CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-006049
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Lipoate-protein ligase A 
Protein Synonyms/Alias
 Lipoate--protein ligase 
Gene Name
 lplA 
Gene Synonyms/Alias
 yjjF; b4386; JW4349 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
170ANYLNPDKKKLAAKGacetylation[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
 Catalyzes both the ATP-dependent activation of exogenously supplied lipoate to lipoyl-AMP and the transfer of the activated lipoyl onto the lipoyl domains of lipoate-dependent enzymes. Is also able to catalyze very poorly the transfer of lipoyl and octanoyl moiety from their acyl carrier protein. 
Sequence Annotation
 NP_BIND 76 79 ATP (By similarity).
 BINDING 71 71 ATP (By similarity).
 BINDING 134 134 ATP (By similarity).
 BINDING 134 134 Lipoate (By similarity).  
Keyword
 3D-structure; ATP-binding; Complete proteome; Cytoplasm; Direct protein sequencing; Nucleotide-binding; Reference proteome; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 338 AA 
Protein Sequence
MSTLRLLISD SYDPWFNLAV EECIFRQMPA TQRVLFLWRN ADTVVIGRAQ NPWKECNTRR 60
MEEDNVRLAR RSSGGGAVFH DLGNTCFTFM AGKPEYDKTI STSIVLNALN ALGVSAEASG 120
RNDLVVKTVE GDRKVSGSAY RETKDRGFHH GTLLLNADLS RLANYLNPDK KKLAAKGITS 180
VRSRVTNLTE LLPGITHEQV CEAITEAFFA HYGERVEAEI ISPNKTPDLP NFAETFARQS 240
SWEWNFGQAP AFSHLLDERF TWGGVELHFD VEKGHITRAQ VFTDSLNPAP LEALAGRLQG 300
CLYRADMLQQ ECEALLVDFP EQEKELRELS AWMAGAVR 338 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:EcoCyc.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0016979; F:lipoate-protein ligase activity; IMP:EcoliWiki.
 GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
 GO:0018055; P:peptidyl-lysine lipoylation; IEA:HAMAP.
 GO:0009249; P:protein lipoylation; IMP:EcoCyc. 
Interpro
 IPR004143; BPL_LipA_LipB.
 IPR023741; Lipoate_ligase_A.
 IPR019491; Lipoate_protein_ligase_C.
 IPR004562; LipoylTrfase_LipoateP_Ligase. 
Pfam
 PF03099; BPL_LplA_LipB
 PF10437; Lip_prot_lig_C 
SMART
  
PROSITE
  
PRINTS