BTUB_ECOLX
ID BTUB_ECOLX Reviewed; 614 AA.
AC Q93SE0;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 2.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Vitamin B12 transporter BtuB;
DE AltName: Full=Cobalamin receptor;
DE AltName: Full=Outer membrane cobalamin translocator;
DE Flags: Precursor;
GN Name=btuB;
OS Escherichia coli.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=O91:H- / 4797/97;
RX PubMed=11598060; DOI=10.1128/iai.69.11.6863-6873.2001;
RA Schmidt H., Zhang W.-L., Hemmrich U., Jelacic S., Brunder W., Tarr P.I.,
RA Dobrindt U., Hacker J., Karch H.;
RT "Identification and characterization of a novel genomic island integrated
RT at selC in locus of enterocyte effacement-negative, Shiga toxin-producing
RT Escherichia coli.";
RL Infect. Immun. 69:6863-6873(2001).
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TonB-dependent receptor family. BtuB (TC
CC 1.B.14.3.1) subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAC39289.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ278144; CAC39289.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_000593013.1; NZ_WSIS01000048.1.
DR AlphaFoldDB; Q93SE0; -.
DR SMR; Q93SE0; -.
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:ion transport; IEA:UniProtKB-KW.
DR Gene3D; 2.170.130.10; -; 1.
DR Gene3D; 2.40.170.20; -; 1.
DR HAMAP; MF_01531; BtuB; 1.
DR InterPro; IPR010101; B12_transptr_BtuB.
DR InterPro; IPR039426; BtuB-like.
DR InterPro; IPR012910; Plug_dom.
DR InterPro; IPR037066; Plug_dom_sf.
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 PANTHER; PTHR30069; PTHR30069; 1.
DR Pfam; PF07715; Plug; 1.
DR Pfam; PF00593; TonB_dep_Rec; 1.
DR TIGRFAMs; TIGR01779; TonB-B12; 1.
DR PROSITE; PS00430; TONB_DEPENDENT_REC_1; 1.
DR PROSITE; PS01156; TONB_DEPENDENT_REC_2; 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:0000250"
FT CHAIN 21..614
FT /note="Vitamin B12 transporter BtuB"
FT /id="PRO_0000003480"
FT TRANSMEM 158..165
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TRANSMEM 169..178
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TRANSMEM 184..195
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TRANSMEM 217..227
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TRANSMEM 232..248
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TRANSMEM 263..277
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TRANSMEM 279..296
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TRANSMEM 309..325
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TRANSMEM 328..337
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TRANSMEM 353..369
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TRANSMEM 371..381
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TRANSMEM 385..400
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TRANSMEM 403..417
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TRANSMEM 434..443
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TRANSMEM 449..458
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TRANSMEM 473..490
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TRANSMEM 494..509
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TRANSMEM 517..529
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TRANSMEM 535..550
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TRANSMEM 558..572
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TRANSMEM 585..596
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TRANSMEM 602..614
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT MOTIF 26..33
FT /note="TonB box"
FT MOTIF 597..614
FT /note="TonB C-terminal box"
FT BINDING 83
FT /ligand="cyanocob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:17439"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
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:0000250"
FT BINDING 211
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 213
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 213
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 215
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 215
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 249
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 250
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 250
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
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:0000250"
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; 69053 MW; 5F48841AD36AC896 CRC64;
MIKKYWFLMV YSVTAFSVWA QDTPLDTLVV TANRFQEPLS TVLAPVTIVT REDIDRWQVS
SVNDVLRRLP GVAISQHGGE GQLSTIFVRG TNSNHTLVLI DGVRLNLAGV SGAADLSQFP
VALVQRIEYI RGPRSAIYGS DAIGGVINII TSRENTGTEI SAGWGSNSYQ HYDISTHQQL
GENTRVTLLG DYTYTRGFDA VAYGSTGMQP QSDRDGFLSK TFYGKLEHNL SDTWSGFVRG
YGYNNRTKYD AWYSPGSPLI DTRKLYSQSW DAGLRYAGET LQSQLVSSYS HSKDYNYDPH
YGRYDTSANL DDMKQYNLQW TNSVTVGHGN VGAGIDWQKQ STTPGTGYLP KGYDQRNTGI
YLTGLQKLGD FTLEGAVRND DNSQFERHTT WQSSAGWEFI EGYRFIASYG TAFKAPNLGQ
LYGMYGNPNL APEKSKQWEG AFEGLTGGVN WRISGYRNDI SEMINYNPHT LRYYNDGKVH
VKGIEATVNF DTGALTHTVS YDYTDARNAL TDKPLERRPK LQVKYQLDWQ VFDFDWGITY
QYMGSRYDSD YSSWPYKSVK MGGVSLWDVA VAYPVTPHLI VRGKIANLFN KDYETGYGYQ
AAGREYILSG SYTF
