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Database: UniProt
Entry: A0A117M2V2_9BACT
LinkDB: A0A117M2V2_9BACT
Original site: A0A117M2V2_9BACT 
ID   A0A117M2V2_9BACT        Unreviewed;       334 AA.
AC   A0A117M2V2;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=lipoate--protein ligase {ECO:0000256|ARBA:ARBA00012367};
DE            EC=6.3.1.20 {ECO:0000256|ARBA:ARBA00012367};
GN   ORFNames=XD94_0522 {ECO:0000313|EMBL:KUK81311.1};
OS   Mesotoga prima.
OC   Bacteria; Thermotogota; Thermotogae; Kosmotogales; Kosmotogaceae; Mesotoga.
OX   NCBI_TaxID=1184387 {ECO:0000313|EMBL:KUK81311.1, ECO:0000313|Proteomes:UP000054092};
RN   [1] {ECO:0000313|Proteomes:UP000054092}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=26787827; DOI=10.1128/mbio.01669-15;
RA   Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA   Andersen G.L., Banfield J.F.;
RT   "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate Phyla and
RT   Other Microbial Community Members in Biogeochemical Transformations in Oil
RT   Reservoirs.";
RL   MBio 7:e01669-15(2015).
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:KUK81311.1}.
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DR   EMBL; LGGP01000066; KUK81311.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A117M2V2; -.
DR   PATRIC; fig|1184387.3.peg.867; -.
DR   UniPathway; UPA00537; UER00594.
DR   Proteomes; UP000054092; 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:KUK81311.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Transferase {ECO:0000313|EMBL:KUK81311.1}.
FT   DOMAIN          35..218
FT                   /note="BPL/LPL catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51733"
SQ   SEQUENCE   334 AA;  38397 MW;  6F561CFD05D3AF45 CRC64;
     MSEVGKIPST IFVESDSFDP WLNLAVEEYL LNSFAKENIV LYLWQNENTV VIGRNQNAWQ
     ECRLDNLHRD GGKLARRLSG GGAVFHDLGN LNFTFLLPKR EYDLHRQLSV IVDGVKSVGI
     DAHFSGRNDI LAEGRKFSGN AFYHGQYASY HHGTILVDVD TRRLSEYLNV SRAKIESKGV
     KSVVSRVVNL RELKPDLTIE RMKEAMYRGF AEEYGRIYEV LDFDELRKSL DVKSLYEKYS
     SKEWLLGKSP EFNFKIGNRF SWGGIELLFT SKKGIISDVI IYSDSMDVDF IEQLKRELIR
     VEFSRVAIVK AIEMLPDCSE RNDIIAWLQT TDLN
//
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