DSBG_ECO57
ID DSBG_ECO57 Reviewed; 248 AA.
AC P58320;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 18-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Thiol:disulfide interchange protein DsbG;
DE Flags: Precursor;
GN Name=dsbG; OrderedLocusNames=Z0748, ECs0643;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
CC -!- FUNCTION: Involved in disulfide bond formation. Functions probably as a
CC disulfide isomerase with a narrower substrate specificity than DsbC.
CC DsbG is maintained in a reduced state by DsbD. In vitro, displays
CC chaperone activity in both redox states (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the thioredoxin family. DsbC subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG54939.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB34066.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE005174; AAG54939.1; ALT_INIT; Genomic_DNA.
DR EMBL; BA000007; BAB34066.1; ALT_INIT; Genomic_DNA.
DR PIR; C90709; C90709.
DR PIR; G85559; G85559.
DR RefSeq; NP_308670.3; NC_002695.1.
DR RefSeq; WP_001301891.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P58320; -.
DR SMR; P58320; -.
DR STRING; 155864.EDL933_0676; -.
DR EnsemblBacteria; AAG54939; AAG54939; Z0748.
DR EnsemblBacteria; BAB34066; BAB34066; ECs_0643.
DR GeneID; 917002; -.
DR KEGG; ece:Z0748; -.
DR KEGG; ecs:ECs_0643; -.
DR PATRIC; fig|386585.9.peg.754; -.
DR eggNOG; COG1651; Bacteria.
DR HOGENOM; CLU_080090_0_0_6; -.
DR OMA; CPYCNMF; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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;
KW Chaperone; Disulfide bond; Periplasm; Redox-active center;
KW Reference proteome; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000250"
FT CHAIN 18..248
FT /note="Thiol:disulfide interchange protein DsbG"
FT /id="PRO_0000034279"
FT DISULFID 126..129
FT /note="Redox-active"
FT /evidence="ECO:0000250"
SQ SEQUENCE 248 AA; 27496 MW; C7C42EB3DBF537DB CRC64;
MLKKILLLAL LPAIAFAEEL PAPVKAIEKQ GITIIKTFDA PGGMKGYLGK YQDMGVTIYL
TPDGKHAISG YMYNEKGENL SNTLIEKEIY APAGREMWQR MEQSHWLLDG KKDAPVIVYV
FADPFCPYCK QFWQQARPWV DSGKVQLRTL LVGVIKPESP ATAAAILASK DPAKTWQEYE
ASGGKLKLNV PANVSTEQMK VLSDNEKLMD DLGANVTPAI YYMSKENTLQ QAVGLPDQKT
LNIIMGNK