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BTUF_ECO57
ID   BTUF_ECO57              Reviewed;         266 AA.
AC   Q8X8Z0;
DT   05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   05-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 110.
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};
GN   OrderedLocusNames=Z0169, ECs0162;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
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}.
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DR   EMBL; AE005174; AAG54462.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB33585.1; -; Genomic_DNA.
DR   PIR; B85500; B85500.
DR   PIR; B90649; B90649.
DR   RefSeq; NP_308189.1; NC_002695.1.
DR   RefSeq; WP_001129925.1; NZ_SEKU01000001.1.
DR   AlphaFoldDB; Q8X8Z0; -.
DR   SMR; Q8X8Z0; -.
DR   STRING; 155864.EDL933_0163; -.
DR   EnsemblBacteria; AAG54462; AAG54462; Z0169.
DR   EnsemblBacteria; BAB33585; BAB33585; ECs_0162.
DR   GeneID; 913812; -.
DR   KEGG; ece:Z0169; -.
DR   KEGG; ecs:ECs_0162; -.
DR   PATRIC; fig|386585.9.peg.262; -.
DR   eggNOG; COG0614; Bacteria.
DR   HOGENOM; CLU_038034_2_5_6; -.
DR   OMA; WQGINLE; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
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;
KW   Disulfide bond; Periplasm; Reference proteome; Signal; Transport.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01000"
FT   CHAIN           23..266
FT                   /note="Vitamin B12-binding protein"
FT                   /id="PRO_0000003498"
FT   DOMAIN          25..266
FT                   /note="Fe/B12 periplasmic-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01000"
FT   BINDING         50
FT                   /ligand="cyanocob(III)alamin"
FT                   /ligand_id="ChEBI:CHEBI:17439"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01000"
FT   BINDING         242..246
FT                   /ligand="cyanocob(III)alamin"
FT                   /ligand_id="ChEBI:CHEBI:17439"
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..259
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01000"
SQ   SEQUENCE   266 AA;  29394 MW;  481FC060C5124F6C CRC64;
     MAKSLFRALV ALSFLAPLWL NAAPRVITLS PANTELAFAA GITPVGVSSY SDYPPQAQKI
     EQVSTWQGMN LERIVALKPD LVIAWRGGNA ERQVDQLASL GIKVMWVDAT NIEQIANALR
     QLAPWSPQPD KAEQAAQSLL DQYAQLKAQY ADKPKKRVFL QFGINPPFTS GKESIQNQVL
     EVCGGENIFK DSRVPWPQVS REQVLARSPQ AIVITGGPDQ IPKIKQYWGE QLKIPVIPLT
     SDWFERASPR IILAAQQLCN ALSQVD
 
 
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