CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-003441
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Class B acid phosphatase 
Protein Synonyms/Alias
 CBAP 
Gene Name
 aphA 
Gene Synonyms/Alias
 napA; yjbP; b4055; JW4015 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
97PESEDYLKNPVFWEKacetylation[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
 Dephosphorylates several organic phosphate monoesters including 3'- and 5'-nucleotides, 2'-deoxy-5'-nucleotides, pNPP, phenyl phosphate, glycerol 2-phosphate, ribose 5-phosphate, O- phospho-L-amino acids and phytic acid, showing the highest activity with aryl phosphoesters (pNPP, phenyl phosphate and O- phospho-L-tyrosine), and to a lesser extent with 3'- and 5'- nucleotides. No activity toward ATP, phosphodiesters, glycerol-1- phosphate, glucose 1-phosphate, glucose 6-phosphate, NADP, GTP or 3',5'-cAMP, ADP or ATP. Also has a phosphotransferase activity catalyzing the transfer of low-energy phosphate groups from organic phosphate monoesters to free hydroxyl groups of various organic compounds. Capable of transferring phosphate from either pNPP or UMP to adenosine or uridine. Does not exhibit nucleotide phosphomutase activity. 
Sequence Annotation
 REGION 137 138 Substrate binding.
 ACT_SITE 69 69 Nucleophile.
 ACT_SITE 71 71 Proton donor.
 METAL 69 69 Magnesium.
 METAL 71 71 Magnesium; via carbonyl oxygen.
 METAL 192 192 Magnesium.
 BINDING 177 177 Substrate.  
Keyword
 3D-structure; Complete proteome; Direct protein sequencing; Hydrolase; Magnesium; Metal-binding; Periplasm; Reference proteome; Signal. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 237 AA 
Protein Sequence
MRKITQAISA VCLLFALNSS AVALASSPSP LNPGTNVARL AEQAPIHWVS VAQIENSLAG 60
RPPMAVGFDI DDTVLFSSPG FWRGKKTFSP ESEDYLKNPV FWEKMNNGWD EFSIPKEVAR 120
QLIDMHVRRG DAIFFVTGRS PTKTETVSKT LADNFHIPAT NMNPVIFAGD KPGQNTKSQW 180
LQDKNIRIFY GDSDNDITAA RDVGARGIRI LRASNSTYKP LPQAGAFGEE VIVNSEY 237 
Gene Ontology
 GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
 GO:0003993; F:acid phosphatase activity; IEA:EC.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. 
Interpro
 IPR005519; Acid_phosphat_B.
 IPR023214; HAD-like_dom.
 IPR010025; HAD-SF_ppase_IIIB_AphA. 
Pfam
 PF03767; Acid_phosphat_B 
SMART
  
PROSITE
  
PRINTS