(data stored in SCRATCH3701 zone)

SWISSPROT: BTUF_VIBVY

ID   BTUF_VIBVY              Reviewed;         273 AA.
AC   Q7MNT2;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   11-DEC-2019, entry version 85.
DE   RecName: Full=Vitamin B12-binding protein {ECO:0000255|HAMAP-Rule:MF_01000};
DE   Flags: Precursor;
GN   Name=btuF {ECO:0000255|HAMAP-Rule:MF_01000}; OrderedLocusNames=VV0633;
OS   Vibrio vulnificus (strain YJ016).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=196600;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJ016;
RX   PubMed=14656965; DOI=10.1101/gr.1295503;
RA   Chen C.-Y., Wu K.-M., Chang Y.-C., Chang C.-H., Tsai H.-C., Liao T.-L.,
RA   Liu Y.-M., Chen H.-J., Shen A.B.-T., Li J.-C., Su T.-L., Shao C.-P.,
RA   Lee C.-T., Hor L.-I., Tsai S.-F.;
RT   "Comparative genome analysis of Vibrio vulnificus, a marine pathogen.";
RL   Genome Res. 13:2577-2587(2003).
CC   -!- FUNCTION: Part of the ABC transporter complex BtuCDF involved in
CC       vitamin B12 import. Binds vitamin B12 and delivers it to the
CC       periplasmic surface of BtuC. {ECO:0000255|HAMAP-Rule:MF_01000}.
CC   -!- SUBUNIT: The complex is composed of two ATP-binding proteins (BtuD),
CC       two transmembrane proteins (BtuC) and a solute-binding protein (BtuF).
CC       {ECO:0000255|HAMAP-Rule:MF_01000}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000255|HAMAP-Rule:MF_01000}.
CC   -!- SIMILARITY: Belongs to the BtuF family. {ECO:0000255|HAMAP-
CC       Rule:MF_01000}.
DR   EMBL; BA000037; BAC93397.1; -; Genomic_DNA.
DR   RefSeq; WP_011149515.1; NC_005139.1.
DR   SMR; Q7MNT2; -.
DR   STRING; 672.VV93_v1c05730; -.
DR   EnsemblBacteria; BAC93397; BAC93397; BAC93397.
DR   GeneID; 2623402; -.
DR   KEGG; vvy:VV0633; -.
DR   PATRIC; fig|196600.6.peg.652; -.
DR   HOGENOM; HOG000282913; -.
DR   KO; K06858; -.
DR   OMA; WQGINLE; -.
DR   OrthoDB; 1473468at2; -.
DR   Proteomes; UP000002675; Chromosome I.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0031419; F:cobalamin binding; IEA:InterPro.
DR   GO; GO:0015889; P:cobalamin transport; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01000; BtuF; 1.
DR   InterPro; IPR002491; ABC_transptr_periplasmic_BD.
DR   InterPro; IPR023544; ABC_transptr_vit_B12-bd.
DR   Pfam; PF01497; Peripla_BP_2; 1.
DR   PROSITE; PS50983; FE_B12_PBP; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q7MNT2.
DR   SWISS-2DPAGE; Q7MNT2.
KW   Disulfide bond; Periplasm; Reference proteome; Signal; Transport.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01000"
FT   CHAIN           19..273
FT                   /note="Vitamin B12-binding protein"
FT                   /id="PRO_0000003511"
FT   DOMAIN          23..273
FT                   /note="Fe/B12 periplasmic-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01000"
FT   SITE            72
FT                   /note="Important for BtuC binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01000"
FT   SITE            202
FT                   /note="Important for BtuC binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01000"
FT   DISULFID        183..263
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01000"
SQ   SEQUENCE   273 AA;  30896 MW;  25C28B6A11A923C2 CRC64;
     MMKTLSSLLL LFSVSLQAAP IERVISLAPH ATEIAYAAGL GDKLIAVSEM SDYPEAAKKL
     EKVSNYKGIN LEKIITLKPD LILAWPAGNP AKELEKLEQF GFKIYYSQTK SLKDIGDNIE
     QLSQYSDDPQ IGLNNARDYR THLEALRAKY QNLPKTRYFY QLSDTPIITV AGQNWPTEVF
     RFCGGENVFD GASAPYPQVS IEQVILKRPQ AMFVSPHAIQ NNGMWSPWVE EIPALKNAHF
     WQLNSDWLNR PTPRTLLAIE QVCEHFASIE QKR
//

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