CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-010297
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Thiol:disulfide interchange protein DsbG 
Protein Synonyms/Alias
  
Gene Name
 dsbG 
Gene Synonyms/Alias
 ybdP; b0604; JW0597 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
185QYEASGGKLKLNVPAacetylation[1]
Reference
 [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli.
 Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C.
 Mol Cell. 2013 Jul 25;51(2):265-72. [PMID: 23830618
Functional Description
 Involved in disulfide bond formation. DsbG and DsbC are part of a periplasmic reducing system that controls the level of cysteine sulfenylation, and provides reducing equivalents to rescue oxidatively damaged secreted proteins such as ErfK, YbiS and YnhG. Probably also functions as a disulfide isomerase with a narrower substrate specificity than DsbC. DsbG is maintained in a reduced state by DsbD. Displays chaperone activity in both redox states in vitro. 
Sequence Annotation
 DISULFID 126 129 Redox-active.  
Keyword
 3D-structure; Chaperone; Complete proteome; Direct protein sequencing; Disulfide bond; Periplasm; Redox-active center; Reference proteome; Signal. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 248 AA 
Protein Sequence
MLKKILLLAL LPAIAFAEEL PAPVKAIEKQ GITIIKTFDA PGGMKGYLGK YQDMGVTIYL 60
TPDGKHAISG YMYNEKGENL SNTLIEKEIY APAGREMWQR MEQSHWLLDG KKDAPVIVYV 120
FADPFCPYCK QFWQQARPWV DSGKVQLRTL LVGVIKPESP ATAAAILASK DPAKTWQQYE 180
ASGGKLKLNV PANVSTEQMK VLSDNEKLMD DLGANVTPAI YYMSKENTLQ QAVGLPDQKT 240
LNIIMGNK 248 
Gene Ontology
 GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
 GO:0003756; F:protein disulfide isomerase activity; IMP:EcoliWiki.
 GO:0015035; F:protein disulfide oxidoreductase activity; IMP:EcoCyc. 
Interpro
 IPR018950; DiS-bond_isomerase_DsbC/G_N.
 IPR012336; Thioredoxin-like_fold. 
Pfam
 PF13098; Thioredoxin_2 
SMART
  
PROSITE
 PS00194; THIOREDOXIN_1 
PRINTS