ID A0A9C7GB42_9BACI Unreviewed; 329 AA.
AC A0A9C7GB42;
DT 03-MAY-2023, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2023, sequence version 1.
DT 18-JUN-2025, entry version 13.
DE RecName: Full=lipoate--protein ligase {ECO:0000256|ARBA:ARBA00012367};
DE EC=6.3.1.20 {ECO:0000256|ARBA:ARBA00012367};
GN Name=lplJ {ECO:0000313|EMBL:CAG9609259.1};
GN ORFNames=NEOCIP111885_03001 {ECO:0000313|EMBL:CAG9609259.1};
OS Pseudoneobacillus rhizosphaerae.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC Pseudoneobacillus.
OX NCBI_TaxID=2880968 {ECO:0000313|EMBL:CAG9609259.1, ECO:0000313|Proteomes:UP000789845};
RN [1] {ECO:0000313|EMBL:CAG9609259.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CIP111885 {ECO:0000313|EMBL:CAG9609259.1};
RA Criscuolo A.;
RL Submitted (OCT-2021) 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}.
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:CAG9609259.1}.
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DR EMBL; CAKJTG010000017; CAG9609259.1; -; Genomic_DNA.
DR RefSeq; WP_230497494.1; NZ_CAKJTG010000017.1.
DR Proteomes; UP000789845; 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:TreeGrafter.
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 FunFam; 3.30.930.10:FF:000072; Lipoate--protein ligase; 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:CAG9609259.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000789845}.
FT DOMAIN 27..214
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51733"
SQ SEQUENCE 329 AA; 37533 MW; 8F1F1E048DE0F4D7 CRC64;
MLFIDNKGIT DPRINLAIEE YALKNLDINE TYLLFYINEP SIIIGKNQNT VEEINTDYVE
SNGIKVVRRL SGGGAVYHDL GNLNFSFITK DDGESFHNFR KFTEPVIAAL QKLGVNAELS
GRNDILAEGR KISGNAQFST KGRMFSHGTL LFDSEIEHVV SALRVKQDKI ESKGIKSIRS
RVANISEFLS DSMDIQQFRS HLLKNIFSES NDIPEYVLTE EDWSKIHELS KERYQNWDWN
YGKSPKFNSQ HSHRFPVGSI DVRLEVNKGI IESCKIYGDF FGVGDVSEIE TLLTGQKYEK
ATIEQALQEA NIPHYFGNIT KEDFINLIY
//
