(data stored in SCRATCH zone)

SWISSPROT: Q3Z5J9_SHISS

ID   Q3Z5J9_SHISS            Unreviewed;       266 AA.
AC   Q3Z5J9;
DT   27-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2005, sequence version 1.
DT   08-MAY-2019, entry version 76.
DE   RecName: Full=Vitamin B12-binding protein {ECO:0000256|HAMAP-Rule:MF_01000};
DE   Flags: Precursor;
GN   Name=yadT {ECO:0000313|EMBL:AAZ86963.1};
GN   Synonyms=btuF {ECO:0000256|HAMAP-Rule:MF_01000};
GN   OrderedLocusNames=SSON_0170 {ECO:0000313|EMBL:AAZ86963.1};
OS   Shigella sonnei (strain Ss046).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300269 {ECO:0000313|EMBL:AAZ86963.1, ECO:0000313|Proteomes:UP000002529};
RN   [1] {ECO:0000313|EMBL:AAZ86963.1, ECO:0000313|Proteomes:UP000002529}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ss046 {ECO:0000313|EMBL:AAZ86963.1,
RC   ECO:0000313|Proteomes:UP000002529};
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X.,
RA   Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S.,
RA   Nie H., Peng J., Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y.,
RA   Qiang B., Hou Y., Yu J., Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic
RT   agents of bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(2005).
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; CP000038; AAZ86963.1; -; Genomic_DNA.
DR   SMR; Q3Z5J9; -.
DR   EnsemblBacteria; AAZ86963; AAZ86963; SSON_0170.
DR   KEGG; ssn:SSON_0170; -.
DR   HOGENOM; HOG000282913; -.
DR   KO; K06858; -.
DR   OMA; WQGINLE; -.
DR   BioCyc; SSON300269:G1GL2-197-MONOMER; -.
DR   Proteomes; UP000002529; 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; Q3Z5J9.
DR   SWISS-2DPAGE; Q3Z5J9.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002529};
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_5009019178.
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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