BTUB_YERPS
ID BTUB_YERPS Reviewed; 624 AA.
AC Q66G57;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 106.
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=YPTB0125;
OS Yersinia pseudotuberculosis serotype I (strain IP32953).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=273123;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IP32953;
RX PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA Derbise A., Hauser L.J., Garcia E.;
RT "Insights into the evolution of Yersinia pestis through whole-genome
RT comparison with Yersinia pseudotuberculosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(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; BX936398; CAH19365.1; -; Genomic_DNA.
DR RefSeq; WP_024063655.1; NZ_CP009712.1.
DR AlphaFoldDB; Q66G57; -.
DR SMR; Q66G57; -.
DR PRIDE; Q66G57; -.
DR EnsemblBacteria; CAH19365; CAH19365; YPTB0125.
DR GeneID; 66843482; -.
DR KEGG; ypo:BZ17_2471; -.
DR KEGG; yps:YPTB0125; -.
DR PATRIC; fig|273123.14.peg.2590; -.
DR OMA; SYELQWR; -.
DR Proteomes; UP000001011; 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; Signal; TonB box; Transmembrane; Transmembrane beta strand;
KW Transport.
FT SIGNAL 1..21
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT CHAIN 22..624
FT /note="Vitamin B12 transporter BtuB"
FT /id="PRO_0000003496"
FT TRANSMEM 163..170
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT TRANSMEM 174..183
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT TRANSMEM 189..200
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT TRANSMEM 222..232
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT TRANSMEM 237..253
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT TRANSMEM 268..282
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT TRANSMEM 284..301
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT TRANSMEM 314..330
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT TRANSMEM 333..342
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT TRANSMEM 358..374
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT TRANSMEM 376..386
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT TRANSMEM 390..405
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT TRANSMEM 408..422
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT TRANSMEM 440..449
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT TRANSMEM 455..464
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT TRANSMEM 480..498
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT TRANSMEM 502..517
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT TRANSMEM 525..537
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT TRANSMEM 543..557
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT TRANSMEM 568..582
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT TRANSMEM 595..606
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT TRANSMEM 612..624
FT /note="Beta stranded"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT MOTIF 31..38
FT /note="TonB box"
FT MOTIF 607..624
FT /note="TonB C-terminal box"
FT BINDING 88
FT /ligand="cyanocob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:17439"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT BINDING 90
FT /ligand="cyanocob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:17439"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT BINDING 97
FT /ligand="cyanocob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:17439"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT BINDING 115..116
FT /ligand="cyanocob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:17439"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT BINDING 204
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT BINDING 216
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT BINDING 218
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT BINDING 218
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT BINDING 220
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT BINDING 220
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT BINDING 254
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT BINDING 255
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT BINDING 255
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT BINDING 266
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT BINDING 314
FT /ligand="cyanocob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:17439"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT BINDING 525
FT /ligand="cyanocob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:17439"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
SQ SEQUENCE 624 AA; 69493 MW; 3C3F3DF774EC4E83 CRC64;
MTIKKYTLLT ALSVTAFSGW AQGNNTTDNN NEMVVTANRF PQPKSSVLAP VDVVTRADID
RWQSTNINDV LRRLPGINIA QYGGPRQLSS LFIRGTNSSH VLVLVDGVRL NQAGISGSSD
LSQIPISLVQ RIEYIRGPRS AVYGSDAIGG VVNIITERET LGSTLTAGLG SNGYQNYNGS
TQQKLGDDTT ITLAGNYDYS KGYDVVAKGN TGMASQPDRD GYLGKMLWLG ANHKFNEQFS
GFVRGYGFDN RSDYDSYYYP GSPLVDTRSL SSRTYDTGIN FSNGGYASQL IGSYSRTQDY
NYDPSYGRYD QSATLDDISQ YNLQWTNTYQ LGLGNVGGGL DWQKQTTEPG TNYLSNGYEQ
RNTGVYGTVQ QFVGPVTLEG AIRGDDNSQF GWHTTWQSSA GWEFVDGYRL IGSYGTAFKA
PNLGQIYSST YGNRDLKPEE STQWEAAITG ITGPLDWRLS AYRNDIDQMI ATRGVYPNSR
YYNVEKATIK GVEWTGSFET GPLSHQVTLE YLDPRNADTH EILARRAKQQ VKYQLDWQMA
DLDWSVTYQY IGQRYDSVFD PITYAASPVK LAGISLWDLA VSYPVTSHLT VRGRIANLFD
KDYEMVYGYQ TPGREYYFTG SYNF
