CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-006797
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 UDP-N-acetylmuramate:L-alanyl-gamma-D-glutamyl-meso-diaminopimelate ligase 
Protein Synonyms/Alias
 Murein peptide ligase 
Gene Name
 mpl 
Gene Synonyms/Alias
 yjfG; b4233; JW4192 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
198ADIFDDLKAIQKQFHacetylation[1]
202DDLKAIQKQFHHLVRacetylation[1]
272GEKVGEVKWSLVGEHacetylation[1]
444GFGGIHQKLLDGLAKacetylation[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
 Reutilizes the intact tripeptide L-alanyl-gamma-D- glutamyl-meso-diaminopimelate by linking it to UDP-N-acetylmuramic acid. 
Sequence Annotation
 NP_BIND 110 116 ATP (Potential).  
Keyword
 ATP-binding; Cell cycle; Cell division; Cell shape; Cell wall biogenesis/degradation; Complete proteome; Ligase; Nucleotide-binding; Peptidoglycan synthesis; Reference proteome; Secreted. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 457 AA 
Protein Sequence
MRIHILGICG TFMGGLAMLA RQLGHEVTGS DANVYPPMST LLEKQGIELI QGYDASQLEP 60
QPDLVIIGNA MTRGNPCVEA VLEKNIPYMS GPQWLHDFVL RDRWVLAVAG THGKTTTAGM 120
ATWILEQCGY KPGFVIGGVP GNFEVSAHLG ESDFFVIEAD EYDCAFFDKR SKFVHYCPRT 180
LILNNLEFDH ADIFDDLKAI QKQFHHLVRI VPGQGRIIWP ENDINLKQTM AMGCWSEQEL 240
VGEQGHWQAK KLTTDASEWE VLLDGEKVGE VKWSLVGEHN MHNGLMAIAA ARHVGVAPAD 300
AANALGSFIN ARRRLELRGE ANGVTVYDDF AHHPTAILAT LAALRGKVGG TARIIAVLEP 360
RSNTMKMGIC KDDLAPSLGR ADEVFLLQPA HIPWQVAEVA EACVQPAHWS GDVDTLADMV 420
VKTAQPGDHI LVMSNGGFGG IHQKLLDGLA KKAEAAQ 457 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:EcoliWiki.
 GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
 GO:0016881; F:acid-amino acid ligase activity; IDA:EcoCyc.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
 GO:0051301; P:cell division; IEA:UniProtKB-KW.
 GO:0071555; P:cell wall organization; IEA:InterPro.
 GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW.
 GO:0009254; P:peptidoglycan turnover; IEA:UniProtKB-UniPathway.
 GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. 
Interpro
 IPR004101; Mur_ligase_C.
 IPR013221; Mur_ligase_cen.
 IPR000713; Mur_ligase_N.
 IPR005757; Murein_peptide_ligase.
 IPR016040; NAD(P)-bd_dom. 
Pfam
 PF01225; Mur_ligase
 PF02875; Mur_ligase_C
 PF08245; Mur_ligase_M 
SMART
  
PROSITE
  
PRINTS