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Database: UniProt
Entry: R3U611_9ENTE
LinkDB: R3U611_9ENTE
Original site: R3U611_9ENTE 
ID   R3U611_9ENTE            Unreviewed;       334 AA.
AC   R3U611;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   RecName: Full=lipoate--protein ligase {ECO:0000256|ARBA:ARBA00012367};
DE            EC=6.3.1.20 {ECO:0000256|ARBA:ARBA00012367};
GN   ORFNames=UC3_00414 {ECO:0000313|EMBL:EOL48863.1};
OS   Enterococcus phoeniculicola ATCC BAA-412.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=1158610 {ECO:0000313|EMBL:EOL48863.1, ECO:0000313|Proteomes:UP000013785};
RN   [1] {ECO:0000313|EMBL:EOL48863.1, ECO:0000313|Proteomes:UP000013785}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-412 {ECO:0000313|EMBL:EOL48863.1,
RC   ECO:0000313|Proteomes:UP000013785};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Earl A.M., Gilmore M.S., Lebreton F., Walker B., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA   Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
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 Enterococcus phoeniculicola BAA-412.";
RL   Submitted (FEB-2013) 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:EOL48863.1}.
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DR   EMBL; AJAT01000007; EOL48863.1; -; Genomic_DNA.
DR   RefSeq; WP_010767089.1; NZ_KB946326.1.
DR   AlphaFoldDB; R3U611; -.
DR   STRING; 154621.RV11_GL003360; -.
DR   PATRIC; fig|1158610.3.peg.390; -.
DR   eggNOG; COG0095; Bacteria.
DR   HOGENOM; CLU_022986_0_2_9; -.
DR   OrthoDB; 9788148at2; -.
DR   UniPathway; UPA00537; UER00594.
DR   Proteomes; UP000013785; 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:EOL48863.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000013785};
KW   Transferase {ECO:0000313|EMBL:EOL48863.1}.
FT   DOMAIN          26..209
FT                   /note="BPL/LPL catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51733"
SQ   SEQUENCE   334 AA;  38205 MW;  50C10E2D35C9AACA CRC64;
     MIFVPNENND PRVNLAIETY LLKEFPLDEP ILLFYINEPS IIIGRNQNTI EEINVDYVEE
     HGIHVVRRLS GGGAVYHDYG NLNFSFIMPD DGNSFRDFAK VTQPIIQALH ELGIEGAELK
     GRNDLVINDM KFSGNAMYAT SGRMFAHGTI MFDSDVNEVV NALKVRKDKI ESKGIKSIRS
     RVTNIKPFLP EEKQGMTTKE FRQDILLKIF GVDSVDDVKT YELTEKDWVE INKISDEYYR
     NWDWNYGKSP EFDIEKRHRF PIGSIEIRLN VSNGEIVEAK IFGDFFGLGE ISDVENALVG
     VKYEKNAINE AVKAIDVKKY FGNIEVQDLA DLIY
//
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