UniProt Accession

 OSMC_ECOLI; P0C0L2; P23929; P77655 

Genbank Protein ID

 X57433; U00096; AP009048 

Genbank Nucleotide ID

 CAA40680.1; AAC74555.1; BAA15128.1 

Protein Name

 Peroxiredoxin OsmC 

Protein Synonyms/Alias

 Osmotically-inducible protein C 

Gene Name

 osmC 

Gene Synonyms/Alias

 b1482; JW1477 

Created Date

 July 27, 2013 

Organism

 Escherichia coli (strain K12) 

NCBI Taxa ID

 83333 

Lysine Modification

Position	Peptide	Type	References
6	**MTIHKKGQAHWEG	acetylation	[1]
16	AHWEGDIKRGKGTVS	acetylation	[1, 2, 3]
97	DAGFAITKIALKSEV	acetylation	[1]
101	AITKIALKSEVAVPG	acetylation	[1, 3]
120	TFDGIIQKAKAGCPV	acetylation	[1, 3]

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]
 [2] Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli.
 Zhang J, Sprung R, Pei J, Tan X, Kim S, Zhu H, Liu CF, Grishin NV, Zhao Y.
 Mol Cell Proteomics. 2009 Feb;8(2):215-25. [PMID: 18723842]
 [3] Comprehensive profiling of protein lysine acetylation in Escherichia coli.
 Zhang K, Zheng S, Yang JS, Chen Y, Cheng Z.
 J Proteome Res. 2013 Feb 1;12(2):844-51. [PMID: 23294111] 

Functional Description

 Preferentially metabolizes organic hydroperoxides over inorganic hydrogen peroxide. 

Sequence Annotation

 MOD_RES 16 16 N6-acetyllysine.  

Keyword

 3D-structure; Acetylation; Antioxidant; Complete proteome; Cytoplasm; Direct protein sequencing; Oxidoreductase; Peroxidase; Reference proteome. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 143 AA 

Protein Sequence

Gene Ontology

 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0004601; F:peroxidase activity; IDA:EcoCyc.
 GO:0051920; F:peroxiredoxin activity; IEA:EC.
 GO:0006979; P:response to oxidative stress; IMP:EcoCyc. 

Interpro

 IPR015946; KH_dom-like_a/b.
 IPR003718; Peroxiredoxin_OsmC-like.
 IPR019904; Peroxiredoxin_OsmC_subgr. 

Pfam

 PF02566; OsmC 

SMART

  

PROSITE

  

PRINTS