDDYPKDVKEGKKQF-DALNLNKEELLKAKPDLILAHESQkaTANKVLSSL 117
Cdd:COG0614    2 RIVSLSPSATELLLALGAGDRLVGVSdwGYCDYPELELKDLPVVgGTGEPNLEAILALKPDLVLASSSG--NDEEDYEQL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671700 118 EKQGIKVVYVkDAQSIDETYNTFKQIGKLTHHDKQAEQLVEETKDNIDKVIDSIPAYHKKSKVFIEVSSKPEIYTAGKHT 197
Cdd:COG0614   80 EKIGIPVVVL-DPRSLEDLYESIRLLGELLGREERAEALIAEYEARLAAVRARLAGAEERPTVLYEIWSGDPLYTAGGGS 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671700 198 FFNDMLEKLEAQNVYSDIN-GWNPVTKESIIKKNPDILI----STEAKTRSDYMDIIKKRGGFNKINAVKNTRIEVVNGD 272
Cdd:COG0614  159 FIGELLELAGGRNVAADLGgGYPEVSLEQVLALDPDVIIlsggGYDAETAEEALEALLADPGWQSLPAVKNGRVYVVPGD 238

                        250       260
                 ....*....|....*....|.
gi 446671700 273 EVSRPGPRIDEGLKELRDAIY 293
Cdd:COG0614  239 LLSRPGPRLLLALEDLAKALH 259
ChuT COG4558
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism] ...
 1-293 2.25e-58

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


Pssm-ID: 443619 [Multi-domain]  Cd Length: 285  Bit Score: 188.48  E-value: 2.25e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671700   1 MKKSLIAFILIFMLVLSGcgmkdndkqGSDDNGSSKSpyhRIVSLMPSNTEILYELGLGKYIVGVSTVDDYPKDVKegkk 80
Cdd:COG4558    1 MKRLALALLLLALAALAA---------GASVAAAAAE---RIVSLGGSVTEIVYALGAGDRLVGVDTTSTYPAAAK---- 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671700  81 qfdAL-------NLNKEELLKAKPDLILAHESqkATANKVLSSLEKQGIKVVYVKDAQSIDETYNTFKQIGKLTHHDKQA 153
Cdd:COG4558   65 ---ALpdvgymrQLSAEGILSLKPTLVLASEG--AGPPEVLDQLRAAGVPVVVVPAAPSLEGVLAKIRAVAAALGVPEAG 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671700 154 EQLVEETKDNIDKVIDSIPAYHKKSKV-FIEVSSKPEIYTAGKHTFFNDMLEKLEAQNVYSDINGWNPVTKESIIKKNPD 232
Cdd:COG4558  140 EALAARLEADLAALAARVAAIGKPPRVlFLLSRGGGRPMVAGRGTAADALIRLAGGVNAAAGFEGYKPLSAEALIAAAPD 219

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446671700 233 -ILISTEAKTRSDYMDIIKKRGGFNKINAVKNTRIEVVNGDEVSRPGPRIDEGLKELRDAIY 293
Cdd:COG4558  220 vILVMTRGLESLGGVDGLLALPGLAQTPAGKNKRIVAMDDLLLLGFGPRTPQAALALAQALY 281
BtuF cd01144
Cobalamin binding protein BtuF. These proteins have been shown to function as initial ...
 41-288 1.73e-48

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: 161.70  E-value: 1.73e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671700  41 RIVSLMPSNTEILYELGLGKYIVGVSTVDDYPKDVKEGKKQFDALNLNKEELLKAKPDLILAHESQKATAnkVLSSLEKQ 120
Cdd:cd01144    2 RIVSLAPSATELLYALGLGDQLVGVTDYCDYPPEAKKLPRVGGFYQLDLERVLALKPDLVIAWDDCNVCA--VVDQLRAA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671700 121 GIKvVYVKDAQSIDETYNTFKQIGKLTHHDKQAEQLVEETKDNIDKvIDSIPAYHKKSKVFIEVSSKPeIYTAGkHTFFN 200
Cdd:cd01144   80 GIP-VLVSEPQTLDDILADIRRLGTLAGRPARAEELAEALRRRLAA-LRKQYASKPPPRVFYQEWIDP-LMTAG-GDWVP 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671700 201 DMLEKLEAQNVYSDI-NGWNPVTKESIIKKNPD-ILISTEAKTRsdYMDIIKKRGGFNKINAVKNTRIEVVNGDEVSRPG 278
Cdd:cd01144  156 ELIALAGGVNVFADAgERSPQVSWEDVLAANPDvIVLSPCGFGF--TPAILRKEPAWQALPAVRNGRVYAVDGNWYFRPS 233

