ID A0A0M2PDD2_9BACI Unreviewed; 330 AA.
AC A0A0M2PDD2;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=lipoate--protein ligase {ECO:0000256|ARBA:ARBA00012367};
DE EC=6.3.1.20 {ECO:0000256|ARBA:ARBA00012367};
GN ORFNames=WQ54_18975 {ECO:0000313|EMBL:KKI90830.1};
OS Bacillus sp. SA1-12.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1455638 {ECO:0000313|EMBL:KKI90830.1, ECO:0000313|Proteomes:UP000034887};
RN [1] {ECO:0000313|EMBL:KKI90830.1, ECO:0000313|Proteomes:UP000034887}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SA1-12 {ECO:0000313|EMBL:KKI90830.1,
RC ECO:0000313|Proteomes:UP000034887};
RA Kumar A., Mathan Kumar R., Kaur N., Kumar N., Singh N.K., Kaur G.,
RA Mayilraj S.;
RT "Taxonomic description and genome sequence of Bacillus tuticoriensis sp.
RT nov., a novel member of the genus Bacillus isolated from solar saltern.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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:KKI90830.1}.
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DR EMBL; LATZ01000113; KKI90830.1; -; Genomic_DNA.
DR RefSeq; WP_046586319.1; NZ_LATZ01000113.1.
DR AlphaFoldDB; A0A0M2PDD2; -.
DR PATRIC; fig|1455638.3.peg.4161; -.
DR OrthoDB; 9788148at2; -.
DR UniPathway; UPA00537; UER00594.
DR Proteomes; UP000034887; 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:KKI90830.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 27..215
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51733"
SQ SEQUENCE 330 AA; 38078 MW; 7A13B6A13D622664 CRC64;
MLFIDNNGIT DPRINLAIEE YAVKHLDPNE TYLLFYINEP SIIIGKNQNT IEEINTSYVE
ENKIHVVRRL SGGGAVYHDK GNLNFSFITK DDGESFHNFK KFTEPVVLAL EKLGVKAEMS
GRNDIIAGDG RKISGNAQFS SRGRMFSHGT LLFDSEIDSV VSALKVKKDK IESKGIKSIR
SRVANIIEYL EEKITIEQFR ELLLRYIFDG ADQIPTYDLT DEDWKKINEI SKERYQNWDW
NYGKSPKFNY QHSHRFPVGQ IDVRLEVQKG VIENCKIYGD FFGVGDVKEV EQALIGTRYD
KSELERMLQE IDVKAYFGNI EKTDFLQLIY
//
