ID A0A060LUW9_9BACI Unreviewed; 329 AA.
AC A0A060LUW9;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=lipoate--protein ligase {ECO:0000256|ARBA:ARBA00012367};
DE EC=6.3.1.20 {ECO:0000256|ARBA:ARBA00012367};
GN ORFNames=BleG1_1419 {ECO:0000313|EMBL:AIC94002.1};
OS Shouchella lehensis G1.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Shouchella.
OX NCBI_TaxID=1246626 {ECO:0000313|EMBL:AIC94002.1, ECO:0000313|Proteomes:UP000027142};
RN [1] {ECO:0000313|EMBL:AIC94002.1, ECO:0000313|Proteomes:UP000027142}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G1 {ECO:0000313|EMBL:AIC94002.1,
RC ECO:0000313|Proteomes:UP000027142};
RX PubMed=24811681; DOI=10.1016/j.gene.2014.05.012;
RA Noor Y.M., Samsulrizal N.H., Jema'on N.A., Low K.O., Ramli A.N.,
RA Alias N.I., Damis S.I., Fuzi S.F., Isa M.N., Murad A.M., Raih M.F.,
RA Bakar F.D., Najimudin N., Mahadi N.M., Illias R.M.;
RT "A comparative genomic analysis of the alkalitolerant soil bacterium
RT Bacillus lehensis G1.";
RL Gene 545:253-261(2014).
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}.
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DR EMBL; CP003923; AIC94002.1; -; Genomic_DNA.
DR RefSeq; WP_038478768.1; NZ_CP003923.1.
DR AlphaFoldDB; A0A060LUW9; -.
DR STRING; 1246626.BleG1_1419; -.
DR KEGG; ble:BleG1_1419; -.
DR PATRIC; fig|1246626.3.peg.1409; -.
DR eggNOG; COG0095; Bacteria.
DR HOGENOM; CLU_022986_0_2_9; -.
DR OrthoDB; 9788148at2; -.
DR UniPathway; UPA00537; UER00594.
DR Proteomes; UP000027142; Chromosome.
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:AIC94002.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000027142}.
FT DOMAIN 27..214
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51733"
SQ SEQUENCE 329 AA; 37534 MW; E15AA5414496F485 CRC64;
MKFINNNNLT DPRINLAIEE WALKNLDPNE SYLLFYINEP SIIIGKNQNT FEEINLDYVK
DNNLHVVRRL SGGGAVYHDL GNLNFSFITK DDGDSFHNFK KFTEPVVQAL KQLGVQAELS
GRNDIQVGER KISGNAQFTT KGRMFSHGTL MLQSEIENVV SALRVKDDKI KSKGIKSIRS
RVANISEFLK QPMTMEEFKS MLLQYIFNGQ EDIPEHVITE EEWKEINALS SERYQSWDWN
YGKSPAFDIQ RSKRFPIGTI DLRLNVKKGV ISDCKIFGDF FGVADVSGLE EQLVGKRYDA
SELAQVLDSA DLKAYFGSIS KEEFLSLIY
//
