ID   LPLA_MYCGE              Reviewed;         336 AA.
AC   P47512;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Probable lipoate-protein ligase A;
DE            Short=Lipoate--protein ligase;
DE            EC=6.3.1.20;
GN   Name=lplA; OrderedLocusNames=MG270;
OS   Mycoplasma genitalium (strain ATCC 33530 / DSM 19775 / NCTC 10195 / G37)
OS   (Mycoplasmoides genitalium).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=243273;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX   PubMed=7569993; DOI=10.1126/science.270.5235.397;
RA   Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A.,
RA   Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M.,
RA   Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L.,
RA   Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M.,
RA   Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S.,
RA   Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.;
RT   "The minimal gene complement of Mycoplasma genitalium.";
RL   Science 270:397-403(1995).
CC   -!- FUNCTION: Catalyzes both the ATP-dependent activation of exogenously
CC       supplied lipoate to lipoyl-AMP and the transfer of the activated lipoyl
CC       onto the lipoyl domains of lipoate-dependent enzymes. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-lipoate + ATP + L-lysyl-[lipoyl-carrier protein] = (R)-
CC         N(6)-lipoyl-L-lysyl-[lipoyl-carrier protein] + AMP + diphosphate +
CC         H(+); 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   -!- PATHWAY: Protein modification; protein lipoylation via exogenous
CC       pathway; protein N(6)-(lipoyl)lysine from lipoate: step 1/2.
CC   -!- PATHWAY: Protein modification; protein lipoylation via exogenous
CC       pathway; protein N(6)-(lipoyl)lysine from lipoate: step 2/2.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- MISCELLANEOUS: In the transfer reaction, the free carboxyl group of
CC       lipoic acid is attached via an amide linkage to the epsilon-amino group
CC       of a specific lysine residue of lipoyl domains of lipoate-dependent
CC       enzymes. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the LplA family. {ECO:0000305}.
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DR   EMBL; L43967; AAC71492.1; -; Genomic_DNA.
DR   PIR; H64229; H64229.
DR   RefSeq; WP_009885902.1; NZ_AAGX01000009.1.
DR   AlphaFoldDB; P47512; -.
DR   SMR; P47512; -.
DR   STRING; 243273.MG_270; -.
DR   EnsemblBacteria; AAC71492; AAC71492; MG_270.
DR   KEGG; mge:MG_270; -.
DR   eggNOG; COG0095; Bacteria.
DR   HOGENOM; CLU_022986_0_2_14; -.
DR   OMA; RTCPEDD; -.
DR   OrthoDB; 871298at2; -.
DR   BioCyc; MGEN243273:G1GJ2-328-MON; -.
DR   UniPathway; UPA00537; UER00594.
DR   UniPathway; UPA00537; UER00595.
DR   Proteomes; UP000000807; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016979; F:lipoate-protein ligase activity; IBA:GO_Central.
DR   GO; GO:0017118; F:lipoyltransferase activity; IBA:GO_Central.
DR   GO; GO:0009249; P:protein lipoylation; IBA:GO_Central.
DR   Gene3D; 3.30.930.10; -; 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   PANTHER; PTHR12561; PTHR12561; 1.
DR   Pfam; PF03099; BPL_LplA_LipB; 1.
DR   Pfam; PF10437; Lip_prot_lig_C; 1.
DR   SUPFAM; SSF55681; SSF55681; 1.
DR   TIGRFAMs; TIGR00545; lipoyltrans; 1.
DR   PROSITE; PS51733; BPL_LPL_CATALYTIC; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Ligase; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..336
FT                   /note="Probable lipoate-protein ligase A"
FT                   /id="PRO_0000209567"
FT   DOMAIN          30..217
FT                   /note="BPL/LPL catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01067"
FT   BINDING         72
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         77..80
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         135
FT                   /ligand="(R)-lipoate"
FT                   /ligand_id="ChEBI:CHEBI:83088"
FT                   /evidence="ECO:0000250"
FT   BINDING         135
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   336 AA;  38944 MW;  9804256E786E1E9C CRC64;
     MQTFIITSPV FNPYFNAALE EWLLTEFRKN ELVKVIYFWQ NANTIVVGRN QNTYAEVNLK
     ELESDKVNLF RRFSGGGAVF HDLGNICFSI ILPRTGKVME NAYEQTTRNV VKFLNSLNVP
     AVFHGRNDLE INNKKFSGLA EYIAKDRLLV HGTLLFDTDF SKLAKYLNVD KTKIASKGVD
     SVAKRVVNVK EYLPNWTTAK FLEEMINFFT VTEKAETIVL TKDALAKVEK RAKEHFQSWE
     WNFGKTYEYN FKNKRYFNNA GLFECNVQVE KGTVVDIKFY GDFLSVVDIT PVTKKLIGQK
     YDYKTFEKLF NELDHFSDYF GSLKPEQLLG VIFDNK