ID   LPLA_SALNS              Reviewed;         338 AA.
AC   B4T4I0;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 77.
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};
GN   OrderedLocusNames=SNSL254_A4933;
OS   Salmonella newport (strain SL254).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=423368;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SL254;
RX   PubMed=21602358; DOI=10.1128/jb.00297-11;
RA   Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA   Leclerc J.E., Ravel J., Cebula T.A.;
RT   "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT   CRISPR-mediated adaptive sublineage evolution.";
RL   J. Bacteriol. 193:3556-3568(2011).
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; CP001113; ACF62330.1; -; Genomic_DNA.
DR   RefSeq; WP_000209753.1; NC_011080.1.
DR   AlphaFoldDB; B4T4I0; -.
DR   SMR; B4T4I0; -.
DR   EnsemblBacteria; ACF62330; ACF62330; SNSL254_A4933.
DR   KEGG; see:SNSL254_A4933; -.
DR   HOGENOM; CLU_022986_0_1_6; -.
DR   OMA; RTCPEDD; -.
DR   UniPathway; UPA00537; UER00594.
DR   UniPathway; UPA00537; UER00595.
DR   Proteomes; UP000008824; 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_1000148115"
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;  37989 MW;  E3C1E27765D83539 CRC64;
     MTTLRLLISD SYDPWFNLAV EECIFRQMPA TQRVLFLWRN ADTVVIGRAQ NPWKECNTRR
     MEEDNVRLAR RSSGGGAVFH DLGNTCFTFM AGKPEYDKTI STHIVLAALN SLGVMADASG
     RNDLVVKTPD GDRKVSGSAY RETKDRGFHH GTLLLNADLS RLAIYLNPDK KKLAAKGITS
     VRSRVANLTE LLPGITHKQV CQAVTEAFFV HYGERVDAEV ISPDKTPDLP NFAETFARQS
     SWEWNFGQAP AFSHLLDERF TWGGVELHFD VEKGVITRAQ VFTDSLNPAP LEALAERLQG
     CLYRADKLQE TCEALLVDFP EQEKELRELS AWIAEAVR