ID E4KRG1_9LACT Unreviewed; 335 AA.
AC E4KRG1;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE RecName: Full=lipoate--protein ligase {ECO:0000256|ARBA:ARBA00012367};
DE EC=6.3.1.20 {ECO:0000256|ARBA:ARBA00012367};
GN ORFNames=HMPREF9257_0462 {ECO:0000313|EMBL:EFR30526.1};
OS Eremococcus coleocola ACS-139-V-Col8.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Aerococcaceae; Eremococcus.
OX NCBI_TaxID=908337 {ECO:0000313|EMBL:EFR30526.1, ECO:0000313|Proteomes:UP000005990};
RN [1] {ECO:0000313|EMBL:EFR30526.1, ECO:0000313|Proteomes:UP000005990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACS-139-V-Col8 {ECO:0000313|EMBL:EFR30526.1,
RC ECO:0000313|Proteomes:UP000005990};
RA Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G.,
RA Nelson K.E.;
RL Submitted (OCT-2010) 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:ARBA00001121};
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:EFR30526.1}.
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DR EMBL; AENN01000018; EFR30526.1; -; Genomic_DNA.
DR RefSeq; WP_006419049.1; NZ_AENN01000018.1.
DR AlphaFoldDB; E4KRG1; -.
DR STRING; 908337.HMPREF9257_0462; -.
DR eggNOG; COG0095; Bacteria.
DR OrthoDB; 9788148at2; -.
DR UniPathway; UPA00537; UER00594.
DR Proteomes; UP000005990; 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:EFR30526.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000005990};
KW Transferase {ECO:0000313|EMBL:EFR30526.1}.
FT DOMAIN 27..209
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51733"
SQ SEQUENCE 335 AA; 38239 MW; CF7F89946E26BE45 CRC64;
MIFVDNQNVY DASMNIALET YLVENRLVDE PILLFYINDP SIIIGRNQNT IEEVNQPYIE
EKGIRVVRRM SGGGAVYHDR GNFSFCFIKD DDGSFRDFQS FTKPVIDALH KMGATGAELQ
GRNDLLIDGK KFSGNAMYAK DGRMTAHGTI LFDSDLDEVN NALKPRKEKV ESKGIKSVRS
RVTNIKPFVD DKYKNLTTEE FRDLVLLEIF GVESRDQVPE FKLTDEIWEG VKKIHAERMG
NWDWNYGQSP DFDYEKSHKF PFGFVDFRFN VSQGEIVDAT IFGDFFGLGD IKDVEEKLNG
VKFEKAAIID ALKDVNLNKY LGDISAEELA NLIFE
//