ID H7FYJ1_9LACO Unreviewed; 339 AA.
AC H7FYJ1;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=lipoate--protein ligase {ECO:0000256|ARBA:ARBA00012367};
DE EC=6.3.1.20 {ECO:0000256|ARBA:ARBA00012367};
GN ORFNames=SMXD51_01188 {ECO:0000313|EMBL:EIA32591.1};
OS Ligilactobacillus salivarius SMXD51.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Ligilactobacillus.
OX NCBI_TaxID=1108963 {ECO:0000313|EMBL:EIA32591.1, ECO:0000313|Proteomes:UP000003657};
RN [1] {ECO:0000313|EMBL:EIA32591.1, ECO:0000313|Proteomes:UP000003657}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SMXD51 {ECO:0000313|EMBL:EIA32591.1,
RC ECO:0000313|Proteomes:UP000003657};
RX PubMed=22582370; DOI=10.1128/JB.00344-12;
RA Kergourlay G., Messaoudi S., Dousset X., Prevost H.;
RT "Genome Sequence of Lactobacillus salivarius SMXD51, a Potential Probiotic
RT Strain Isolated from Chicken Cecum, Showing Anti-Campylobacter Activity.";
RL J. Bacteriol. 194:3008-3009(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-lipoate + ATP + L-lysyl-[lipoyl-carrier protein] = AMP +
CC diphosphate + H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[lipoyl-carrier
CC protein]; 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;
CC Evidence={ECO:0000256|ARBA:ARBA00043803};
CC -!- PATHWAY: Protein modification; protein lipoylation via exogenous
CC pathway; protein N(6)-(lipoyl)lysine from lipoate: step 1/2.
CC {ECO:0000256|ARBA:ARBA00005124}.
CC -!- PATHWAY: Protein modification; protein lipoylation via exogenous
CC pathway; protein N(6)-(lipoyl)lysine from lipoate: step 2/2.
CC {ECO:0000256|ARBA:ARBA00005085}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EIA32591.1}.
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DR EMBL; AICL01000003; EIA32591.1; -; Genomic_DNA.
DR RefSeq; WP_003709185.1; NZ_AICL01000003.1.
DR AlphaFoldDB; H7FYJ1; -.
DR PATRIC; fig|1108963.3.peg.924; -.
DR HOGENOM; CLU_022986_0_2_9; -.
DR UniPathway; UPA00537; UER00594.
DR Proteomes; UP000003657; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016979; F:lipoate-protein ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0036211; P:protein modification process; IEA:InterPro.
DR CDD; cd16443; LplA; 1.
DR Gene3D; 3.30.390.50; CO dehydrogenase flavoprotein, C-terminal domain; 1.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004143; BPL_LPL_catalytic.
DR InterPro; IPR019491; Lipoate_protein_ligase_C.
DR InterPro; IPR004562; LipoylTrfase_LipoateP_Ligase.
DR NCBIfam; TIGR00545; lipoyltrans; 1.
DR PANTHER; PTHR12561; LIPOATE-PROTEIN LIGASE; 1.
DR PANTHER; PTHR12561:SF3; LIPOYLTRANSFERASE 1, MITOCHONDRIAL; 1.
DR Pfam; PF03099; BPL_LplA_LipB; 1.
DR Pfam; PF10437; Lip_prot_lig_C; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR SUPFAM; SSF82649; SufE/NifU; 1.
DR PROSITE; PS51733; BPL_LPL_CATALYTIC; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:EIA32591.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 26..217
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51733"
SQ SEQUENCE 339 AA; 38684 MW; 8254F0D9C9D9597F CRC64;
MQYVVMKTDD IRTNLATEQY LMNSDKIKPP FMLFYIEKPC IIVGRNQNTM EEINQKYCEE
HGITITRRLS GGGAMYQDLG NLCFSFVVPA ENQKFGDFKS LVQPVVDALH KMGVTGAETT
GRNDIVVDGK KFSGNAMYTR GGKTFSHGTL MFDVDTDAVA DALRVPKDKI ESKGIKSVRS
RVTNLKPYVS EEYKDFDTFQ FRDELIKLIW GVDSLEEAQQ YEYQLDDEDK KGIEAIEQKL
YKNWDWVYGK SPEFTVKRRK HFTSGTIDAR FLVEDGKIKD IKIYGDFFGS GDVKDVEDAL
RGLKYDVSTI KEALGKLDLN KYFVGIDAED IKELISTQQ
//