CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-003467
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Thiol:disulfide interchange protein DsbC 
Protein Synonyms/Alias
  
Gene Name
 dsbC 
Gene Synonyms/Alias
 xprA; b2893; JW2861 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
85APVNVTNKMLLKQLNacetylation[1]
89VTNKMLLKQLNALEKacetylation[1]
231EFLDEHQKMTSGK**acetylation[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
 Acts as a disulfide isomerase, interacting with incorrectly folded proteins to correct non-native disulfide bonds. 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. Acts by transferring its disulfide bond to other proteins and is reduced in the process. DsbC is reoxidized by DsbD. 
Sequence Annotation
 DOMAIN 36 231 Thioredoxin.
 DISULFID 118 121 Redox-active.
 DISULFID 161 183  
Keyword
 3D-structure; Complete proteome; Direct protein sequencing; Disulfide bond; Periplasm; Redox-active center; Reference proteome; Signal. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 236 AA 
Protein Sequence
MKKGFMLFTL LAAFSGFAQA DDAAIQQTLA KMGIKSSDIQ PAPVAGMKTV LTNSGVLYIT 60
DDGKHIIQGP MYDVSGTAPV NVTNKMLLKQ LNALEKEMIV YKAPQEKHVI TVFTDITCGY 120
CHKLHEQMAD YNALGITVRY LAFPRQGLDS DAEKEMKAIW CAKDKNKAFD DVMAGKSVAP 180
ASCDVDIADH YALGVQLGVS GTPAVVLSNG TLVPGYQPPK EMKEFLDEHQ KMTSGK 236 
Gene Ontology
 GO:0030288; C:outer membrane-bounded periplasmic space; NAS:EcoliWiki.
 GO:0003756; F:protein disulfide isomerase activity; IDA:EcoCyc.
 GO:0015035; F:protein disulfide oxidoreductase activity; IMP:UniProtKB.
 GO:0045454; P:cell redox homeostasis; IEA:InterPro. 
Interpro
 IPR018950; DiS-bond_isomerase_DsbC/G_N.
 IPR009094; DiS-bond_isomerase_DsbC_N.
 IPR012336; Thioredoxin-like_fold.
 IPR017937; Thioredoxin_CS. 
Pfam
 PF10411; DsbC_N
 PF13098; Thioredoxin_2 
SMART
  
PROSITE
 PS00194; THIOREDOXIN_1
 PS51352; THIOREDOXIN_2 
PRINTS