BTUB_SHIFL
ID BTUB_SHIFL Reviewed; 614 AA.
AC Q83IS4; Q7UB95;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 2.
DT 03-AUG-2022, entry version 131.
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};
GN OrderedLocusNames=SF4048, S3696;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE005674; AAN45477.2; -; Genomic_DNA.
DR EMBL; AE014073; AAP18725.1; -; Genomic_DNA.
DR RefSeq; NP_709770.2; NC_004337.2.
DR RefSeq; WP_000591336.1; NZ_WPGW01000135.1.
DR AlphaFoldDB; Q83IS4; -.
DR SMR; Q83IS4; -.
DR STRING; 198214.SF4048; -.
DR EnsemblBacteria; AAN45477; AAN45477; SF4048.
DR EnsemblBacteria; AAP18725; AAP18725; S3696.
DR GeneID; 1025065; -.
DR KEGG; sfl:SF4048; -.
DR KEGG; sft:NCTC1_04385; -.
DR KEGG; sfx:S3696; -.
DR PATRIC; fig|198214.7.peg.4771; -.
DR HOGENOM; CLU_008287_18_5_6; -.
DR OrthoDB; 71288at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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: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; 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; PS01156; TONB_DEPENDENT_REC_2; 1.
PE 3: Inferred from homology;
KW Calcium; Cell outer membrane; Ion transport; Membrane; Metal-binding;
KW Porin; Reference proteome; Signal; TonB box; Transmembrane;
KW Transmembrane beta strand; 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_0000003490"
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 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: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; 68436 MW; 1582DF2F00249988 CRC64;
MIKKASLLTA CSVTAFSAWA QDTSPDTLVV TAIRFEQPRS TVLAPTTVVT RQDIDRWQST
SVNDVLRRLP GVDITQNGGS GQLSSIFIRG TNASHVLVLI DGVRLNLAGV SGSADLSQFP
IALVQRIEYI RGPRSAVYGS DAIGGVVNII TTRDEPGTEI SAGWGSNSYQ NYDVSTQQQL
GDKTRVTLLG DYAHTHGYDV VAYGNTGTQA QTDNDGFLSK TLYGALEHNF TDAWSGFVRG
YGYDNRTNYD AYYSPGSPLL DTRKLYSQSW DAGLRYNGEL IKSQLITSYS HSKDYNYDPH
YGRYDSSATL DEMKQYTVQW ANNVIVGHGS IGAGVDWQKQ TTTPGTGYVE DGYDQRNTGI
YLTGLQQVGD FTFEGAARSD DNSQFGRHGT WQTSAGWEFI EGYRFIASYG TSYKALNLGQ
LYGFYGNPNL DPEKSKQWEG AFEGLTAGVN WRISGYRNDV SDLIDYDDHT LKYYNEGKAR
IKGVEATANF DTGPLTHTVS YDYVDARNAI TDTPLLRRAK QQVKYQLDWQ LYDFDWGITY
QYLGTRYDKD YSSYPYQTVK MGGVSLWDLA VAYPVTSHLT VRGKIANLFD KDYETVYGYQ
TAGREYTLSG SYTF
