ID A0A150WDK3_BDEBC Unreviewed; 339 AA.
AC A0A150WDK3;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=lipoate--protein ligase {ECO:0000256|ARBA:ARBA00012367};
DE EC=6.3.1.20 {ECO:0000256|ARBA:ARBA00012367};
GN Name=lplA {ECO:0000313|EMBL:KYG60952.1};
GN ORFNames=AZI86_18720 {ECO:0000313|EMBL:KYG60952.1};
OS Bdellovibrio bacteriovorus.
OC Bacteria; Bdellovibrionota; Bdellovibrionia; Bdellovibrionales;
OC Pseudobdellovibrionaceae; Bdellovibrio.
OX NCBI_TaxID=959 {ECO:0000313|EMBL:KYG60952.1, ECO:0000313|Proteomes:UP000075320};
RN [1] {ECO:0000313|EMBL:KYG60952.1, ECO:0000313|Proteomes:UP000075320}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R0 {ECO:0000313|EMBL:KYG60952.1,
RC ECO:0000313|Proteomes:UP000075320};
RA Ploux O.;
RL Submitted (MAR-2016) 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:KYG60952.1}.
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DR EMBL; LUKE01000008; KYG60952.1; -; Genomic_DNA.
DR RefSeq; WP_061836830.1; NZ_LUKE01000008.1.
DR AlphaFoldDB; A0A150WDK3; -.
DR UniPathway; UPA00537; UER00594.
DR Proteomes; UP000075320; 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:KYG60952.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000075320}.
FT DOMAIN 29..216
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51733"
SQ SEQUENCE 339 AA; 38767 MW; 3DDF572AA308EE5E CRC64;
MKKLKVFLSE SKNPHLNIAT EEWIFDNLDP SQQVLFLWQN EETVVIGRNQ NPWNECNLAK
MKEDKVHLAR RKTGGGAVFH DLGNICFTFL SPREEYKREN NVQIIFNALK ELGITGEASG
RNDLLIPFPD GPRKFSGSAY REKKDRAFHH GTLLLHADLT RLGNYLTPNP KKLQAKGKES
VRARVANLNE VRPGIEAKHI VEYMVPAFER FYDGKADIEM LSLATVNKNA ELKGHYDQLS
SWEWLYGNTL EFTHKMDEYL SLGFFDFQFK VEDGVIKDVH IYTDCLYPSL VDELTTRLKG
QPYRGDSVKA AIEAAKTKHP DLIAGVSELG QWLLKNIEI
//
