CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005810
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Peptidase T 
Protein Synonyms/Alias
 Aminotripeptidase; Tripeptidase; Tripeptide aminopeptidase 
Gene Name
 pepT 
Gene Synonyms/Alias
 b1127; JW1113 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
33PSTEGQWKLLHLLKEacetylation[1]
88TSPDCSGKNVNPQIVacetylation[1]
158ALAVLQQKKIPHGDIacetylation[1]
177TPDEEVGKGAKHFDVacetylation[1]
180EEVGKGAKHFDVDAFacetylation[1, 2]
267FYHLASMKGTVERADacetylation[1]
285IIRDFDRKQFEARKRacetylation[1]
299RKMMEIAKKVGKGLHacetylation[1]
350CDIEPELKPIRGGTDacetylation[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]
 [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
 Cleaves the N-terminal amino acid of tripeptides (By similarity). 
Sequence Annotation
 ACT_SITE 80 80 By similarity.
 ACT_SITE 173 173 Proton acceptor (By similarity).
 METAL 78 78 Zinc 1.
 METAL 140 140 Zinc 1.
 METAL 140 140 Zinc 2.
 METAL 174 174 Zinc 2.
 METAL 196 196 Zinc 1.
 METAL 379 379 Zinc 2.  
Keyword
 3D-structure; Aminopeptidase; Complete proteome; Cytoplasm; Hydrolase; Metal-binding; Metalloprotease; Protease; Reference proteome; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 408 AA 
Protein Sequence
MDKLLERFLN YVSLDTQSKA GVRQVPSTEG QWKLLHLLKE QLEEMGLINV TLSEKGTLMA 60
TLPANVPGDI PAIGFISHVD TSPDCSGKNV NPQIVENYRG GDIALGIGDE VLSPVMFPVL 120
HQLLGQTLIT TDGKTLLGAD DKAGIAEIMT ALAVLQQKKI PHGDIRVAFT PDEEVGKGAK 180
HFDVDAFDAR WAYTVDGGGV GELEFENFNA ASVNIKIVGN NVHPGTAKGV MVNALSLAAR 240
IHAEVPADES PEMTEGYEGF YHLASMKGTV ERADMHYIIR DFDRKQFEAR KRKMMEIAKK 300
VGKGLHPDCY IELVIEDSYY NMREKVVEHP HILDIAQQAM RDCDIEPELK PIRGGTDGAQ 360
LSFMGLPCPN LFTGGYNYHG KHEFVTLEGM EKAVQVIVRI AELTAQRK 408 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
 GO:0045148; F:tripeptide aminopeptidase activity; IDA:EcoCyc.
 GO:0008270; F:zinc ion binding; IEA:HAMAP.
 GO:0006518; P:peptide metabolic process; IDA:EcoCyc.
 GO:0006508; P:proteolysis; IEA:HAMAP. 
Interpro
 IPR001261; ArgE/DapE_CS.
 IPR002933; Peptidase_M20.
 IPR011650; Peptidase_M20_dimer.
 IPR010161; Peptidase_M20B. 
Pfam
 PF07687; M20_dimer
 PF01546; Peptidase_M20 
SMART
  
PROSITE
 PS00758; ARGE_DAPE_CPG2_1
 PS00759; ARGE_DAPE_CPG2_2 
PRINTS