                        250
                 ....*....|
gi 446671700 279 PRIDEGLKEL 288
Cdd:cd01144  234 PRLVDGLEQL 243
TroA_a cd01148
Metal binding protein TroA_a. These proteins are predicted to function as initial receptors ...
 41-289 2.32e-33

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: 123.22  E-value: 2.32e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671700  41 RIVSLMPSNTEILYELGLGKYIVGVSTVddYPKDVKEGKKQFDALNLN------KEELLKAKPDLILAHESQKATANKVL 114
Cdd:cd01148   20 RVVSNDQNTTEMMLALGLQDRMVGTAGI--DNKDLPELKAKYDKVPELakkypsKETVLAARPDLVFGGWSYGFDKGGLG 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671700 115 S--SLEKQGIKV-------VYVKDAQSIDETYNTFKQIGKLTHHDKQAEQLVEETKDNIDKVIDSIPAYHKKSKVFIEVS 185
Cdd:cd01148   98 TpdSLAELGIKTyilpescGQRRGEATLDDVYNDIRNLGKIFDVEDRADKLVADLKARLAEISAKVKGDGKKVAVFVYDS 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671700 186 SKPEIYTAGKHTFFNDMLEKLEAQNVYSDIN-GWNPVTKESIIKKNPDILISTEAKTRSDYMDIIKKRGGF---NKINAV 261
Cdd:cd01148  178 GEDKPFTSGRGGIPNAIITAAGGRNVFADVDeSWTTVSWETVIARNPDVIVIIDYGDQNAAEQKIKFLKENpalKNVPAV 257

                        250       260
                 ....*....|....*....|....*...
gi 446671700 262 KNTRIeVVNGDEVSRPGPRIDEGLKELR 289
Cdd:cd01148  258 KNNRF-IVLPLAEATPGIRNVDAIEKLA 284
HutB cd01149
Hemin binding protein HutB. These proteins have been shown to function as initial receptors ...
 41-271 1.72e-32

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: 119.68  E-value: 1.72e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671700  41 RIVSLMPSNTEILYELGLGKYIVGVSTVDDYPKDVKegkkqfdAL-------NLNKEELLKAKPDLILA-HESQKATAnk 112
Cdd:cd01149    3 RIVSLGGSVTEIVYALGAGDRLVGVDSTSTYPEAAA-------KLpdvgymrQLSAEGVLSLKPTLVIAsDEAGPPEA-- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671700 113 vLSSLEKQGIKVVYVKDAQSIDETYNTFKQIGKLTHHDKQAEQLVEETKDNIDKVIDSIPAYHKKSKV-FIEVSSKPEIY 191
Cdd:cd01149   74 -LDQLRAAGVPVVTVPSTPTLDGLLTKIRQVAQALGVPEKGEALAQEVRQRLAALRKTVAAHKKPPRVlFLLSHGGGAAM 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671700 192 TAGKHTFFNDMLEKLEAQNVYSDINGWNPVTKESIIKKNPD-ILISTEAKTRSDYMDIIKKRGGFNKINAVKNTRIEVVN 270
Cdd:cd01149  153 AAGRNTAADAIIALAGAVNAAAGFRGYKPLSAEALIAAQPDvILVMSRGLDAVGGVDGLLKLPGLAQTPAGRNKRILAMD 232


                 .
gi 446671700 271 G 271
Cdd:cd01149  233 D 233
Peripla_BP_2 pfam01497
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ...
 43-266 1.56e-28

