ID   BTUB_VIBPA              Reviewed;         624 AA.
AC   Q87KN9;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 110.
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=VP2938;
OS   Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=223926;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIMD 2210633;
RX   PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA   Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA   Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA   Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT   "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT   distinct from that of V. cholerae.";
RL   Lancet 361:743-749(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}.
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DR   EMBL; BA000031; BAC61201.1; -; Genomic_DNA.
DR   RefSeq; NP_799317.1; NC_004603.1.
DR   RefSeq; WP_005454756.1; NC_004603.1.
DR   AlphaFoldDB; Q87KN9; -.
DR   SMR; Q87KN9; -.
DR   STRING; 223926.28807964; -.
DR   PRIDE; Q87KN9; -.
DR   EnsemblBacteria; BAC61201; BAC61201; BAC61201.
DR   GeneID; 1190524; -.
DR   KEGG; vpa:VP2938; -.
DR   PATRIC; fig|223926.6.peg.2828; -.
DR   eggNOG; COG4206; Bacteria.
DR   HOGENOM; CLU_008287_18_5_6; -.
DR   OMA; SYELQWR; -.
DR   Proteomes; UP000002493; Chromosome 1.
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: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   PROSITE; PS00430; TONB_DEPENDENT_REC_1; 1.
DR   PROSITE; PS01156; TONB_DEPENDENT_REC_2; 1.
PE   3: Inferred from homology;
KW   Cell outer membrane; Ion transport; Membrane; Porin; Reference proteome;
KW   Signal; TonB box; Transmembrane; Transmembrane beta strand; Transport.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01531"
FT   CHAIN           23..624
FT                   /note="Vitamin B12 transporter BtuB"
FT                   /id="PRO_0000003492"
FT   MOTIF           29..36
FT                   /note="TonB box"
FT   MOTIF           607..624
FT                   /note="TonB C-terminal box"
SQ   SEQUENCE   624 AA;  69317 MW;  5A5FD501BCE54496 CRC64;
     MKKSALAITL ASLLSPVSYL QAQEISVDET IVVTANRFKQ IDGAVLAQTV TVTKEDIRRQ
     QADSLFDVFR TLPSIEVAQY GGRGQSASIF VRGGSATQVL VLVDGVRMPR AIMGGIDFNQ
     FPINSIERID YIRGARASIY GSEAISGVIN IITRASIDDD ASRVSAGYGS NNHKKGTFAV
     SKPVGEGKHI KGVLGYEKTD GFNVKPLPGL NDGDEHGFET LNLKLGYQQN FSDNFSGYVG
     FSTYSNEYDY DNSSYGNPGW GTVDKHEKKT GEVEYVGADL SLEYSKDVYT SELKLAYGQQ
     DNYDLKSGQS KSTGDHVAIE QFNAIWLNSY SINDELSIGG GLDYRNEKLA KGYLAPSDWG
     PAKDYNPEKN PRTNIGISAI AQYALNAWTF EASVRNDENN QFGNNTTWQT AAGWKVYEGY
     ELTLSHGTAF RAPSFVDLYY PGYEMPNLKP EESKNTELSL SGVASIVDWT VTGYYNQIEN
     MLIWKGAGMQ NIGEAEIKGI ELEVKLDTDI VSHEFYLDYK DPVDKSGAED TQLAYRSKRG
     AKWNAYATFD QWTLGSQYLY QGERFNGSTR LPSYSLWNFT ASYAVNSSWD INAKLSNAFD
     KNYEMYSGYA TPGRQYFVSA DYRF