UniProt Accession

 YCDX_ECOLI; P75914 

Genbank Protein ID

 U00096; AP009048 

Genbank Nucleotide ID

 AAC74118.1; BAA35815.1 

Protein Name

 Probable phosphatase YcdX 

Protein Synonyms/Alias

  

Gene Name

 ycdX 

Gene Synonyms/Alias

 b1034; JW1017 

Created Date

 July 27, 2013 

Organism

 Escherichia coli (strain K12) 

NCBI Taxa ID

 83333 

Lysine Modification

Position	Peptide	Type	References
77	RGIEANIKNVDGEID	acetylation	[1]
88	GEIDCSGKMFDSLDL	acetylation	[2]
136	ISHPGNPKYEIDVKA	acetylation	[1]
150	AVAEAAAKHQVALEI	acetylation	[1, 2]

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

 Hydrolyzes p-nitrophenyl phosphate (pNPP) in vitro. Involved in the swarming motility process. 

Sequence Annotation

 METAL 7 7 Zinc 1.
 METAL 9 9 Zinc 1.
 METAL 15 15 Zinc 2.
 METAL 40 40 Zinc 2.
 METAL 73 73 Zinc 1.
 METAL 73 73 Zinc 3.
 METAL 101 101 Zinc 3.
 METAL 131 131 Zinc 3.
 METAL 192 192 Zinc 1.
 METAL 194 194 Zinc 2.  

Keyword

 3D-structure; Complete proteome; Hydrolase; Metal-binding; Reference proteome; Zinc. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 245 AA 

Protein Sequence

Gene Ontology

 GO:0003677; F:DNA binding; IEA:InterPro.
 GO:0003887; F:DNA-directed DNA polymerase activity; IEA:InterPro.
 GO:0016791; F:phosphatase activity; IEA:HAMAP.
 GO:0042578; F:phosphoric ester hydrolase activity; IDA:EcoCyc.
 GO:0008270; F:zinc ion binding; IDA:EcoCyc.
 GO:0071978; P:bacterial-type flagellar swarming motility; IMP:EcoCyc.
 GO:0016311; P:dephosphorylation; IEA:GOC.
 GO:0006260; P:DNA replication; IEA:InterPro. 

Interpro

 IPR023710; Phosphatase_YcdX_put.
 IPR004013; PHP_C.
 IPR003141; Pol/His_phosphatase_N.
 IPR016195; Pol/histidinol_Pase-like. 

Pfam

 PF02811; PHP 

SMART

 SM00481; POLIIIAc 

PROSITE

  

PRINTS