CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004286
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Xaa-Pro aminopeptidase 
Protein Synonyms/Alias
 Aminoacylproline aminopeptidase; Aminopeptidase P II; APP-II; X-Pro aminopeptidase 
Gene Name
 pepP 
Gene Synonyms/Alias
 b2908; JW2876 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
102GQDAAPEKLGVDRALacetylation[1]
282RTFPVNGKFTQAQREacetylation[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
  
Sequence Annotation
 METAL 261 261 Manganese 2.
 METAL 272 272 Manganese 1.
 METAL 272 272 Manganese 2.
 METAL 355 355 Manganese 1.
 METAL 384 384 Manganese 1.
 METAL 407 407 Manganese 1.
 METAL 407 407 Manganese 2.  
Keyword
 3D-structure; Aminopeptidase; Complete proteome; Cytoplasm; Direct protein sequencing; Hydrolase; Manganese; Metal-binding; Metalloprotease; Protease; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 441 AA 
Protein Sequence
MSEISRQEFQ RRRQALVEQM QPGSAALIFA APEVTRSADS EYPYRQNSDF WYFTGFNEPE 60
AVLVLIKSDD THNHSVLFNR VRDLTAEIWF GRRLGQDAAP EKLGVDRALA FSEINQQLYQ 120
LLNGLDVVYH AQGEYAYADV IVNSALEKLR KGSRQNLTAP ATMIDWRPVV HEMRLFKSPE 180
EIAVLRRAGE ITAMAHTRAM EKCRPGMFEY HLEGEIHHEF NRHGARYPSY NTIVGSGENG 240
CILHYTENEC EMRDGDLVLI DAGCEYKGYA GDITRTFPVN GKFTQAQREI YDIVLESLET 300
SLRLYRPGTS ILEVTGEVVR IMVSGLVKLG ILKGDVDELI AQNAHRPFFM HGLSHWLGLD 360
VHDVGVYGQD RSRILEPGMV LTVEPGLYIA PDAEVPEQYR GIGIRIEDDI VITETGNENL 420
TASVVKKPEE IEALMVAARK Q 441 
Gene Ontology
 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0004177; F:aminopeptidase activity; IDA:EcoCyc.
 GO:0030145; F:manganese ion binding; IEA:InterPro.
 GO:0008235; F:metalloexopeptidase activity; IEA:InterPro.
 GO:0009987; P:cellular process; IEA:InterPro.
 GO:0006508; P:proteolysis; IEA:UniProtKB-KW. 
Interpro
 IPR007865; Aminopep_P_N.
 IPR001714; Pept_M24_MAP.
 IPR000994; Pept_M24_structural-domain.
 IPR001131; Peptidase_M24B_aminopep-P_CS. 
Pfam
 PF05195; AMP_N
 PF00557; Peptidase_M24 
SMART
 SM01011; AMP_N 
PROSITE
 PS00491; PROLINE_PEPTIDASE 
PRINTS
 PR00599; MAPEPTIDASE.