CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005569
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Oligopeptidase A 
Protein Synonyms/Alias
  
Gene Name
 prlC 
Gene Synonyms/Alias
 opdA; b3498; JW3465 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
77VSHLNSVKNSPELREacetylation[1]
108GQHEGLYKAYRDLRDacetylation[1]
146LSGIGLPKEKQQRYGacetylation[1]
252DQGPNAGKWDNSKVMacetylation[1]
257AGKWDNSKVMEEILAacetylation[1]
281GFENYAFKSLATKMAacetylation[1, 2]
303DFLTDLAKRARPQGEacetylation[1]
311RARPQGEKELAQLRAacetylation[1]
361RPYFPENKAVNGLFEacetylation[1]
371NGLFEVVKRIYGITAacetylation[1]
382GITAKERKDVDVWHPacetylation[1]
535LPKELLDKMLAAKNYacetylation[1]
572FRPDQGAKILETLAEacetylation[1]
581LETLAEIKKLVAVVPacetylation[1]
660EEPMDLFKRFRGREPacetylation[1]
679MLEHYGIKG******acetylation[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
 May play a specific role in the degradation of signal peptides after they are released from precursor forms of secreted proteins. Can cleave N-acetyl-L-Ala(4). 
Sequence Annotation
 ACT_SITE 470 470 By similarity.
 METAL 469 469 Zinc; catalytic (By similarity).
 METAL 473 473 Zinc; catalytic (By similarity).
 METAL 476 476 Zinc; catalytic (By similarity).  
Keyword
 Complete proteome; Hydrolase; Metal-binding; Metalloprotease; Protease; Reference proteome; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 680 AA 
Protein Sequence
MTNPLLTPFE LPPFSKILPE HVVPAVTKAL NDCRENVERV VAQGAPYTWE NLCQPLAEVD 60
DVLGRIFSPV SHLNSVKNSP ELREAYEQTL PLLSEYSTWV GQHEGLYKAY RDLRDGDHYA 120
TLNTAQKKAV DNALRDFELS GIGLPKEKQQ RYGEIATRLS ELGNQYSNNV LDATMGWTKL 180
VTDEAELAGM PESALAAAKA QAEAKELEGY LLTLDIPSYL PVMTYCDNQA LREEMYRAYS 240
TRASDQGPNA GKWDNSKVME EILALRHELA QLLGFENYAF KSLATKMAEN PQQVLDFLTD 300
LAKRARPQGE KELAQLRAFA KAEFGVDELQ PWDIAYYSEK QKQHLYSISD EQLRPYFPEN 360
KAVNGLFEVV KRIYGITAKE RKDVDVWHPD VRFFELYDEN NELRGSFYLD LYARENKRGG 420
AWMDDCVGQM RKADGSLQKP VAYLTCNFNR PVNGKPALFT HDEVITLFHE FGHGLHHMLT 480
RIETAGVSGI SGVPWDAVEL PSQFMENWCW EPEALAFISG HYETGEPLPK ELLDKMLAAK 540
NYQAALFILR QLEFGLFDFR LHAEFRPDQG AKILETLAEI KKLVAVVPSP SWGRFPHAFS 600
HIFAGGYAAG YYSYLWADVL AADAFSRFEE EGIFNRETGQ SFLDNILSRG GSEEPMDLFK 660
RFRGREPQLD AMLEHYGIKG 680 
Gene Ontology
 GO:0005737; C:cytoplasm; TAS:EcoliWiki.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
 GO:0008233; F:peptidase activity; IDA:EcoCyc.
 GO:0006260; P:DNA replication; TAS:EcoCyc.
 GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
 GO:0006465; P:signal peptide processing; IDA:EcoliWiki. 
Interpro
 IPR024079; MetalloPept_cat_dom.
 IPR024077; Neurolysin/TOP_dom2.
 IPR024080; Neurolysin/TOP_N.
 IPR001567; Pept_M3A_M3B. 
Pfam
 PF01432; Peptidase_M3 
SMART
  
PROSITE
 PS00142; ZINC_PROTEASE 
PRINTS