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GSIB_SALPA
ID   GSIB_SALPA              Reviewed;         512 AA.
AC   Q5PGP4;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Glutathione-binding protein GsiB {ECO:0000250|UniProtKB:P75797};
DE   Flags: Precursor;
GN   Name=gsiB {ECO:0000250|UniProtKB:P75797}; OrderedLocusNames=SPA1906;
OS   Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=295319;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9150 / SARB42;
RX   PubMed=15531882; DOI=10.1038/ng1470;
RA   McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S.,
RA   Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R.,
RA   Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F.,
RA   Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W.,
RA   Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M.,
RA   Warren W., Florea L., Spieth J., Wilson R.K.;
RT   "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT   restricted serovars of Salmonella enterica that cause typhoid.";
RL   Nat. Genet. 36:1268-1274(2004).
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; CP000026; AAV77817.1; -; Genomic_DNA.
DR   RefSeq; WP_000191431.1; NC_006511.1.
DR   AlphaFoldDB; Q5PGP4; -.
DR   SMR; Q5PGP4; -.
DR   EnsemblBacteria; AAV77817; AAV77817; SPA1906.
DR   KEGG; spt:SPA1906; -.
DR   HOGENOM; CLU_017028_7_3_6; -.
DR   OMA; KESPWVP; -.
DR   Proteomes; UP000008185; 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; IPR000914; SBP_5_dom.
DR   PANTHER; PTHR30290; PTHR30290; 1.
DR   Pfam; PF00496; SBP_bac_5; 1.
DR   PIRSF; PIRSF002741; MppA; 1.
PE   3: Inferred from homology;
KW   Periplasm; Signal; Transport.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..512
FT                   /note="Glutathione-binding protein GsiB"
FT                   /id="PRO_0000279979"
SQ   SEQUENCE   512 AA;  56563 MW;  2B6691394074C6A9 CRC64;
     MTQFITHKWL AALGLASSIA AFPALAAKDV VVAVGSNFTT LDPYDANDTL SQAVAKSFYQ
     GLFGLDKDMK VKNVLAEGYT VSDDGLTYTI TLRQGVKFQD GADFDAAAVK ANLDRASNPD
     NHLKRYNLYK NIAKTEVVDP VTVKITLKQP FSAFINILAH PATAMISPQA LEKYGKDIGF
     HPVGTGPYQL ETWNQTDFVK VKKFSGYWQQ GLPKLDSITW RPVTDNNTRA AMLQTGEAQF
     AFPIPYEQAA LLAKNKNLEL VASPSIMQRY ISMNVTQKPF DNPKVREALN YAINRQALVK
     VAFAGYATPA TGVVPPSIAY AQSYQPWPYD PAKARELLKE AGYPDGFSTT LWSSHNHSTA
     QKVLQFTQQQ LAQIGIKARI TAMDAGQRAA EVEGKGQKES GVRMFYTGWS ASTGEADWAL
     SPLFASQNWP PTQFNTALYS NKQVDSDLAA ALKTNDPQEK TRLYKEAQDI IWKESPWIPL
     VVEKLVSAHS KNLTGFWIMP DTGFSFDDAD LK
 
 
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