(data stored in ACNUC7421 zone)

SWISSPROT: Q3Z4I9_SHISS

ID   Q3Z4I9_SHISS            Unreviewed;       252 AA.
AC   Q3Z4I9;
DT   27-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2005, sequence version 1.
DT   08-MAY-2019, entry version 85.
DE   RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|RuleBase:RU364038};
GN   Name=dsbG {ECO:0000313|EMBL:AAZ87323.1};
GN   OrderedLocusNames=SSON_0556 {ECO:0000313|EMBL:AAZ87323.1};
OS   Shigella sonnei (strain Ss046).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300269 {ECO:0000313|EMBL:AAZ87323.1, ECO:0000313|Proteomes:UP000002529};
RN   [1] {ECO:0000313|EMBL:AAZ87323.1, ECO:0000313|Proteomes:UP000002529}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ss046 {ECO:0000313|EMBL:AAZ87323.1,
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: Required for disulfide bond formation in some
CC       periplasmic proteins. Acts by transferring its disulfide bond to
CC       other proteins and is reduced in the process.
CC       {ECO:0000256|RuleBase:RU364038}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|RuleBase:RU364038}.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. DsbC subfamily.
CC       {ECO:0000256|RuleBase:RU364038}.
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DR   EMBL; CP000038; AAZ87323.1; -; Genomic_DNA.
DR   EnsemblBacteria; AAZ87323; AAZ87323; SSON_0556.
DR   KEGG; ssn:SSON_0556; -.
DR   HOGENOM; HOG000117889; -.
DR   KO; K03805; -.
DR   OMA; CPYCNMF; -.
DR   BioCyc; SSON300269:G1GL2-654-MONOMER; -.
DR   Proteomes; UP000002529; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   CDD; cd03020; DsbA_DsbC_DsbG; 1.
DR   Gene3D; 3.10.450.70; -; 1.
DR   InterPro; IPR033954; DiS-bond_Isoase_DsbC/G.
DR   InterPro; IPR009094; DiS-bond_isomerase_DsbC/G_N_sf.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   Pfam; PF13098; Thioredoxin_2; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   SUPFAM; SSF54423; SSF54423; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q3Z4I9.
DR   SWISS-2DPAGE; Q3Z4I9.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002529};
KW   Periplasm {ECO:0000256|RuleBase:RU364038};
KW   Redox-active center {ECO:0000256|RuleBase:RU364038};
KW   Signal {ECO:0000256|RuleBase:RU364038}.
FT   SIGNAL        1     17       {ECO:0000256|RuleBase:RU364038}.
FT   CHAIN        18    252       Thiol:disulfide interchange protein.
FT                                {ECO:0000256|RuleBase:RU364038}.
FT                                /FTId=PRO_5010007035.
FT   DOMAIN      115    241       Thioredoxin-like_fold. {ECO:0000259|Pfam:
FT                                PF13098}.
SQ   SEQUENCE   252 AA;  27962 MW;  81CEB053329AD962 CRC64;
     MLKKILLLAL LPAIAFAEEL PSPVKAIEKQ GITIIKTFDA PGGMKGYLGK YQDMGVTIYL
     TPDGKHAISG YMYNEKGENL SNTLIEKEIY APAGREMWQR MEQSHWILDG KKDAPVIVYV
     FADPFCPYCK QFWQQARPWV DSGKVQLRTL LVGVIKPESP ATAAAILASK DPAKTWQQYE
     ASGGKLKLNV PANVSTEQMK VLSDNEKLMD DLGANVTPAI YYMSKENTLQ QAVGLPDQKT
     LNIIMGVMTP TY
//

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