DSBG_ECOLI
ID DSBG_ECOLI Reviewed; 248 AA.
AC P77202;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Thiol:disulfide interchange protein DsbG;
DE Flags: Precursor;
GN Name=dsbG; Synonyms=ybdP; OrderedLocusNames=b0604, JW0597;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE,
RP CHARACTERIZATION, AND MUTAGENESIS.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=9383195; DOI=10.1046/j.1365-2958.1997.5581925.x;
RA Andersen C.L., Matthey-Dupraz A., Missiakas D., Raina S.;
RT "A new Escherichia coli gene, dsbG, encodes a periplasmic protein involved
RT in disulphide bond formation, required for recycling DsbA/DsbB and DsbC
RT redox proteins.";
RL Mol. Microbiol. 26:121-132(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP PROTEIN SEQUENCE OF 18-22.
RC STRAIN=BL21-DE3;
RX PubMed=9654144; DOI=10.1016/s0014-5793(98)00539-0;
RA van Straaten M., Missiakas D., Raina S., Darby N.J.;
RT "The functional properties of DsbG, a thiol-disulfide oxidoreductase from
RT the periplasm of Escherichia coli.";
RL FEBS Lett. 428:255-258(1998).
RN [7]
RP CHARACTERIZATION.
RC STRAIN=BL21-DE3;
RX PubMed=10075670; DOI=10.1074/jbc.274.12.7784;
RA Bessette P.H., Cotto J.J., Gilbert H.F., Georgiou G.;
RT "In vivo and in vitro function of the Escherichia coli periplasmic cysteine
RT oxidoreductase DsbG.";
RL J. Biol. Chem. 274:7784-7792(1999).
RN [8]
RP CHARACTERIZATION, AND MUTAGENESIS OF CYS-126 AND CYS-129.
RC STRAIN=BL21-DE3;
RX PubMed=10788443; DOI=10.1074/jbc.275.18.13349;
RA Shao F., Bader M.W., Jakob U., Bardwell J.C.A.;
RT "DsbG, a protein disulfide isomerase with chaperone activity.";
RL J. Biol. Chem. 275:13349-13352(2000).
RN [9]
RP FUNCTION, INTERACTION WITH ERFK; YBIS AND YNHG, MUTAGENESIS OF CYS-129, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MC1000 / ATCC 39531;
RX PubMed=19965429; DOI=10.1126/science.1179557;
RA Depuydt M., Leonard S.E., Vertommen D., Denoncin K., Morsomme P., Wahni K.,
RA Messens J., Carroll K.S., Collet J.F.;
RT "A periplasmic reducing system protects single cysteine residues from
RT oxidation.";
RL Science 326:1109-1111(2009).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 18-248, AND DISULFIDE BOND.
RX PubMed=15184683; DOI=10.1073/pnas.0402769101;
RA Heras B., Edeling M.A., Schirra H.J., Raina S., Martin J.L.;
RT "Crystal structures of the DsbG disulfide isomerase reveal an unstable
RT disulfide.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:8876-8881(2004).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 19-89, AND SUBUNIT.
RX PubMed=17372350; DOI=10.1107/s0907444907003320;
RA Yeh S.-M., Koon N., Squire C., Metcalf P.;
RT "Structures of the dimerization domains of the Escherichia coli disulfide-
RT bond isomerase enzymes DsbC and DsbG.";
RL Acta Crystallogr. D 63:465-471(2007).
CC -!- FUNCTION: Involved in disulfide bond formation. DsbG and DsbC are part
CC of a periplasmic reducing system that controls the level of cysteine
CC sulfenylation, and provides reducing equivalents to rescue oxidatively
CC damaged secreted proteins such as ErfK, YbiS and YnhG. Probably also
CC functions as a disulfide isomerase with a narrower substrate
CC specificity than DsbC. DsbG is maintained in a reduced state by DsbD.
CC Displays chaperone activity in both redox states in vitro.
CC {ECO:0000269|PubMed:19965429}.
CC -!- SUBUNIT: Homodimer. Interacts with ErfK, YbiS and YnhG.
CC {ECO:0000269|PubMed:17372350, ECO:0000269|PubMed:19965429}.
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:19965429}.
CC -!- SIMILARITY: Belongs to the thioredoxin family. DsbC subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB40805.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF000956; AAC45785.1; -; Genomic_DNA.
DR EMBL; U82598; AAB40805.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC73705.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA35234.2; -; Genomic_DNA.
DR PIR; B64794; B64794.
DR RefSeq; NP_415137.2; NC_000913.3.
DR RefSeq; WP_000913829.1; NZ_SSZK01000032.1.
DR PDB; 1V57; X-ray; 2.00 A; A/B=18-248.
DR PDB; 1V58; X-ray; 1.70 A; A/B=18-248.
DR PDB; 2H0G; X-ray; 2.30 A; A/B=18-248.
DR PDB; 2H0H; X-ray; 1.80 A; A/B=18-248.
DR PDB; 2H0I; X-ray; 2.40 A; A/B=18-248.
DR PDB; 2IY2; X-ray; 1.90 A; A/B=19-89.
DR PDB; 5G1K; X-ray; 1.96 A; A/B=1-248.
DR PDB; 5G1L; X-ray; 1.70 A; A/B=1-248.
DR PDBsum; 1V57; -.
DR PDBsum; 1V58; -.
DR PDBsum; 2H0G; -.
DR PDBsum; 2H0H; -.
