ID BTUB_SALPA Reviewed; 614 AA.
AC Q5PK67;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 27-MAR-2024, entry version 108.
DE RecName: Full=Vitamin B12 transporter BtuB {ECO:0000255|HAMAP-Rule:MF_01531};
DE AltName: Full=Cobalamin receptor {ECO:0000255|HAMAP-Rule:MF_01531};
DE AltName: Full=Outer membrane cobalamin translocator {ECO:0000255|HAMAP-Rule:MF_01531};
DE Flags: Precursor;
GN Name=btuB {ECO:0000255|HAMAP-Rule:MF_01531}; OrderedLocusNames=SPA3968;
OS Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=295319;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9150 / SARB42;
RX PubMed=15531882; DOI=10.1038/ng1470;
RA McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S.,
RA Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R.,
RA Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F.,
RA Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W.,
RA Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M.,
RA Warren W., Florea L., Spieth J., Wilson R.K.;
RT "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT restricted serovars of Salmonella enterica that cause typhoid.";
RL Nat. Genet. 36:1268-1274(2004).
CC -!- FUNCTION: Involved in the active translocation of vitamin B12
CC (cyanocobalamin) across the outer membrane to the periplasmic space. It
CC derives its energy for transport by interacting with the trans-
CC periplasmic membrane protein TonB. {ECO:0000255|HAMAP-Rule:MF_01531}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000255|HAMAP-
CC Rule:MF_01531}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01531}.
CC -!- SIMILARITY: Belongs to the TonB-dependent receptor family. BtuB (TC
CC 1.B.14.3.1) subfamily. {ECO:0000255|HAMAP-Rule:MF_01531}.
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DR EMBL; CP000026; AAV79730.1; -; Genomic_DNA.
DR RefSeq; WP_000591403.1; NC_006511.1.
DR AlphaFoldDB; Q5PK67; -.
DR SMR; Q5PK67; -.
DR KEGG; spt:SPA3968; -.
DR HOGENOM; CLU_008287_18_5_6; -.
DR Proteomes; UP000008185; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046930; C:pore complex; IEA:UniProtKB-KW.
DR GO; GO:0015420; F:ABC-type vitamin B12 transporter activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015288; F:porin activity; IEA:UniProtKB-KW.
DR GO; GO:0006811; P:monoatomic ion transport; IEA:UniProtKB-KW.
DR CDD; cd01347; ligand_gated_channel; 1.
DR Gene3D; 2.40.170.20; TonB-dependent receptor, beta-barrel domain; 1.
DR Gene3D; 2.170.130.10; TonB-dependent receptor, plug domain; 1.
DR HAMAP; MF_01531; BtuB; 1.
DR InterPro; IPR010101; B12_transptr_BtuB.
DR InterPro; IPR012910; Plug_dom.
DR InterPro; IPR037066; Plug_dom_sf.
DR InterPro; IPR039426; TonB-dep_rcpt-like.
DR InterPro; IPR000531; TonB-dep_rcpt_b-brl.
DR InterPro; IPR010916; TonB_box_CS.
DR InterPro; IPR036942; TonB_rcpt_b-brl_sf.
DR InterPro; IPR010917; TonB_rcpt_CS.
DR NCBIfam; TIGR01779; TonB-B12; 1.
DR PANTHER; PTHR30069; TONB-DEPENDENT OUTER MEMBRANE RECEPTOR; 1.
DR PANTHER; PTHR30069:SF29; VITAMIN B12 TRANSPORTER BTUB; 1.
DR Pfam; PF07715; Plug; 1.
DR Pfam; PF00593; TonB_dep_Rec; 1.
DR SUPFAM; SSF56935; Porins; 1.
DR PROSITE; PS00430; TONB_DEPENDENT_REC_1; 1.
DR PROSITE; PS01156; TONB_DEPENDENT_REC_2; 1.
DR PROSITE; PS52016; TONB_DEPENDENT_REC_3; 1.
PE 3: Inferred from homology;
KW Calcium; Cell outer membrane; Ion transport; Membrane; Metal-binding;
KW Porin; Signal; TonB box; Transmembrane; Transmembrane beta strand;
KW Transport.
FT SIGNAL 1..20
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT CHAIN 21..614
FT /note="Vitamin B12 transporter BtuB"
FT /id="PRO_0000003487"
FT TRANSMEM 158..165
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT TRANSMEM 169..178
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT TRANSMEM 184..195
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT TRANSMEM 217..227
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT TRANSMEM 232..248
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT TRANSMEM 263..277
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT TRANSMEM 279..296
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT TRANSMEM 309..325
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT TRANSMEM 328..337
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT TRANSMEM 353..369
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT TRANSMEM 371..381
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT TRANSMEM 385..400
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT TRANSMEM 403..417
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT TRANSMEM 434..443
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT TRANSMEM 449..458
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT TRANSMEM 473..490
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT TRANSMEM 494..509
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT TRANSMEM 517..529
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT TRANSMEM 535..550
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT TRANSMEM 558..572
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT TRANSMEM 585..596
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT TRANSMEM 602..614
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT DOMAIN 38..152
FT /note="TBDR plug"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01360"
FT DOMAIN 155..614
FT /note="TBDR beta-barrel"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01360"
FT MOTIF 26..33
FT /note="TonB box"
FT MOTIF 597..614
FT /note="TonB C-terminal box"
FT BINDING 85
FT /ligand="cyanocob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:17439"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT BINDING 92
FT /ligand="cyanocob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:17439"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT BINDING 110..111
FT /ligand="cyanocob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:17439"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT BINDING 199
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT BINDING 211
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT BINDING 213
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT BINDING 213
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT BINDING 215
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT BINDING 215
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT BINDING 249
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT BINDING 250
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT BINDING 250
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT BINDING 251
FT /ligand="cyanocob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:17439"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT BINDING 261
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT BINDING 309
FT /ligand="cyanocob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:17439"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT BINDING 517
FT /ligand="cyanocob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:17439"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT BINDING 551
FT /ligand="cyanocob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:17439"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
SQ SEQUENCE 614 AA; 68512 MW; 5A342AF435E065F5 CRC64;
MIKKATLLTA FSVTAFSAWA QDTSPDTLVV TANRFQQPRS AVLAPVTIVT RQDIERWQST
SVNDVLRRLP GVDIAQSGGA GQNSSIFIRG TNSSHVLVLI DGVRLNLAGV SGSADLSQFP
VSLVQRIEYI RGPRSAIYGS DAIGGVVNII TTRDNPGTEL TAGWGSNSYQ NYDISTQQQL
GENTRATLIG DYEYTKGFDV VAKGGTGMQA QPDRDGFLSK TLYGALEHTF SDRWSGFVRG
YGYDNRTDYD AYYSPGSPLI DTRKLYSQSW DAGLRFNGER IQSQLVSSYS HSKDYNYDPH
YGRYDTSATL DEMKQYNVQW TNSVVVGHGN VGAGVDWQKQ TTTPGTGYVP EGYDQRNTGV
YLTGLQQLGD FTLEAAARSD DNSQFGRHGT WQTSAGWEFI EGYRFIASYG TSYKAPNLGQ
LYGYYGNPNL NPEKSKQWEG AFEGLTAGVS WRISGYRNDI NDMIDYDDHL QKYYNEGKAR
IKGIEATANF DTGPLTHTVS YDYVDARNAI TDTPLPRRSK QMAKYQLDWD VYDFDWGVTY
QYLGSRYDSD YSAYPYRTVK MGGVSLWDLT VAYPVTSHLT VRGKIANLFD KDYETVYGYQ
TAGREYTLSG SYTF
//
