UniProt Accession

 HCHA_ECOLI; P31658; P76338 

Genbank Protein ID

 U00096; AP009048 

Genbank Nucleotide ID

 AAC75033.1; BAA15794.1 

Protein Name

 Molecular chaperone Hsp31 and glyoxalase 3 

Protein Synonyms/Alias

 Aminopeptidase HchA; D-lactate dehydratase; Glyoxalase III; Holdase; Holding molecular chaperone 

Gene Name

 hchA 

Gene Synonyms/Alias

 yedU; yzzC; b1967; JW1950 

Created Date

 July 27, 2013 

Organism

 Escherichia coli (strain K12) 

NCBI Taxa ID

 83333 

Lysine Modification

Position	Peptide	Type	References
43	LDGVDYPKPYRGKHK	acetylation	[1]
112	EYWAMPHKDEKVMPF	acetylation	[1, 2]
115	AMPHKDEKVMPFFEQ	acetylation	[1]
124	MPFFEQHKSLFRNPK	acetylation	[1]
236	WYFGEELKKMGMNII	acetylation	[1]
237	YFGEELKKMGMNIIN	acetylation	[2]
256	GRVHKDRKLLTGDSP	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]
 [2] 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

 Functions as a holding molecular chaperone (holdase) which stabilizes unfolding intermediates and rapidly releases them in an active form once stress has abated. Plays an important role in protecting cells from severe heat shock and starvation, as well as in acid resistance of stationary-phase cells. It uses temperature-induced exposure of structured hydrophobic domains to capture and stabilizes early unfolding and denatured protein intermediates under severe thermal stress. Catalyzes the conversion of methylglyoxal (MG) to D-lactate in a single glutathione (GSH)-independent step. It can also use phenylglyoxal as substrate. Glyoxalase activity protects cells against dicarbonyl stress. Displays an aminopeptidase activity that is specific against peptide substrates with alanine or basic amino acids (lysine, arginine) at N-terminus. 

Sequence Annotation

 ACT_SITE 185 185 Probable.
 ACT_SITE 186 186 Probable.
 ACT_SITE 214 214 Probable.
 METAL 86 86 Zinc.
 METAL 91 91 Zinc.
 METAL 123 123 Zinc.  

Keyword

 3D-structure; Chaperone; Complete proteome; Cytoplasm; Direct protein sequencing; Hydrolase; Lyase; Metal-binding; Reference proteome; Stress response; Zinc. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 283 AA 

Protein Sequence

Gene Ontology

 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0019172; F:glyoxalase III activity; IDA:EcoCyc.
 GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
 GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
 GO:0008270; F:zinc ion binding; IEA:HAMAP.
 GO:0019243; P:methylglyoxal catabolic process to D-lactate; IMP:EcoCyc.
 GO:0042026; P:protein refolding; IEA:HAMAP.
 GO:0010447; P:response to acidity; IMP:EcoCyc.
 GO:0051595; P:response to methylglyoxal; IMP:EcoCyc.
 GO:0006950; P:response to stress; IEA:UniProtKB-KW. 

Interpro

 IPR017283; Hsp31_and_glyoxalase_3.
 IPR002818; ThiJ/PfpI. 

Pfam

 PF01965; DJ-1_PfpI 

SMART

  

PROSITE

  

PRINTS