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: 109.38  E-value: 1.56e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671700   43 VSLMPSNTEILYELGLGKYIVGVS--TVDDYPKDVKEGKKQFDA-LNLNKEELLKAKPDLILAHESQKATANkvlSSLEK 119
Cdd:pfam01497   1 AALSPAYTEILYALGATDSIVGVDayTRDPLKADAVAAIVKVGAyGEINVERLAALKPDLVILSTGYLTDEA---EELLS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671700  120 QGIKVVYVKDAQSIDETYNTFKQIGKLTHHDKQAEQLVEETKDNIDKVIDSIPAYHKKSKVFIEVSSKPEIYTAGKHTFF 199
Cdd:pfam01497  78 LIIPTVIFESSSTGESLKEQIKQLGELLGLEDEAEELVAEIDSALAAAKKAVPSLTRKPVLVFGGADGGGYVVAGSNTYI 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671700  200 NDMLEKLEAQNVYSDIN--GWNPVTKESIIKKNPDILI-STEAKTRSDYMDIIKKRGGFNKINAVKNTRI 266
Cdd:pfam01497 158 GDLLRILGIENIAAELSgsEYAPISFEAILSSNPDVIIvSGRDSFTKTGPEFVAANPLWAGLPAVKNGRV 227
FhuD cd01146
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ...
 41-279 1.87e-27

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: 106.99  E-value: 1.87e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671700  41 RIVSLMPSNTEILyeLGLGKYIVGVSTVDDYPKDVKEGKKQFD---------ALNLnkEELLKAKPDLILAHESQKATAN 111
Cdd:cd01146    5 RIVALDWGALETL--LALGVKPVGVADTAGYKPWIPEPALPLEgvvdvgtrgQPNL--EAIAALKPDLILGSASRHDEIY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671700 112 KVLSSlekqgI-KVVYVKDAQSIDETYNTFKQIGKLTHHDKQAEQLVEETKDNIDKVIDSIPAYHKKSKVFIEVSSKPEI 190
Cdd:cd01146   81 DQLSQ-----IaPTVLLDSSPWLAEWKENLRLIAKALGKEEEAEKLLAEYDQRLAELRQKLPDKGPKPVSVVRFSDAGSI 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671700 191 YTAGKHTFFNDMLEKL-----EAQNVYSDiNGWNPVTKESIIKKNPDILISTEAKTRSDYmDIIKKRGGFNKINAVKNTR 265
Cdd:cd01146  156 RLYGPNSFAGSVLEDLglqnpWAQETTND-SGFATISLERLAKADADVLFVFTYEDEELA-QALQANPLWQNLPAVKNGR 233

                        250
                 ....*....|....
gi 446671700 266 IEVVNGDEVSRPGP 279
Cdd:cd01146  234 VYVVDDVWWFFGGG 247
PRK03379 PRK03379
vitamin B12-transporter protein BtuF; Provisional
 41-281 1.43e-26

vitamin B12-transporter protein BtuF; Provisional


Pssm-ID: 179575 [Multi-domain]  Cd Length: 260  Bit Score: 104.77  E-value: 1.43e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671700  41 RIVSLMPSNTEILYELGLGKyiVGVSTVDDYPKDVKEGKKQFDALNLNKEELLKAKPDLILAHesQKATANKVLSSLEKQ 120
Cdd:PRK03379  19 RVITLSPANTELAFAAGITP--VGVSSYSDYPPQAKKIEQVATWQGMNLERIVALKPDLVLAW--RGGNAERQVDQLASL 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671700 121 GIKVVYVkDAQSIDETYNTFKQIGKLTHHDKQAEQLVEETKDNIDKVIDSIPAYHKKsKVFIEVSSKPeIYTAGKHTFFN 200
Cdd:PRK03379  95 GIKVMWV-DATSIEQIANALRQLAPWSPQPEKAEQAAQSLLQQYAALKAQYADKPKK-RVFLQFGTNP-LFTSGKHSIQS 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671700 201 DMLEKLEAQNVYSDIN-GWNPVTKESIIKKNPDILISTeaktrsdymdiikkrGGFNKINAVKN-----TRIEV--VNGD 272
Cdd:PRK03379 172 QVLSLCGGENIFADSRvPWPQVSREQVLARKPQAIVIT---------------GGPDQIPKIKQfwgpqLKIPVipLNSD 236


