DSBC_ECOLI
ID DSBC_ECOLI Reviewed; 236 AA.
AC P0AEG6; P21892; Q2M9U8;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Thiol:disulfide interchange protein DsbC;
DE Flags: Precursor;
GN Name=dsbC; Synonyms=xprA; OrderedLocusNames=b2893, JW2861;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1987126; DOI=10.1128/jb.173.1.353-364.1991;
RA Lovett S.T., Kolodner R.D.;
RT "Nucleotide sequence of the Escherichia coli recJ chromosomal region and
RT construction of recJ-overexpression plasmids.";
RL J. Bacteriol. 173:353-364(1991).
RN [2]
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 [3]
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 [4]
RP PROTEIN SEQUENCE OF 21-32.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [5]
RP CHARACTERIZATION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF CYS-118;
RP CYS-121; CYS-161 AND CYS-183.
RX PubMed=8168498; DOI=10.1002/j.1460-2075.1994.tb06471.x;
RA Missiakas D., Georgopoulos C., Raina S.;
RT "The Escherichia coli dsbC (xprA) gene encodes a periplasmic protein
RT involved in disulfide bond formation.";
RL EMBO J. 13:2013-2020(1994).
RN [6]
RP CHARACTERIZATION, MUTAGENESIS, AND SEQUENCE REVISION TO 219.
RX PubMed=7536035; DOI=10.1021/bi00015a019;
RA Zapun A., Missiakas D., Raina S., Creighton T.E.;
RT "Structural and functional characterization of DsbC, a protein involved in
RT disulfide bond formation in Escherichia coli.";
RL Biochemistry 34:5075-5089(1995).
RN [7]
RP CHARACTERIZATION.
RX PubMed=8168497; DOI=10.1002/j.1460-2075.1994.tb06470.x;
RA Shevchik V.E., Condemine G., Robert-Baudouy J.;
RT "Characterization of DsbC, a periplasmic protein of Erwinia chrysanthemi
RT and Escherichia coli with disulfide isomerase activity.";
RL EMBO J. 13:2007-2012(1994).
RN [8]
RP CHARACTERIZATION.
RX PubMed=9254601; DOI=10.1021/bi9707739;
RA Joly J.C., Swartz J.R.;
RT "In vitro and in vivo redox states of the Escherichia coli periplasmic
RT oxidoreductases DsbA and DsbC.";
RL Biochemistry 36:10067-10072(1997).
RN [9]
RP FUNCTION.
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 (1.9 ANGSTROMS), AND DISULFIDE BONDS.
RX PubMed=10700276; DOI=10.1038/73295;
RA McCarthy A.A., Haebel P.W., Torronen A., Rybin V., Baker E.N., Metcalf P.;
RT "Crystal structure of the protein disulfide bond isomerase, DsbC, from
RT Escherichia coli.";
RL Nat. Struct. Biol. 7:196-199(2000).
CC -!- FUNCTION: Acts as a disulfide isomerase, interacting with incorrectly
CC folded proteins to correct non-native disulfide bonds. DsbG and DsbC
CC are part of a periplasmic reducing system that controls the level of
CC cysteine sulfenylation, and provides reducing equivalents to rescue
CC oxidatively damaged secreted proteins. Acts by transferring its
CC disulfide bond to other proteins and is reduced in the process. DsbC is
CC reoxidized by DsbD. {ECO:0000269|PubMed:19965429}.
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:8168498}.
CC -!- SIMILARITY: Belongs to the thioredoxin family. DsbC subfamily.
CC {ECO:0000305}.
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DR EMBL; M54884; AAA62788.1; -; Genomic_DNA.
DR EMBL; U28375; AAA83074.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75931.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76958.1; -; Genomic_DNA.
DR PIR; E65073; E65073.
DR RefSeq; NP_417369.1; NC_000913.3.
DR RefSeq; WP_000715214.1; NZ_STEB01000001.1.
DR PDB; 1EEJ; X-ray; 1.90 A; A/B=21-236.
DR PDB; 1G0T; X-ray; 2.60 A; A/B=21-236.
DR PDB; 1JZD; X-ray; 2.30 A; A/B=20-236.
DR PDB; 1JZO; X-ray; 1.92 A; A/B=21-236.
DR PDB; 1TJD; X-ray; 2.50 A; A=21-236.
DR PDB; 2IYJ; X-ray; 2.00 A; A/B=19-91.
DR PDBsum; 1EEJ; -.
DR PDBsum; 1G0T; -.
DR PDBsum; 1JZD; -.
DR PDBsum; 1JZO; -.
DR PDBsum; 1TJD; -.
DR PDBsum; 2IYJ; -.
DR AlphaFoldDB; P0AEG6; -.
DR SMR; P0AEG6; -.
DR BioGRID; 4261304; 500.
DR DIP; DIP-35818N; -.
DR IntAct; P0AEG6; 9.
DR STRING; 511145.b2893; -.
DR DrugBank; DB03814; 2-(N-morpholino)ethanesulfonic acid.
DR jPOST; P0AEG6; -.
DR PaxDb; P0AEG6; -.
DR PRIDE; P0AEG6; -.
