ID A0A1W1WJE0_SULTA Unreviewed; 358 AA.
AC A0A1W1WJE0;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 05-FEB-2025, entry version 24.
DE RecName: Full=lipoate--protein ligase {ECO:0000256|ARBA:ARBA00012367};
DE EC=6.3.1.20 {ECO:0000256|ARBA:ARBA00012367};
GN ORFNames=SAMN00768000_2780 {ECO:0000313|EMBL:SMC06366.1};
OS Sulfobacillus thermosulfidooxidans (strain DSM 9293 / VKM B-1269 / AT-1).
OC Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
OC Clostridiales Family XVII. Incertae Sedis; Sulfobacillus.
OX NCBI_TaxID=929705 {ECO:0000313|EMBL:SMC06366.1, ECO:0000313|Proteomes:UP000192660};
RN [1] {ECO:0000313|Proteomes:UP000192660}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 9293 {ECO:0000313|Proteomes:UP000192660};
RA Varghese N., Submissions S.;
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl-[lipoyl-carrier protein] + (R)-lipoate + ATP = N(6)-
CC [(R)-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;
CC Evidence={ECO:0000256|ARBA:ARBA00048037};
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}.
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DR EMBL; FWWY01000001; SMC06366.1; -; Genomic_DNA.
DR RefSeq; WP_020373189.1; NZ_FWWY01000001.1.
DR AlphaFoldDB; A0A1W1WJE0; -.
DR STRING; 28034.BFX07_11300; -.
DR OrthoDB; 9788148at2; -.
DR UniPathway; UPA00537; UER00594.
DR Proteomes; UP000192660; 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; 3.30.930.10; Bira Bifunctional Protein, Domain 2; 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; IPR050664; Octanoyltrans_LipM/LipL.
DR PANTHER; PTHR43679:SF2; OCTANOYL-[GCVH]:PROTEIN N-OCTANOYLTRANSFERASE; 1.
DR PANTHER; PTHR43679; OCTANOYLTRANSFERASE LIPM-RELATED; 1.
DR Pfam; PF10437; Lip_prot_lig_C; 1.
DR Pfam; PF21948; LplA-B_cat; 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:SMC06366.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000192660}.
FT DOMAIN 27..216
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51733"
SQ SEQUENCE 358 AA; 40513 MW; F52158CFF5B59881 CRC64;
MRYLDLGTVK REISQAVYHA LAERMRPHDE ITLVTVSPDR PYVCVGYHQL ASREIDRAFC
EAHQILVGRR FVGGGAVYLD HGQVFWHLLL PTPRGPVEDL YREILKAPIE TYQQMGINAQ
FRPVNDIVVG PRKIGGTGAS TMGTTTVIVG SLLFDFNIEL MARVLKVPSE KFRDKMISSL
SEYMTTINQE LGQPPERQMV VAKLVDNFSR LLNEPVHHDQ LTAEEEADIE QYALKLFDPE
FVYRGERGLF HSGIKIRSGV FLHEGVFKAP GGLLRLIYRV NDGVFDDVNF SGDFFMEPWD
SSAVEDFQGY LQGRLVNEQN VEEAARQLFE KVSIPGVVAS DIVECFRRAE STEQSSVR
//
