ID A0A091C559_9ENTE Unreviewed; 334 AA.
AC A0A091C559;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=lipoate--protein ligase {ECO:0000256|ARBA:ARBA00012367};
DE EC=6.3.1.20 {ECO:0000256|ARBA:ARBA00012367};
GN ORFNames=TMU3MR103_0686 {ECO:0000313|EMBL:KFN92044.1};
OS Tetragenococcus muriaticus 3MR10-3.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Tetragenococcus.
OX NCBI_TaxID=1302648 {ECO:0000313|EMBL:KFN92044.1, ECO:0000313|Proteomes:UP000029381};
RN [1] {ECO:0000313|EMBL:KFN92044.1, ECO:0000313|Proteomes:UP000029381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3MR10-3 {ECO:0000313|EMBL:KFN92044.1,
RC ECO:0000313|Proteomes:UP000029381};
RA Chuea-nongthon C., Rodtong S., Yongsawatdigul J., Steele J.L., Liu X.-y.,
RA Speers J., Glasner J.D., Neeno-Eckwall E.C.;
RT "Genome sequence of Tetragenococcus muriaticus.";
RL Submitted (AUG-2014) 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:KFN92044.1}.
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DR EMBL; JPVT01000064; KFN92044.1; -; Genomic_DNA.
DR RefSeq; WP_028789658.1; NZ_JPVT01000064.1.
DR AlphaFoldDB; A0A091C559; -.
DR PATRIC; fig|1302648.3.peg.667; -.
DR UniPathway; UPA00537; UER00594.
DR Proteomes; UP000029381; 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:KFN92044.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000029381};
KW Transferase {ECO:0000313|EMBL:KFN92044.1}.
FT DOMAIN 26..209
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51733"
SQ SEQUENCE 334 AA; 38767 MW; 6076503F5CEB1061 CRC64;
MIYVPNENND PRVNLAIENY LLDEMRTDEP ILLFYINEPS IIIGRNQNTF EEINQEYVDE
HGIHVVRRLS GGGAVYHDLG NLNYSFITPD DGNSFRNFAR FTEPVIKALH DIGVTNAYLK
GRNDLVIDDM KFSGNAMYST NGRMYAHGTL MLDSDKNEVT NALKVRKDKI ESKGVKSIRS
RVTNIKPFLP KENQDMTTEE FKEEILLKIF GVDSVDEVNT YELTDEDWQK IQEYTDKYYG
NWDWNYGHSP EFNVERYKRF SIGSIDIRLN VQEGKIANAK IYGDFFGLGD IKDVEDKLIG
TRYEKEALKK VVDTIDVKKY FGDMENKELF DLIY
//
