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GSIB_SHIF8
ID   GSIB_SHIF8              Reviewed;         514 AA.
AC   Q0T6D2;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Glutathione-binding protein GsiB {ECO:0000250|UniProtKB:P75797};
DE   Flags: Precursor;
GN   Name=gsiB {ECO:0000250|UniProtKB:P75797}; OrderedLocusNames=SFV_0813;
OS   Shigella flexneri serotype 5b (strain 8401).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=373384;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=8401;
RX   PubMed=16822325; DOI=10.1186/1471-2164-7-173;
RA   Nie H., Yang F., Zhang X., Yang J., Chen L., Wang J., Xiong Z., Peng J.,
RA   Sun L., Dong J., Xue Y., Xu X., Chen S., Yao Z., Shen Y., Jin Q.;
RT   "Complete genome sequence of Shigella flexneri 5b and comparison with
RT   Shigella flexneri 2a.";
RL   BMC Genomics 7:173-173(2006).
CC   -!- FUNCTION: Part of the ABC transporter complex GsiABCD involved in
CC       glutathione import. Binds glutathione. {ECO:0000250|UniProtKB:P75797}.
CC   -!- SUBUNIT: The complex is composed of two ATP-binding proteins (GsiA),
CC       two transmembrane proteins (GsiC and GsiD) and a solute-binding protein
CC       (GsiB). {ECO:0000250|UniProtKB:P75797}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250|UniProtKB:P75797}.
CC   -!- SIMILARITY: Belongs to the bacterial solute-binding protein 5 family.
CC       {ECO:0000305}.
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DR   EMBL; CP000266; ABF03044.1; -; Genomic_DNA.
DR   RefSeq; WP_000090148.1; NC_008258.1.
DR   AlphaFoldDB; Q0T6D2; -.
DR   SMR; Q0T6D2; -.
DR   EnsemblBacteria; ABF03044; ABF03044; SFV_0813.
DR   KEGG; sfv:SFV_0813; -.
DR   HOGENOM; CLU_017028_7_3_6; -.
DR   OMA; KESPWVP; -.
DR   BioCyc; SFLE373384:SFV_RS04520-MON; -.
DR   Proteomes; UP000000659; Chromosome.
DR   GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:UniProt.
DR   GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR   InterPro; IPR030678; Peptide/Ni-bd.
DR   InterPro; IPR039424; SBP_5.
DR   InterPro; IPR023765; SBP_5_CS.
DR   InterPro; IPR000914; SBP_5_dom.
DR   PANTHER; PTHR30290; PTHR30290; 1.
DR   Pfam; PF00496; SBP_bac_5; 1.
DR   PIRSF; PIRSF002741; MppA; 1.
DR   PROSITE; PS01040; SBP_BACTERIAL_5; 1.
PE   3: Inferred from homology;
KW   Periplasm; Signal; Transport.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..514
FT                   /note="Glutathione-binding protein GsiB"
FT                   /id="PRO_0000279985"
SQ   SEQUENCE   514 AA;  56715 MW;  A543DFF0FB8193FD CRC64;
     MARAVHRSGL VALGIATALM ASCAFAAKDV VVAVGSNFTT LDPYDANDTL SQAVAKSFYQ
     GLFGLDKEMK LKNVLAESYT VSDDGITYTV KLREGIKFQD GTDFNAVAVK ANLDRASDPA
     NHLKRYNLYK NIAKTEAIDP TTVKITLKQP FSAFINILVH PATAMISPTA LEKYGKEIGF
     HPVGTGPYEL DTWNQTDFVK VKKFAGYWQP GLPKLDSITW RPVADNNTRA AMLQTGEAQF
     AFPIPYEQAT LLEKNKNIEL MASPSIMQRY ISMNVTQKPF DNPKVREALN YAINRPALVK
     VAFAGYATPA TGVVPPSIAI AYAQSYKPWP YDPVKARELL KEAGYPNGFS TTLWSSHNHS
     TAQKVLQFTQ QQLAQVGIKA QVTAMDAGQR AAEVEGKGQK ESGVRMFYTG WSASTGEADW
     ALSPLFASQN WPPTLFNTAF YSNKQVDDFL AQALKTNDPA EKTRLYKAAQ DIIWQESPWI
     PLVVEKLVSA HSKNLTGFWI MPDTGFSFED ADLQ
 
 
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