CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-007140
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Non-canonical purine NTP phosphatase 
Protein Synonyms/Alias
 Inosine triphosphatase; ITPase; Non-standard purine NTP phosphatase; Nucleoside-triphosphate phosphatase; NTPase; Xanthosine triphosphatase; XTPase 
Gene Name
 yjjX 
Gene Synonyms/Alias
 b4394; JW5801 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
113LPAVILEKVREGEALacetylation[1]
136GIDEIGRKEGAIGVFacetylation[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
 Phosphatase that hydrolyzes non-canonical purine nucleotides such as XTP and ITP to their respective diphosphate derivatives. Probably excludes non-canonical purines from DNA precursor pool, thus preventing their incorporation into DNA and avoiding chromosomal lesions. ITP is the best substrate, followed by XTP, GDP or dITP. Also implicated in the resistance against the thiamine metabolism inhibitors bacimethrin and CF3-HMP. 
Sequence Annotation
 REGION 8 13 Substrate binding.
 REGION 68 69 Substrate binding (By similarity).
 METAL 38 38 Manganese or magnesium (By similarity).
 METAL 68 68 Manganese or magnesium (By similarity).  
Keyword
 3D-structure; Antibiotic resistance; Complete proteome; Hydrolase; Magnesium; Manganese; Metal-binding; Nucleotide metabolism; Nucleotide-binding; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 170 AA 
Protein Sequence
MHQVVCATTN PAKIQAILQA FHEIFGEGSC HIASVAVESG VPEQPFGSEE TRAGARNRVA 60
NARRLLPEAD FWVAIEAGID GDSTFSWVVI ENASQRGEAR SATLPLPAVI LEKVREGEAL 120
GPVMSRYTGI DEIGRKEGAI GVFTAGKLTR ASVYHQAVIL ALSPFHNAVY 170 
Gene Ontology
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0017111; F:nucleoside-triphosphatase activity; IDA:EcoCyc.
 GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
 GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
 GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
 GO:0006772; P:thiamine metabolic process; EXP:EcoliWiki. 
Interpro
 IPR002786; Non_canon_purine_NTPase.
 IPR026533; NTPase/PRRC1. 
Pfam
 PF01931; NTPase_I-T 
SMART
  
PROSITE
  
PRINTS