UniProt Accession

 IPYR_ECOLI; P0A7A9; P17288; Q2M679 

Genbank Protein ID

 M23550; U14003; U00096; AP009048 

Genbank Nucleotide ID

 AAB88583.1; AAA97123.1; AAC77183.1; BAE78227.1 

Protein Name

 Inorganic pyrophosphatase 

Protein Synonyms/Alias

 Pyrophosphate phospho-hydrolase; PPase 

Gene Name

 ppa 

Gene Synonyms/Alias

 b4226; JW4185 

Created Date

 July 27, 2013 

Organism

 Escherichia coli (strain K12) 

NCBI Taxa ID

 83333 

Lysine Modification

Position	Peptide	Type	References
10	LLNVPAGKDLPEDIY	acetylation	[1]
30	PANADPIKYEIDKES	acetylation	[1, 2]
35	PIKYEIDKESGALFV	acetylation	[2]
95	CRPVGVLKMTDEAGE	acetylation	[2]
105	DEAGEDAKLVAVPHS	acetylation	[2, 3]
113	LVAVPHSKLSKEYDH	acetylation	[2, 3]
116	VPHSKLSKEYDHIKD	acetylation	[2, 3]
122	SKEYDHIKDVNDLPE	acetylation	[1, 2, 3]
132	NDLPELLKAQIAHFF	acetylation	[2]
143	AHFFEHYKDLEKGKW	acetylation	[1, 2, 3]
147	EHYKDLEKGKWVKVE	acetylation	[2, 3]
149	YKDLEKGKWVKVEGW	acetylation	[2]
152	LEKGKWVKVEGWENA	acetylation	[2]
163	WENAEAAKAEIVASF	acetylation	[2]

Reference

 [1] 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]
 [2] 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]
 [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

  

Sequence Annotation

 METAL 66 66 Magnesium 1.
 METAL 71 71 Magnesium 1.
 METAL 71 71 Magnesium 2.
 METAL 103 103 Magnesium 1.  

Keyword

 3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing; Hydrolase; Magnesium; Metal-binding; Reference proteome. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 176 AA 

Protein Sequence

Gene Ontology

 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0016020; C:membrane; IDA:UniProtKB.
 GO:0004427; F:inorganic diphosphatase activity; IDA:EcoCyc.
 GO:0000287; F:magnesium ion binding; IDA:EcoCyc.
 GO:0050355; F:triphosphatase activity; IDA:EcoCyc.
 GO:0008270; F:zinc ion binding; IDA:EcoCyc.
 GO:0006796; P:phosphate-containing compound metabolic process; IEA:InterPro. 

Interpro

 IPR008162; Pyrophosphatase. 

Pfam

 PF00719; Pyrophosphatase 

SMART

  

PROSITE

 PS00387; PPASE 

PRINTS