                 ....*....
gi 446671700 273 EVSRPGPRI 281
Cdd:PRK03379 237 WFERASPRI 245
TroA-like cd00636
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function ...
 41-182 1.13e-23

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: 94.16  E-value: 1.13e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671700  41 RIVSLMPSNTEILYELGLGKYIVGVSTVDDYPKDVKEGKKQ----FDALNLNKEELLKAKPDLILAHESQkatANKVLSS 116
Cdd:cd00636    2 RVVALDPGATELLLALGGDDKPVGVADPSGYPPEAKALLEKvpdvGHGYEPNLEKIAALKPDLIIANGSG---LEAWLDK 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446671700 117 LEKQGIKVVYVKDAQ--SIDETYNTFKQIGKLTHHDKQAEQLVEETKDNIDKVIDSIPAYHKKSKVFI 182
Cdd:cd00636   79 LSKIAIPVVVVDEASelSLENIKESIRLIGKALGKEENAEELIAELDARLAELRAKLAKIPKKKVSLV 146
btuF PRK09534
corrinoid ABC transporter substrate-binding protein; Reviewed
 41-292 5.72e-23

corrinoid ABC transporter substrate-binding protein; Reviewed


Pssm-ID: 236552 [Multi-domain]  Cd Length: 359  Bit Score: 96.90  E-value: 5.72e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671700  41 RIVSLMPSNTEILYELGLGKYIVGVSTVDDYPKDVKEGK--KQFDALNLNKEELLKAKPDLILAhesQKATANKVLSSLE 118
Cdd:PRK09534  62 RVVTLNPSAAQTMWELGARDRVVGVTQYASYLDGAEERTnvSGGQPFGVNVEAVVGLDPDLVLA---PNAVAGDTVTRLR 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671700 119 KQGIKVVYVKDAQSIDETYNTFKQIGKLTHHDKQAEQLVEETKDNIDKVIDSIPAYHKKSKVFIEVSSKpeiYTAGKHTF 198
Cdd:PRK09534 139 EAGITVFHFPAATSIEDVAEKTATIGRLTGNCEAAAETNAEMRDRVDAVEDRTADVDDRPRVLYPLGDG---YTAGGNTF 215

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671700 199 FNDMLEKLEAQNVYSD--INGWNPVTKESIIKKNPDILISTEAKTrsdymdIIKKRGGFNKINAVKNTRIEVVNGDEVSR 276
Cdd:PRK09534 216 IGALIEAAGGHNVAADatTDGYPQLSEEVIVQQDPDVIVVATASA------LVAETEPYASTTAGETGNVVTVNVNHINQ 289

                        250
                 ....*....|....*.
gi 446671700 277 PGPRIDEGLKELRDAI 292
Cdd:PRK09534 290 PAPRIVESMATMATAF 305
FecB COG4594
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and ...
 1-272 3.48e-22

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


Pssm-ID: 443650 [Multi-domain]  Cd Length: 316  Bit Score: 93.83  E-value: 3.48e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671700   1 MKK-SLIAFILIFMLVLSGCGMKDNDKQGSDDNGSSKSPYH------------RIVSLMPSNTEILYELGLGKyiVGVST 67
Cdd:COG4594    1 MKKlLLLLILLLALLLLAACGSSSSDSSSSEAAAGARTVKHamgettipgtpkRVVVLEWSFADALLALGVTP--VGIAD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671700  68 VDDYPKDVKEGKKQFDAL---------NLnkEELLKAKPDLILA----HESQKATANK-----VLSSLEKQgikvvYvkd 129
Cdd:COG4594   79 DNDYDRWVPYLRDLIKGVtsvgtrsqpNL--EAIAALKPDLIIAdksrHEAIYDQLSKiaptvLFKSRNGD-----Y--- 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671700 130 aqsiDETYNTFKQIGKLTHHDKQAEQLVEETKDNIDKVIDSIPAYHKKSKVFIEVSSKPEIYTAGKHTFFNDMLEKLEAQ 209
Cdd:COG4594  149 ----QENLESFKTIAKALGKEEEAEAVLADHDQRIAEAKAKLAAADKGKKVAVGQFRADGLRLYTPNSFAGSVLAALGFE 224

