ID   LPLA_ECOBW              Reviewed;         338 AA.
AC   C4ZT68;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-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=BWG_4078;
OS   Escherichia coli (strain K12 / MC4100 / BW2952).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=595496;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MC4100 / BW2952;
RX   PubMed=19376874; DOI=10.1128/jb.00118-09;
RA   Ferenci T., Zhou Z., Betteridge T., Ren Y., Liu Y., Feng L., Reeves P.R.,
RA   Wang L.;
RT   "Genomic sequencing reveals regulatory mutations and recombinational events
RT   in the widely used MC4100 lineage of Escherichia coli K-12.";
RL   J. Bacteriol. 191:4025-4029(2009).
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; CP001396; ACR63657.1; -; Genomic_DNA.
DR   RefSeq; WP_000105884.1; NC_012759.1.
DR   AlphaFoldDB; C4ZT68; -.
DR   SMR; C4ZT68; -.
DR   KEGG; ebw:BWG_4078; -.
DR   HOGENOM; CLU_022986_0_1_6; -.
DR   OMA; RTCPEDD; -.
DR   UniPathway; UPA00537; UER00594.
DR   UniPathway; UPA00537; UER00595.
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_1000215689"
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;  37926 MW;  102788082E182A6F CRC64;
     MSTLRLLISD SYDPWFNLAV EECIFRQMPA TQRVLFLWRN ADTVVIGRAQ NPWKECNTRR
     MEEDNVRLAR RSSGGGAVFH DLGNTCFTFM AGKPEYDKTI STSIVLNALN ALGVSAEASG
     RNDLVVKTVE GDRKVSGSAY RETKDRGFHH GTLLLNADLS RLANYLNPDK KKLAAKGITS
     VRSRVTNLTE LLPGITHEQV CEAITEAFFA HYGERVEAEI ISPNKTPDLP NFAETFARQS
     SWEWNFGQAP AFSHLLDERF TWGGVELHFD VEKGHITRAQ VFTDSLNPAP LEALAGRLQG
     CLYRADMLQQ ECEALLVDFP EQEKELRELS AWMAGAVR