ID A0A3S0TN50_9MOLU Unreviewed; 328 AA.
AC A0A3S0TN50;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 18-JUN-2025, entry version 27.
DE RecName: Full=lipoate--protein ligase {ECO:0000256|ARBA:ARBA00012367};
DE EC=6.3.1.20 {ECO:0000256|ARBA:ARBA00012367};
GN ORFNames=D9R21_00635 {ECO:0000313|EMBL:RUO86856.1};
OS Spiroplasma endosymbiont of Megaselia nigra.
OC Bacteria; Bacillati; Mycoplasmatota; Mollicutes; Entomoplasmatales;
OC Spiroplasmataceae; Spiroplasma.
OX NCBI_TaxID=2478537 {ECO:0000313|EMBL:RUO86856.1, ECO:0000313|Proteomes:UP000270797};
RN [1] {ECO:0000313|EMBL:RUO86856.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SNigra {ECO:0000313|EMBL:RUO86856.1};
RX PubMed=30576446; DOI=.1093/gbe/evy272;
RA Ballinger M.J., Gawryluk R.M., Perlman S.J.;
RT "Toxin and genome evolution in a Drosophila defensive symbiosis.";
RL Genome Biol. Evol. 11:253-262(2019).
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}.
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:RUO86856.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; RCOO01000004; RUO86856.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S0TN50; -.
DR UniPathway; UPA00537; UER00594.
DR Proteomes; UP000270797; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
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:0017118; F:lipoyltransferase activity; IEA:TreeGrafter.
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; 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; 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:RUO86856.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 25..212
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51733"
SQ SEQUENCE 328 AA; 37346 MW; 289F3F8EE6B2EAF2 CRC64;
MICFKNSSTD VYFNLALDEY LLKSDIKDNI FFLWKNFNTI VIGRNQNTIE EINLQAVETD
KVNVARRITG GGAVYQDDGN LCFSSIFNKD DKIAQNYESI LQPIINVLQK LGLNAKFAGK
NDIEIDGKKI SGNAQIKYKN RLLHHGTFLF DVDLSKMQKY LNVSQDKIIS KGIKSIPARV
TNIRPLLTND ITIDEFMLFI TNEFLAQGTP VLDLPPDIIA AVNKLADEKY RTWEWNFGNS
PEFSYQNKIR YEGKGTVYVC LNVNEVKITN IKFFGDFLGS GGTEPLETLL TGCEYNLDKI
KTKLLEINIK DIFGDKFELQ EILDVIFT
//