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446671700 210 NVYS----DINGWNPVTKESIIKKNPDILISTEAKTRSDYmDIIKKRGGFNKINAVKNTRIEVVNGD 272
Cdd:COG4594  225 NPPKqskdNGYGYSEVSLEQLPALDPDVLFIATYDDPSIL-KEWKNNPLWKNLKAVKNGRVYEVDGD 290
TroA_e cd01142
Periplasmic binding protein TroA_e. These proteins are predicted to function as initial ...
 41-269 4.17e-22

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: 93.19  E-value: 4.17e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671700  41 RIVSLMPSNTEILYELGLGKYIVGVSTV----DDYPK---DVKEGKKQFDALNLNKEELLKAKPDLILahesqkatankV 113
Cdd:cd01142   26 RIAALWGAGNAVVAALGGGKLIVATTSTvqqePWLYRlapSLENVATGGTGNDVNIEELLALKPDVVI-----------V 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671700 114 LSSLEKQ-GIKVVYVKDAQSID----ETYN-TFKQIGKLTHHDKQAEQLVEETKDNIDKVID---SIPAYHKKsKVFIEV 184
Cdd:cd01142   95 WSTDGKEaGKAVLRLLNALSLRdaelEEVKlTIALLGELLGRQEKAEALVAYFDDNLAYVAArtkKLPDSERP-RVYYAG 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671700 185 SSKpeIYTAGKHTFFNDMLEKLEAQNVYSDI--NGWNPVTKESIIKKNPDILISTEAKTRsdymDIIKKRGGFNKINAVK 262
Cdd:cd01142  174 PDP--LTTDGTGSITNSWIDLAGGINVASEAtkKGSGEVSLEQLLKWNPDVIIVGNADTK----AAILADPRWQNLRAVK 247


                 ....*..
gi 446671700 263 NTRIEVV 269
Cdd:cd01142  248 NGRVYVN 254
HemV-2 cd01147
Metal binding protein HemV-2. These proteins are predicted to function as initial receptors ...
 38-266 3.29e-21

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: 90.47  E-value: 3.29e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671700  38 PYHRIVSLMPSNTEILYELGLGKYIVGVSTVDDYPKD--VKEGKKQFDAL----------NLNKEELLKAKPDLILAHES 105
Cdd:cd01147    4 PVERVVAAGPGALRLLYALAAPDKIVGVDDAEKSDEGrpYFLASPELKDLpvigrggrgnTPNYEKIAALKPDVVIDVGS 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671700 106 QKATanKVLSSLEKQ-GIKVVYVKDAQSIDETYNTFKQIGKLTHHDKQAEQLV---EETKDNIDKVIDSIPAYHKKSkVF 181
Cdd:cd01147   84 DDPT--SIADDLQKKtGIPVVVLDGGDSLEDTPEQIRLLGKVLGKEERAEELIsfiESILADVEERTKDIPDEEKPT-VY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671700 182 IEvsskpEIYTAGKHTFFND------MLEKLEAQNVYSDINGWN--PVTKESIIKKNPDILISTEAKTRSDYMDIIKKRG 253
Cdd:cd01147  161 FG-----RIGTKGAAGLESGlagsieVFELAGGINVADGLGGGGlkEVSPEQILLWNPDVIFLDTGSFYLSLEGYAKNRP 235

                        250
                 ....*....|...
gi 446671700 254 GFNKINAVKNTRI 266
Cdd:cd01147  236 FWQSLKAVKNGRV 248
TroA_f cd01139
Periplasmic binding protein TroA_f. These proteins are predicted to function as initial ...
 86-266 5.55e-17

