ID Q6F279_MESFL Unreviewed; 334 AA.
AC Q6F279;
DT 16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT 16-AUG-2004, sequence version 1.
DT 27-MAR-2024, entry version 108.
DE RecName: Full=lipoate--protein ligase {ECO:0000256|ARBA:ARBA00012367};
DE EC=6.3.1.20 {ECO:0000256|ARBA:ARBA00012367};
GN OrderedLocusNames=Mfl038 {ECO:0000313|EMBL:AAT75394.1};
OS Mesoplasma florum (strain ATCC 33453 / NBRC 100688 / NCTC 11704 / L1)
OS (Acholeplasma florum).
OC Bacteria; Mycoplasmatota; Mollicutes; Entomoplasmatales;
OC Entomoplasmataceae; Mesoplasma.
OX NCBI_TaxID=265311 {ECO:0000313|EMBL:AAT75394.1, ECO:0000313|Proteomes:UP000006647};
RN [1] {ECO:0000313|EMBL:AAT75394.1, ECO:0000313|Proteomes:UP000006647}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33453 / NBRC 100688 / NCTC 11704 / L1
RC {ECO:0000313|Proteomes:UP000006647};
RA Birren B.W., Stange-Thomann N., Hafez N., DeCaprio D., Fisher S.,
RA Butler J., Elkins T., Kodira C.D., Major J., Wang S., Nicol R., Nusbaum C.;
RL Submitted (JUN-2004) 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: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; AE017263; AAT75394.1; -; Genomic_DNA.
DR RefSeq; WP_011182935.1; NC_006055.1.
DR RefSeq; YP_053278.1; NC_006055.1.
DR AlphaFoldDB; Q6F279; -.
DR STRING; 265311.Mfl038; -.
DR PaxDb; 265311-Mfl038; -.
DR EnsemblBacteria; AAT75394; AAT75394; Mfl038.
DR GeneID; 2898104; -.
DR KEGG; mfl:Mfl038; -.
DR PATRIC; fig|265311.5.peg.38; -.
DR eggNOG; COG0095; Bacteria.
DR HOGENOM; CLU_022986_0_2_14; -.
DR OrthoDB; 9788148at2; -.
DR UniPathway; UPA00537; UER00594.
DR Proteomes; UP000006647; 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:AAT75394.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000006647}.
FT DOMAIN 27..200
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51733"
SQ SEQUENCE 334 AA; 38531 MW; 995BD56CDB125D59 CRC64;
MINLFISKSN DPAYNLAVEE YLTYHYQTKD PILYIWQNSN TIVVGRNQNT YAEINIAEAM
KDEVKIIRRN TGGGTVFHDM GNVCYSLIVN NDKNSQSNFE IALQPIIQYL RSEGLNANFS
GRNDIEIDGY KISGNAQLKT NNKILQHGTL LFDVELPRIL KYLNVDPEKI KHQKVKSKPA
RVANIKALLE GINKNIELTD FINNIINSYT KNEETKWIEF SETDELAINK CFEEKYQSRD
WTFAKNENFE ISNKKYLESK GLTEIKINVD KGKIQNIKIY GDFLGYIGTE ALEFSLLNVN
YDYHSVKNIL DKFALKEIFG DNFEAEDILN LIFN
//
