ID K1M239_9LACT Unreviewed; 335 AA.
AC K1M239;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=lipoate--protein ligase {ECO:0000256|ARBA:ARBA00012367};
DE EC=6.3.1.20 {ECO:0000256|ARBA:ARBA00012367};
GN ORFNames=HMPREF9707_00262 {ECO:0000313|EMBL:EKB58367.1};
OS Falseniella ignava CCUG 37419.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Aerococcaceae; Falseniella.
OX NCBI_TaxID=883112 {ECO:0000313|EMBL:EKB58367.1, ECO:0000313|Proteomes:UP000005147};
RN [1] {ECO:0000313|EMBL:EKB58367.1, ECO:0000313|Proteomes:UP000005147}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 37419 {ECO:0000313|EMBL:EKB58367.1,
RC ECO:0000313|Proteomes:UP000005147};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Huys G., Walker B., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S.,
RA Hansen M., Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Facklamia ignava CCUG 37419.";
RL Submitted (JUL-2012) 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}.
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:EKB58367.1}.
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DR EMBL; AGZE01000005; EKB58367.1; -; Genomic_DNA.
DR RefSeq; WP_006700926.1; NZ_JH932300.1.
DR AlphaFoldDB; K1M239; -.
DR STRING; 883112.HMPREF9707_00262; -.
DR PATRIC; fig|883112.3.peg.261; -.
DR eggNOG; COG0095; Bacteria.
DR HOGENOM; CLU_022986_0_2_9; -.
DR UniPathway; UPA00537; UER00594.
DR Proteomes; UP000005147; 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:EKB58367.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000005147};
KW Transferase {ECO:0000313|EMBL:EKB58367.1}.
FT DOMAIN 27..209
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51733"
SQ SEQUENCE 335 AA; 38286 MW; C183F6A971BB9371 CRC64;
MIFVDNGQNY DADLNIALET YLVENKLVDE PILLFYINKP SIIVGRNQNT AEEINQTYVD
EHGINVVRRM SGGGAVYHDL GNVSFCFIKD DDGSFRDFAS FTKPVIQALH KMGATGAVLE
GRNDLLIDGK KFSGNAMYAK DGRMTAHGTI LFDSDLDEVT NALKPRKAKI ESKGVKSIRS
RVTNLKPYVS EEYKDLTIEE FRDRLLLEIF GVDRREDVPE LKLTDKDWEG VMKIREERMG
NWDWNYGQSP DFQYEQSHKF PFGFVDVRFN VRQGKMQDVR IYGDFFGLGN ISDVEAKLEG
VKYERQAVIE ALKDVDVVHY FGKTTVEEIV ELIFA
//