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: 79.66  E-value: 5.55e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671700  86 NLNKEELLKAKPDLILAHESQKAT--ANKVLSSLEKQGIKVVYVKDAQSIDEtyNTFKQI---GKLTHHDKQAEQLVEET 160
Cdd:cd01139   81 DFSVEKVLTLKPDLVILNIWAKTTaeESGILEKLEQAGIPVVFVDFRQKPLK--NTTPSMrllGKALGREERAEEFIEFY 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671700 161 KDNIDKVIDSIPAYH-KKSKVFIEVSSK-PEIY--TAGKHTfFNDMLEKLEAQNVYSDING--WNPVTKESIIKKNPDIL 234
Cdd:cd01139  159 QERIDRIRDRLAKINePKPKVFIELGAGgPEECcsTYGNGN-WGELVDAAGGDNIADGLIPgtSGELNAEYVIAANPEII 237

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 446671700 235 I------------------STEAKTRSDYMDIIKKRGGFNKINAVKNTRI 266
Cdd:cd01139  238 IatggnwakdpsgvslgpdGTTADAKESLLRALLKRPGWSSLQAVKNGRV 287
FatB cd01140
Siderophore binding protein FatB. These proteins have been shown to function as ABC-type ...
 41-266 6.58e-12

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: 64.20  E-value: 6.58e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671700  41 RIVSLMPSNTEILYELGLGkyIVGVSTVDDYPKDVK--EGKKQFDALNL---NKEELLKAKPDLILaheSQKATANKVLS 115
Cdd:cd01140   14 KVVVFDVGALDTLDALGVK--VVGVPKSSTLPEYLKkyKDDKYANVGTLfepDLEAIAALKPDLII---IGGRLAEKYDE 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671700 116 SLEKQGIKVVYVKDAQSIDETYNTFKQIGKLTHHDKQAEQLVEETKDNIDKVIDsipAYHKKSKVFIEVSSKPEIYTAGK 195
Cdd:cd01140   89 LKKIAPTIDLGADLKNYLESVKQNIETLGKIFGKEEEAKELVAEIDASIAEAKS---AAKGKKKALVVLVNGGKLSAFGP 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671700 196 HTFFNDMLEKLEAQNVYSDINGWN---PVTKESIIKKNPDIL--------ISTEAKTRSDYM--DIIKkrggfnKINAVK 262
Cdd:cd01140  166 GSRFGWLHDLLGFEPADENIKASShgqPVSFEYILEANPDWLfvidrgaaIGAEGSSAKEVLdnDLVK------NTTAWK 239


                 ....
gi 446671700 263 NTRI 266
Cdd:cd01140  240 NGKV 243
TroA_d cd01141
Periplasmic binding protein TroA_d. These proteins are predicted to function as initial ...
 36-205 3.94e-08

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: 52.42  E-value: 3.94e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671700  36 KSPYHRIVSLMPSNTEILYELGLGKYIVGVSTVDDYPKDVKEgKKQFDAL-----NLNKEELLKAKPDLILAheSQKATA 110
Cdd:cd01141    5 KVPPKRIVVLSPTHVDLLLALDKADKIVGVSASAYDLNTPAV-KERIDIQvgptgSLNVELIVALKPDLVIL--YGGFQA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671700 111 NKVLSSLEKQGIKVVYVKDAQS----IDETYNTFKQIGKLThhdkqaEQLVEETKDNIDKVIDSIPAYHK---KSKVFIE 183
Cdd:cd01141   82 QTILDKLEQLGIPVLYVNEYPSplgrAEWIKFAAAFYGVGK------EDKADEAFAQIAGRYRDLAKKVSnlnKPTVAIG 155

                        170       180
                 ....*....|....*....|..
gi 446671700 184 VSSKPEIYTAGKHTFFNDMLEK 205
Cdd:cd01141  156 KPVKGLWYMPGGNSYVAKMLRD 177
FeuA cd01138
Periplasmic binding protein FeuA. These proteins have predicted to function as initial ...
 41-272 6.97e-06

