ID   LPLA_PECCP              Reviewed;         338 AA.
AC   C6DKP5;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Lipoate-protein ligase A {ECO:0000255|HAMAP-Rule:MF_01602};
DE            EC=6.3.1.20 {ECO:0000255|HAMAP-Rule:MF_01602};
DE   AltName: Full=Lipoate--protein ligase {ECO:0000255|HAMAP-Rule:MF_01602};
GN   Name=lplA {ECO:0000255|HAMAP-Rule:MF_01602}; OrderedLocusNames=PC1_2465;
OS   Pectobacterium carotovorum subsp. carotovorum (strain PC1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=561230;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PC1;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C.,
RA   Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Balakrishnan V., Glasner J., Perna N.T.;
RT   "Complete sequence of Pectobacterium carotovorum subsp. carotovorum PC1.";
RL   Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes both the ATP-dependent activation of exogenously
CC       supplied lipoate to lipoyl-AMP and the transfer of the activated lipoyl
CC       onto the lipoyl domains of lipoate-dependent enzymes.
CC       {ECO:0000255|HAMAP-Rule:MF_01602}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-lipoate + ATP + L-lysyl-[lipoyl-carrier protein] = (R)-
CC         N(6)-lipoyl-L-lysyl-[lipoyl-carrier protein] + AMP + diphosphate +
CC         H(+); Xref=Rhea:RHEA:49288, Rhea:RHEA-COMP:10500, Rhea:RHEA-
CC         COMP:10502, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:83088, ChEBI:CHEBI:83099,
CC         ChEBI:CHEBI:456215; EC=6.3.1.20; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01602};
CC   -!- PATHWAY: Protein modification; protein lipoylation via exogenous
CC       pathway; protein N(6)-(lipoyl)lysine from lipoate: step 1/2.
CC       {ECO:0000255|HAMAP-Rule:MF_01602}.
CC   -!- PATHWAY: Protein modification; protein lipoylation via exogenous
CC       pathway; protein N(6)-(lipoyl)lysine from lipoate: step 2/2.
CC       {ECO:0000255|HAMAP-Rule:MF_01602}.
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01602}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01602}.
CC   -!- MISCELLANEOUS: In the transfer reaction, the free carboxyl group of
CC       lipoic acid is attached via an amide linkage to the epsilon-amino group
CC       of a specific lysine residue of lipoyl domains of lipoate-dependent
CC       enzymes. {ECO:0000255|HAMAP-Rule:MF_01602}.
CC   -!- SIMILARITY: Belongs to the LplA family. {ECO:0000255|HAMAP-
CC       Rule:MF_01602}.
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DR   EMBL; CP001657; ACT13496.1; -; Genomic_DNA.
DR   RefSeq; WP_015840676.1; NC_012917.1.
DR   AlphaFoldDB; C6DKP5; -.
DR   SMR; C6DKP5; -.
DR   STRING; 561230.PC1_2465; -.
DR   EnsemblBacteria; ACT13496; ACT13496; PC1_2465.
DR   KEGG; pct:PC1_2465; -.
DR   eggNOG; COG0095; Bacteria.
DR   HOGENOM; CLU_022986_0_1_6; -.
DR   OMA; RTCPEDD; -.
DR   OrthoDB; 871298at2; -.
DR   UniPathway; UPA00537; UER00594.
DR   UniPathway; UPA00537; UER00595.
DR   Proteomes; UP000002736; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016979; F:lipoate-protein ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009249; P:protein lipoylation; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.930.10; -; 1.
DR   HAMAP; MF_01602; LplA; 1.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR004143; BPL_LPL_catalytic.
DR   InterPro; IPR023741; Lipoate_ligase_A.
DR   InterPro; IPR019491; Lipoate_protein_ligase_C.
DR   InterPro; IPR004562; LipoylTrfase_LipoateP_Ligase.
DR   PANTHER; PTHR12561; PTHR12561; 1.
DR   Pfam; PF03099; BPL_LplA_LipB; 1.
DR   Pfam; PF10437; Lip_prot_lig_C; 1.
DR   SUPFAM; SSF55681; SSF55681; 1.
DR   TIGRFAMs; TIGR00545; lipoyltrans; 1.
DR   PROSITE; PS51733; BPL_LPL_CATALYTIC; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Ligase; Nucleotide-binding.
FT   CHAIN           1..338
FT                   /note="Lipoate-protein ligase A"
FT                   /id="PRO_1000215690"
FT   DOMAIN          29..216
FT                   /note="BPL/LPL catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01067"
FT   BINDING         71
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01602"
FT   BINDING         76..79
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01602"
FT   BINDING         134
FT                   /ligand="(R)-lipoate"
FT                   /ligand_id="ChEBI:CHEBI:83088"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01602"
FT   BINDING         134
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01602"
SQ   SEQUENCE   338 AA;  37858 MW;  4FD33600FC3851A0 CRC64;
     MSSLRLLISD SYDPWFNLAV EECIFRQMPT TQRVLFLWRN AETVVIGRAQ NPWKECNTRR
     MEEDGIKLAR RSSGGGAVFH DLGNTCFTFM AGKPEYDKSV STQIVLDALS ALGLKASASG
     RNDLVVETAD GVRKVSGSAY RETKDRGFHH GTLLLNADLN RLADYLNPDI KKLQAKGITS
     VRSRVANLVE LLPSVDHQVI CQAVTQAFFD YFGEQCEPEI ISPSAYPDLP GFSEQFARQS
     SWEWNFGQAP DFSHLLDNRF TWGGIELHFD VERGVIIRAQ VYTDSLNPAP LEALACALQG
     TAYRPENMAA TCQALITAFP EQQNELQELA EWLEQSLR