CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-010197
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Putative Lon protease homolog 
Protein Synonyms/Alias
 ATP-dependent protease La homolog 
Gene Name
 ycbZ 
Gene Synonyms/Alias
 b0955; JW0938 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
518SLHSELVKAVEEGKFacetylation[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
 ACT_SITE 438 438 By similarity.
 ACT_SITE 481 481 By similarity.  
Keyword
 Complete proteome; Hydrolase; Protease; Reference proteome; Serine protease. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 586 AA 
Protein Sequence
MTITKLAWRD LVPDTDSYQE IFAQPHLIDE NDPLFSDTQP RLQFALEQLL HTRASSSFML 60
AKAPEESEYL NLIANAARTL QSDAGQLVGG HYEVSGHSIR LRHAVSADDN FATLTQVVAA 120
DWVEAEQLFG CLRQFNGDIT LQPGLVHQAN GGILIISLRT LLAQPLLWMR LKNIVNRERF 180
DWVAFDESRP LPVSVPSMPL KLKVILVGER ESLADFQEME PELSEQAIYS EFEDTLQIVD 240
AESVTQWCRW VTFTARHNHL PAPGADAWPI LIREAARYTG EQETLPLSPQ WILRQCKEVA 300
SLCDGDTFSG EQLNLMLQQR EWREGFLAER MQDEILQEQI LIETEGERIG QINALSVIEF 360
PGHPRAFGEP SRISCVVHIG DGEFTDIERK AELGGNIHAK GMMIMQAFLM SELQLEQQIP 420
FSASLTFEQS YSEVDGDSAS MAELCALISA LADVPVNQSI AITGSVDQFG RAQPVGGLNE 480
KIEGFFAICQ QRELTGKQGV IIPTANVRHL SLHSELVKAV EEGKFTIWAV DDVTDALPLL 540
LNLVWDGEGQ TTLMQTIQER IAQASQQEGR HRFPWPLRWL NWFIPN 586 
Gene Ontology
 GO:0005524; F:ATP binding; IEA:InterPro.
 GO:0004176; F:ATP-dependent peptidase activity; IEA:InterPro.
 GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
 GO:0030163; P:protein catabolic process; IEA:InterPro.
 GO:0006508; P:proteolysis; IEA:UniProtKB-KW. 
Interpro
 IPR027065; Lon_Prtase.
 IPR008269; Pept_S16_C.
 IPR020568; Ribosomal_S5_D2-typ_fold.
 IPR014721; Ribosomal_S5_D2-typ_fold_subgr. 
Pfam
 PF05362; Lon_C 
SMART
  
PROSITE
 PS01046; LON_SER 
PRINTS