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: 46.17  E-value: 6.97e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671700  41 RIVSLMPSNTEilyELGLGKYIVGVSTVD----DYPKDVKEGKKQfDALNLNKEELLKAKPDLILAHESQKATANKvlss 116
Cdd:cd01138   11 RIVALSGETEG---LALLGIKPVGAASIGgknpYYKKKTLAKVVG-IVDEPNLEKVLELKPDLIIVSSKQEENYEK---- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671700 117 LEKQGIKVVYVKDAQSIDEtynTFKQIGKLTHHDKQAE-------QLVEETKDNIDKVIDsipayhKKSKVFIEVSSKpE 189
Cdd:cd01138   83 LSKIAPTVPVSYNSSDWEE---QLKEIGKLLNKEDEAEkwladykQKAKEAKEKIKKKLG------NDKSVAVLRGRK-Q 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671700 190 IYTAGK-HTFFNDMLEK---LEAQNVYSDIN---GWNPVTKESIIKKNPD---ILISTEAKTRSDYMdiikKRGGFNKIN 259
Cdd:cd01138  153 IYVFGEdGRGGGPILYAdlgLKAPEKVKEIEdkpGYAAISLEVLPEFDADyifLLFFTGPEAKADFE----SLPIWKNLP 228

                        250
                 ....*....|...
gi 446671700 260 AVKNTRIEVVNGD 272
Cdd:cd01138  229 AVKNNHVYIVDAW 241
fecB PRK11411
iron-dicitrate transporter substrate-binding subunit; Provisional
 63-276 3.82e-05

iron-dicitrate transporter substrate-binding subunit; Provisional


Pssm-ID: 183123 [Multi-domain]  Cd Length: 303  Bit Score: 44.28  E-value: 3.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671700  63 VGVSTV---DDYPK-----DVKEGKKQFDALNLNKEELLKA----KPDLILAHESQKATANKVLSSLEkqgiKVVYVKda 130
Cdd:PRK11411  56 VGVSPVgvaDDNDAkrilpEVRAHLKPWQSVGTRSQPSLEAiaalKPDLIIADSSRHAGVYIALQKIA----PTLLLK-- 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671700 131 qSIDETY----NTFKQIGKLTHHDKQAEQLVEETKDNIDKVIDSIPayhKKSKVFIEVSSKPEIYTAGKHTFFNDMLEKL 206
Cdd:PRK11411 130 -SRNETYqenlQSAAIIGEVLGKKREMQARIEQHKERMAQFASQLP---KGTRVAFGTSREQQFNLHSPESYTGSVLAAL 205

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446671700 207 EAQNVYSDING--WNPVTKESIIKKNPDILISTEAKTRSdymdIIK---KRGGFNKINAVKNTRIEVVNGDEVSR 276
Cdd:PRK11411 206 GLNVPKAPMNGaaMPSISLEQLLALNPDWLLVAHYRQES----IVKrwqQDPLWQMLTAAKKQQVASVDSNTWAR 276
PRK10957 PRK10957
iron-enterobactin transporter periplasmic binding protein; Provisional
 5-159 2.52e-03

iron-enterobactin transporter periplasmic binding protein; Provisional


Pssm-ID: 236806 [Multi-domain]  Cd Length: 317  Bit Score: 38.80  E-value: 2.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671700   5 LIAFILIFMLVLSGCGMKDNDKQG-----SDDNGSS--KSPYHRIVSLMPSNTEILyeLGLGKYIV--GVSTVDDYPKDV 75
Cdd:PRK10957   3 YRLALLLLGLLLSGIAAAQASAAGwprtvTDSRGSVtlESKPQRIVSTSVTLTGTL--LAIDAPVIasGATTPNTRVADD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671700  76 K------------EGKKQFDALNLNKEELLKAKPDLILAHESQKATANKVLSSLEKQGIKVVYVKDAQSIDETYntfKQI 143
Cdd:PRK10957  81 QgffrqwsdvakeRGVEVLYIGEPDAEAVAAQMPDLIVISATGGDSALALYDQLSAIAPTLVIDYDDKSWQELA---TQL 157

                        170
                 ....*....|....*.
gi 446671700 144 GKLTHHDKQAEQLVEE 159
Cdd:PRK10957 158 GEATGLEKQAAAVIAQ 173
 
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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