DR EnsemblBacteria; AAC75931; AAC75931; b2893.
DR EnsemblBacteria; BAE76958; BAE76958; BAE76958.
DR GeneID; 66673233; -.
DR GeneID; 947363; -.
DR KEGG; ecj:JW2861; -.
DR KEGG; eco:b2893; -.
DR PATRIC; fig|1411691.4.peg.3840; -.
DR EchoBASE; EB1063; -.
DR eggNOG; COG1651; Bacteria.
DR HOGENOM; CLU_083593_0_0_6; -.
DR InParanoid; P0AEG6; -.
DR OMA; QMIVYKA; -.
DR PhylomeDB; P0AEG6; -.
DR BioCyc; EcoCyc:DSBC-MON; -.
DR BioCyc; MetaCyc:DSBC-MON; -.
DR EvolutionaryTrace; P0AEG6; -.
DR PRO; PR:P0AEG6; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR GO; GO:0042597; C:periplasmic space; IDA:EcoliWiki.
DR GO; GO:0003756; F:protein disulfide isomerase activity; IDA:EcoCyc.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IMP:UniProtKB.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IDA:EcoCyc.
DR GO; GO:0046688; P:response to copper ion; IMP: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; IPR018950; DiS-bond_isomerase_DsbC/G_N.
DR InterPro; IPR009094; DiS-bond_isomerase_DsbC/G_N_sf.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF10411; DsbC_N; 1.
DR Pfam; PF13098; Thioredoxin_2; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR SUPFAM; SSF54423; SSF54423; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Periplasm;
KW Redox-active center; Reference proteome; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000269|PubMed:9298646"
FT CHAIN 21..236
FT /note="Thiol:disulfide interchange protein DsbC"
FT /id="PRO_0000034273"
FT DOMAIN 36..231
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DISULFID 118..121
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691,
FT ECO:0000269|PubMed:10700276"
FT DISULFID 161..183
FT /evidence="ECO:0000269|PubMed:10700276"
FT MUTAGEN 118
FT /note="C->T,A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:8168498"
FT MUTAGEN 121
FT /note="C->A: Partial loss of activity."
FT /evidence="ECO:0000269|PubMed:8168498"
FT MUTAGEN 121
FT /note="C->V: Loss of activity."
FT /evidence="ECO:0000269|PubMed:8168498"
FT MUTAGEN 161
FT /note="C->S: Destabilization of protein."
FT /evidence="ECO:0000269|PubMed:8168498"
FT MUTAGEN 183
FT /note="C->L: Destabilization of protein."
FT /evidence="ECO:0000269|PubMed:8168498"
FT CONFLICT 219
FT /note="Missing (in Ref. 1; AAA62788)"
FT /evidence="ECO:0000305"
FT HELIX 22..31
FT /evidence="ECO:0007829|PDB:1EEJ"
FT STRAND 36..41
FT /evidence="ECO:0007829|PDB:1EEJ"
FT STRAND 47..52
FT /evidence="ECO:0007829|PDB:1EEJ"
FT STRAND 55..60
FT /evidence="ECO:0007829|PDB:1EEJ"
FT STRAND 65..69
FT /evidence="ECO:0007829|PDB:1EEJ"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:1EEJ"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:1EEJ"
FT HELIX 82..92
FT /evidence="ECO:0007829|PDB:1EEJ"
FT HELIX 93..97
FT /evidence="ECO:0007829|PDB:1EEJ"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:1EEJ"
FT STRAND 108..114
FT /evidence="ECO:0007829|PDB:1EEJ"
FT HELIX 119..125
FT /evidence="ECO:0007829|PDB:1EEJ"
FT HELIX 128..133
FT /evidence="ECO:0007829|PDB:1EEJ"
FT STRAND 136..142
FT /evidence="ECO:0007829|PDB:1EEJ"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:1EEJ"
FT HELIX 151..160
FT /evidence="ECO:0007829|PDB:1EEJ"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:1EEJ"
FT HELIX 165..173
FT /evidence="ECO:0007829|PDB:1EEJ"
FT HELIX 187..197
FT /evidence="ECO:0007829|PDB:1EEJ"
FT STRAND 201..206
FT /evidence="ECO:0007829|PDB:1EEJ"
FT STRAND 212..215
FT /evidence="ECO:0007829|PDB:1EEJ"
FT HELIX 219..234
FT /evidence="ECO:0007829|PDB:1EEJ"
SQ SEQUENCE 236 AA; 25622 MW; 69A834A666BAA6D6 CRC64;
MKKGFMLFTL LAAFSGFAQA DDAAIQQTLA KMGIKSSDIQ PAPVAGMKTV LTNSGVLYIT
DDGKHIIQGP MYDVSGTAPV NVTNKMLLKQ LNALEKEMIV YKAPQEKHVI TVFTDITCGY
CHKLHEQMAD YNALGITVRY LAFPRQGLDS DAEKEMKAIW CAKDKNKAFD DVMAGKSVAP
ASCDVDIADH YALGVQLGVS GTPAVVLSNG TLVPGYQPPK EMKEFLDEHQ KMTSGK
