ID   LPLA_SALPK              Reviewed;         338 AA.
AC   B5BAK2;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 73.
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=SSPA4071;
OS   Salmonella paratyphi A (strain AKU_12601).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=554290;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AKU_12601;
RX   PubMed=19159446; DOI=10.1186/1471-2164-10-36;
RA   Holt K.E., Thomson N.R., Wain J., Langridge G.C., Hasan R., Bhutta Z.A.,
RA   Quail M.A., Norbertczak H., Walker D., Simmonds M., White B., Bason N.,
RA   Mungall K., Dougan G., Parkhill J.;
RT   "Pseudogene accumulation in the evolutionary histories of Salmonella
RT   enterica serovars Paratyphi A and Typhi.";
RL   BMC Genomics 10:36-36(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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FM200053; CAR62368.1; -; Genomic_DNA.
DR   RefSeq; WP_000209782.1; NC_011147.1.
DR   AlphaFoldDB; B5BAK2; -.
DR   SMR; B5BAK2; -.
DR   KEGG; sek:SSPA4071; -.
DR   HOGENOM; CLU_022986_0_1_6; -.
DR   OMA; RTCPEDD; -.
DR   UniPathway; UPA00537; UER00594.
DR   UniPathway; UPA00537; UER00595.
DR   Proteomes; UP000001869; 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_1000148116"
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;  37840 MW;  0586A04E9EA2B3F1 CRC64;
     MTTLRLLISD SYDPWFNLAV EEYIFRQMPA TQRVLFLWRN ADTVVIGRAQ NPWKECNTRR
     MEEDNVRLAR RSSGGGAVFH DLGNTCFTFM AGKPEYDKTI STHIVLAALN SLGVMADASG
     RNDLVVKTPD GDRKVSGSAY RETKDRGFHH GTLLLNADLS RLANYLNPDK KKLAAKGITS
     VRSRVANLTE LLPGITHEQV CQAVTEAFFA HYGERIDAEV ISPDKTPDLP NFTETFARQS
     SWEWNFGQAP AFSHLLDERF TWGGVELHFD VEKGVITRAQ AFTDSLNPAP LEALAGRLQG
     CQYRADKLQE TCEALIATFP EQESELRELA NWVAGAVR