UniProt Accession

 PPIC_ECOLI; P0A9L5; P39159; Q2M884 

Genbank Protein ID

 S73874; M87049; U00096; AP009048 

Genbank Nucleotide ID

 AAB32054.1; AAA67578.1; AAC76780.1; BAE77522.1 

Protein Name

 Peptidyl-prolyl cis-trans isomerase C 

Protein Synonyms/Alias

 PPIase C; Par10; Parvulin; Rotamase C 

Gene Name

 ppiC 

Gene Synonyms/Alias

 parVA; b3775; JW3748 

Created Date

 July 27, 2013 

Organism

 Escherichia coli (strain K12) 

NCBI Taxa ID

 83333 

Lysine Modification

Position	Peptide	Type	References
13	AALHILVKEEKLALD	acetylation	[1]
16	HILVKEEKLALDLLE	acetylation	[1]
26	LDLLEQIKNGADFGK	acetylation	[1]
33	KNGADFGKLAKKHSI	acetylation	[1]
36	ADFGKLAKKHSICPS	acetylation	[1]
64	QMVPAFDKVVFSCPV	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

 PPIases accelerate the folding of proteins. It prefers amino acid residues with hydrophobic side chains like leucine and phenylalanine in the P1 position of the peptides substrates. 

Sequence Annotation

 DOMAIN 2 91 PpiC.  

Keyword

 3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing; Isomerase; Reference proteome; Rotamase. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 93 AA 

Protein Sequence

Gene Ontology

 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IDA:EcoCyc.
 GO:0006457; P:protein folding; IEA:UniProtKB-KW. 

Interpro

 IPR000297; PPIase_PpiC.
 IPR023058; PPIase_PpiC_CS. 

Pfam

 PF00639; Rotamase 

SMART

  

PROSITE

 PS01096; PPIC_PPIASE_1
 PS50198; PPIC_PPIASE_2 

PRINTS