(data stored in ACNUC7421 zone)

SWISSPROT: 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   05-JUL-2017, entry version 94.
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.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., 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.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and 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
CC       (BtuD), two transmembrane proteins (BtuC) and a solute-binding
CC       protein (BtuF). {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; 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_MWVM01000012.1.
DR   ProteinModelPortal; Q8X8Z0; -.
DR   SMR; Q8X8Z0; -.
DR   STRING; 155864.Z0169; -.
DR   EnsemblBacteria; AAG54462; AAG54462; Z0169.
DR   EnsemblBacteria; BAB33585; BAB33585; BAB33585.
DR   GeneID; 913812; -.
DR   KEGG; ece:Z0169; -.
DR   KEGG; ecs:ECs0162; -.
DR   PATRIC; fig|386585.9.peg.262; -.
DR   eggNOG; ENOG4105JKQ; Bacteria.
DR   eggNOG; COG0614; LUCA.
DR   HOGENOM; HOG000282913; -.
DR   KO; K06858; -.
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:InterPro.
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; Q8X8Z0.
DR   SWISS-2DPAGE; Q8X8Z0.
KW   Complete proteome; Disulfide bond; Periplasm; Signal; Transport.
FT   SIGNAL        1     22       {ECO:0000255|HAMAP-Rule:MF_01000}.
FT   CHAIN        23    266       Vitamin B12-binding protein.
FT                                /FTId=PRO_0000003498.
FT   DOMAIN       25    266       Fe/B12 periplasmic-binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_01000}.
FT   REGION      242    246       Cobalamin-binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_01000}.
FT   BINDING      50     50       Cobalamin. {ECO:0000255|HAMAP-
FT                                Rule:MF_01000}.
FT   SITE         72     72       Important for BtuC binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_01000}.
FT   SITE        202    202       Important for BtuC binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_01000}.
FT   DISULFID    183    259       {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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