(data stored in SCRATCH zone)

SWISSPROT: C8U1M8_ECO10

ID   C8U1M8_ECO10            Unreviewed;       266 AA.
AC   C8U1M8;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 52.
DE   RecName: Full=Vitamin B12-binding protein {ECO:0000256|HAMAP-Rule:MF_01000};
DE   Flags: Precursor;
GN   Name=btuF {ECO:0000256|HAMAP-Rule:MF_01000,
GN   ECO:0000313|EMBL:BAI29036.1};
GN   OrderedLocusNames=ECO103_0158 {ECO:0000313|EMBL:BAI29036.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI29036.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI29036.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009).
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:0000256|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:0000256|HAMAP-Rule:MF_01000}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|HAMAP-Rule:MF_01000}.
CC   -!- SIMILARITY: Belongs to the BtuF family. {ECO:0000256|HAMAP-
CC       Rule:MF_01000}.
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DR   EMBL; AP010958; BAI29036.1; -; Genomic_DNA.
DR   RefSeq; WP_001129927.1; NC_013353.1.
DR   SMR; C8U1M8; -.
DR   EnsemblBacteria; BAI29036; BAI29036; ECO103_0158.
DR   KEGG; eoh:ECO103_0158; -.
DR   HOGENOM; HOG000282913; -.
DR   KO; K06858; -.
DR   OMA; WQGINLE; -.
DR   BioCyc; ECOL585395:ECO103_RS00810-MONOMER; -.
DR   Proteomes; UP000000959; 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;
DR   PRODOM; C8U1M8.
DR   SWISS-2DPAGE; C8U1M8.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
KW   Disulfide bond {ECO:0000256|HAMAP-Rule:MF_01000};
KW   Periplasm {ECO:0000256|HAMAP-Rule:MF_01000};
KW   Signal {ECO:0000256|HAMAP-Rule:MF_01000};
KW   Transport {ECO:0000256|HAMAP-Rule:MF_01000}.
FT   SIGNAL        1     22       {ECO:0000256|HAMAP-Rule:MF_01000}.
FT   CHAIN        23    266       Vitamin B12-binding protein.
FT                                {ECO:0000256|HAMAP-Rule:MF_01000}.
FT                                /FTId=PRO_5009008809.
FT   DOMAIN       25    266       Fe/B12 periplasmic-binding.
FT                                {ECO:0000259|PROSITE:PS50983}.
FT   REGION      242    246       Cobalamin-binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01000}.
FT   BINDING      50     50       Cobalamin. {ECO:0000256|HAMAP-Rule:
FT                                MF_01000}.
FT   SITE         72     72       Important for BtuC binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_01000}.
FT   SITE        202    202       Important for BtuC binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_01000}.
FT   DISULFID    183    259       {ECO:0000256|HAMAP-Rule:MF_01000}.
SQ   SEQUENCE   266 AA;  29367 MW;  480F2E620ACD6EA1 CRC64;
     MAKSLFRALV ALSFLAPLWL NAAPRVITLS PANTELAFAA GITPVGVSSY SDYPPQAQKI
     EQVSTWQGMN LERIVALKPD LVIAWRGGNA ERQVDQLASL GIKVMWVDAT SIEQIANALR
     QLAPWSPQPD KAEQAAQSLL DQYAQLKAQY ADKPKKRVFL QFGINPPFTS GKESIQNQVL
     EVCGGENIFK DSRVPWPQVS REQVLARSPQ AIVITGGPDQ IPKIKQYWGE QLKIPVIPLT
     SDWFERASPR IILAAQQLCN ALSQVD
//

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