Tag | Content |
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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 |
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170 | ANYLNPDKKKLAAKG | acetylation | [1] |
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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 |
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