CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-003062
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Thiol peroxidase 
Protein Synonyms/Alias
 Scavengase P20 
Gene Name
 tpx 
Gene Synonyms/Alias
 yzzJ; b1324; JW1317 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
24SIPQAGSKAQTFTLVacetylation[1]
33QTFTLVAKDLSDVTLacetylation[1, 2, 3]
46TLGQFAGKRKVLNIFacetylation[1, 3]
48GQFAGKRKVLNIFPSacetylation[1]
128AIADGPLKGLAARAVacetylation[1, 3]
Reference
 [1] 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]
 [2] The diversity of lysine-acetylated proteins in Escherichia coli.
 Yu BJ, Kim JA, Moon JH, Ryu SE, Pan JG.
 J Microbiol Biotechnol. 2008 Sep;18(9):1529-36. [PMID: 18852508]
 [3] 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
 Has antioxidant activity. Could remove peroxides or H(2)O(2) within the catalase- and peroxidase-deficient periplasmic space. 
Sequence Annotation
 DOMAIN 19 168 Thioredoxin.  
Keyword
 3D-structure; Antioxidant; Complete proteome; Direct protein sequencing; Oxidoreductase; Periplasm; Peroxidase; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 168 AA 
Protein Sequence
MSQTVHFQGN PVTVANSIPQ AGSKAQTFTL VAKDLSDVTL GQFAGKRKVL NIFPSIDTGV 60
CAASVRKFNQ LATEIDNTVV LCISADLPFA QSRFCGAEGL NNVITLSTFR NAEFLQAYGV 120
AIADGPLKGL AARAVVVIDE NDNVIFSQLV DEITTEPDYE AALAVLKA 168 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:EcoCyc.
 GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
 GO:0032843; F:hydroperoxide reductase activity; IDA:EcoCyc.
 GO:0008379; F:thioredoxin peroxidase activity; IDA:EcoCyc.
 GO:0045454; P:cell redox homeostasis; IEA:HAMAP.
 GO:0034599; P:cellular response to oxidative stress; IMP:EcoCyc. 
Interpro
 IPR018219; Antioxidant_Tpx_CS.
 IPR002065; Put_TPX.
 IPR013740; Redoxin.
 IPR012336; Thioredoxin-like_fold. 
Pfam
 PF08534; Redoxin 
SMART
  
PROSITE
 PS51352; THIOREDOXIN_2
 PS01265; TPX 
PRINTS