LPLA_SALA4
ID LPLA_SALA4 Reviewed; 338 AA.
AC B5F534;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 03-AUG-2022, entry version 75.
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=SeAg_B4899;
OS Salmonella agona (strain SL483).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=454166;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SL483;
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; CP001138; ACH50548.1; -; Genomic_DNA.
DR RefSeq; WP_000209772.1; NC_011149.1.
DR AlphaFoldDB; B5F534; -.
DR SMR; B5F534; -.
DR EnsemblBacteria; ACH50548; ACH50548; SeAg_B4899.
DR KEGG; sea:SeAg_B4899; -.
DR HOGENOM; CLU_022986_0_1_6; -.
DR OMA; RTCPEDD; -.
DR UniPathway; UPA00537; UER00594.
DR UniPathway; UPA00537; UER00595.
DR Proteomes; UP000008819; 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_1000148110"
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; 37862 MW; 88570E9559DA947A CRC64;
MTTLRLLISD SYDPWFNLAV EECIFRQMPA TQRVLFLWRN ADTVVIGRAQ NPWKECNTRR
MEEDNVRLAR RSSGGGAVFH DLGNTCFTFM AGKPEYDKTI STHIVLAALN SLGVMADASG
RNDLVVKTPD GDRKVSGSAY RETKDRGFHH GTLLLNADLS RLANYLNPDK KKLAAKGITS
VRSRVANLTK LLPGITHEQV CQAVTEAFFA HYGERVDAEV ISPDKTPDLP NFAETFARQS
SWEWNFGQAP AFSHLLDERF TWGGVELHFD VEKGVITRAQ VFTDSLNPAP LEALAERLQG
CLYRADMLQQ ACEALLVDFP EQEKELRELS AWIAGAVR