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DSBA_BUCAP
ID   DSBA_BUCAP              Reviewed;         209 AA.
AC   Q8K9D1;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Thiol:disulfide interchange protein DsbA;
DE   Flags: Precursor;
GN   Name=dsbA; OrderedLocusNames=BUsg_415;
OS   Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=198804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sg;
RX   PubMed=12089438; DOI=10.1126/science.1071278;
RA   Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA   Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT   "50 million years of genomic stasis in endosymbiotic bacteria.";
RL   Science 296:2376-2379(2002).
CC   -!- FUNCTION: Involved in disulfide-bond formation. Acts by transferring
CC       its disulfide bond to other proteins (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. DsbA subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AE013218; AAM67960.1; -; Genomic_DNA.
DR   RefSeq; WP_011053927.1; NC_004061.1.
DR   AlphaFoldDB; Q8K9D1; -.
DR   SMR; Q8K9D1; -.
DR   STRING; 198804.BUsg_415; -.
DR   PRIDE; Q8K9D1; -.
DR   EnsemblBacteria; AAM67960; AAM67960; BUsg_415.
DR   KEGG; bas:BUsg_415; -.
DR   eggNOG; COG1651; Bacteria.
DR   HOGENOM; CLU_088255_3_0_6; -.
DR   OMA; NAIHKQK; -.
DR   OrthoDB; 1805428at2; -.
DR   Proteomes; UP000000416; Chromosome.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   CDD; cd03019; DsbA_DsbA; 1.
DR   InterPro; IPR001853; DSBA-like_thioredoxin_dom.
DR   InterPro; IPR023205; DsbA/DsbL.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   Pfam; PF01323; DSBA; 1.
DR   PIRSF; PIRSF001488; Tdi_protein; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Redox-active center; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000250"
FT   CHAIN           20..209
FT                   /note="Thiol:disulfide interchange protein DsbA"
FT                   /id="PRO_0000034249"
FT   DISULFID        49..52
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   209 AA;  25137 MW;  D3A3F8EFEC3BF037 CRC64;
     MKKILIVLYS IFLSFTASSY EFNNKKEYEI EKRNISNVPK VMHFFSFFCP YCYELEKIYN
     IQSLIKNKID KKIKIQTYHV NFLGGEFSKI LTKIWIIAQK MKVEEKIMMP IFKEIQENNT
     ISHTSNIKNI FLQKTGINKD QYNKFWNSFT IKMLIKKNDN DINKIKLNHV PTMIVNGKYV
     IDYYKLEKIF KTNFSKKYIK LIKFLLSKK
 
 
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