DR PDBsum; 2H0I; -.
DR PDBsum; 2IY2; -.
DR PDBsum; 5G1K; -.
DR PDBsum; 5G1L; -.
DR AlphaFoldDB; P77202; -.
DR SMR; P77202; -.
DR BioGRID; 4260900; 174.
DR DIP; DIP-9478N; -.
DR IntAct; P77202; 11.
DR STRING; 511145.b0604; -.
DR jPOST; P77202; -.
DR PaxDb; P77202; -.
DR PRIDE; P77202; -.
DR EnsemblBacteria; AAC73705; AAC73705; b0604.
DR EnsemblBacteria; BAA35234; BAA35234; BAA35234.
DR GeneID; 945224; -.
DR KEGG; ecj:JW0597; -.
DR KEGG; eco:b0604; -.
DR PATRIC; fig|1411691.4.peg.1664; -.
DR EchoBASE; EB3306; -.
DR eggNOG; COG1651; Bacteria.
DR HOGENOM; CLU_080090_0_0_6; -.
DR InParanoid; P77202; -.
DR OMA; CPYCNMF; -.
DR PhylomeDB; P77202; -.
DR BioCyc; EcoCyc:DSBG-MON; -.
DR BioCyc; MetaCyc:DSBG-MON; -.
DR EvolutionaryTrace; P77202; -.
DR PRO; PR:P77202; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR GO; GO:0003756; F:protein disulfide isomerase activity; IMP:EcoliWiki.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IDA:EcoCyc.
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 1: Evidence at protein level;
KW 3D-structure; Chaperone; Direct protein sequencing; Disulfide bond;
KW Periplasm; Redox-active center; Reference proteome; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000269|PubMed:9654144"
FT CHAIN 18..248
FT /note="Thiol:disulfide interchange protein DsbG"
FT /id="PRO_0000034278"
FT DISULFID 126..129
FT /note="Redox-active"
FT /evidence="ECO:0000269|PubMed:15184683"
FT MUTAGEN 126
FT /note="C->A: Complete loss of redox activity."
FT /evidence="ECO:0000269|PubMed:10788443"
FT MUTAGEN 126
FT /note="C->S: No loss of chaperone activity; when associated
FT with S-129."
FT /evidence="ECO:0000269|PubMed:10788443"
FT MUTAGEN 129
FT /note="C->A: Partial loss of redox activity. Traps the
FT protein in complex with ErfK, YbiS and YnhG."
FT /evidence="ECO:0000269|PubMed:10788443,
FT ECO:0000269|PubMed:19965429"
FT MUTAGEN 129
FT /note="C->S: No loss of chaperone activity; when associated
FT with S-126."
FT /evidence="ECO:0000269|PubMed:10788443,
FT ECO:0000269|PubMed:19965429"
FT HELIX 22..28
FT /evidence="ECO:0007829|PDB:1V58"
FT TURN 29..31
FT /evidence="ECO:0007829|PDB:1V58"
FT STRAND 32..39
FT /evidence="ECO:0007829|PDB:1V58"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:2H0G"
FT STRAND 45..51
FT /evidence="ECO:0007829|PDB:1V58"
FT STRAND 54..60
FT /evidence="ECO:0007829|PDB:1V58"
FT STRAND 67..70
FT /evidence="ECO:0007829|PDB:1V58"
FT HELIX 80..88
FT /evidence="ECO:0007829|PDB:1V58"
FT HELIX 92..94
FT /evidence="ECO:0007829|PDB:1V58"
FT HELIX 95..102
FT /evidence="ECO:0007829|PDB:1V58"
FT STRAND 107..110
FT /evidence="ECO:0007829|PDB:1V58"
FT STRAND 115..122
FT /evidence="ECO:0007829|PDB:1V58"
FT HELIX 127..141
FT /evidence="ECO:0007829|PDB:1V58"
FT STRAND 144..151
FT /evidence="ECO:0007829|PDB:1V58"
FT HELIX 159..168
FT /evidence="ECO:0007829|PDB:1V58"
FT STRAND 169..171
FT /evidence="ECO:0007829|PDB:1V58"
FT HELIX 172..181
FT /evidence="ECO:0007829|PDB:1V58"
FT TURN 182..184
FT /evidence="ECO:0007829|PDB:1V58"
FT HELIX 196..212
FT /evidence="ECO:0007829|PDB:1V58"
FT STRAND 219..224
FT /evidence="ECO:0007829|PDB:1V58"
FT TURN 225..227
FT /evidence="ECO:0007829|PDB:1V58"
FT STRAND 228..235
FT /evidence="ECO:0007829|PDB:1V58"
FT HELIX 238..244
FT /evidence="ECO:0007829|PDB:1V58"
SQ SEQUENCE 248 AA; 27495 MW; 73D57BF7DBF52A06 CRC64;
MLKKILLLAL LPAIAFAEEL PAPVKAIEKQ GITIIKTFDA PGGMKGYLGK YQDMGVTIYL
TPDGKHAISG YMYNEKGENL SNTLIEKEIY APAGREMWQR MEQSHWLLDG KKDAPVIVYV
FADPFCPYCK QFWQQARPWV DSGKVQLRTL LVGVIKPESP ATAAAILASK DPAKTWQQYE
ASGGKLKLNV PANVSTEQMK VLSDNEKLMD DLGANVTPAI YYMSKENTLQ QAVGLPDQKT
LNIIMGNK
