ID B3VUB4_LISMN Unreviewed; 138 AA.
AC B3VUB4;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=lipoate--protein ligase {ECO:0000256|ARBA:ARBA00012367};
DE EC=6.3.1.20 {ECO:0000256|ARBA:ARBA00012367};
DE Flags: Fragment;
GN Name=lplA1 {ECO:0000313|EMBL:ACF16441.1};
OS Listeria monocytogenes.
OC Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=1639 {ECO:0000313|EMBL:ACF16441.1};
RN [1] {ECO:0000313|EMBL:ACF16441.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=J2-031 {ECO:0000313|EMBL:ACF16441.1};
RX PubMed=19244915;
RA Lomonaco S., Chen Y., Knabel S.J.;
RT "Analysis of additional virulence genes and virulence gene regions in
RT Listeria monocytogenes confirms the epidemiologic relevance of multi-
RT virulence-locus sequence typing.";
RL J. Food Prot. 71:2559-2566(2008).
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; EU817333; ACF16441.1; -; Genomic_DNA.
DR AlphaFoldDB; B3VUB4; -.
DR UniPathway; UPA00537; UER00594.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016979; F:lipoate-protein ligase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.30.390.50; CO dehydrogenase flavoprotein, C-terminal domain; 1.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR019491; Lipoate_protein_ligase_C.
DR InterPro; IPR004562; LipoylTrfase_LipoateP_Ligase.
DR PANTHER; PTHR12561; LIPOATE-PROTEIN LIGASE; 1.
DR PANTHER; PTHR12561:SF3; LIPOYLTRANSFERASE 1, MITOCHONDRIAL; 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.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:ACF16441.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 72..137
FT /note="Lipoate protein ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10437"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ACF16441.1"
FT NON_TER 138
FT /evidence="ECO:0000313|EMBL:ACF16441.1"
SQ SEQUENCE 138 AA; 16027 MW; BF3EBD390B00D379 CRC64;
IKSVRSRVAN ISDFMDQEMT TEEFRDLLLL YIFGVEKVED VKEYKLTAAD WEKIHEISAK
RYGNWDWNYG KSPKFDLTRT KRFPVGAVDV RLNVQKGVVT DIKIFGDFFG VKNVADIEEK
LVNTTYKREV LAEALVDI
//
