ID   LPLA_MYCPN              Reviewed;         339 AA.
AC   P75394;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Probable lipoate-protein ligase A;
DE            Short=Lipoate--protein ligase;
DE            EC=6.3.1.20;
GN   Name=lplA; OrderedLocusNames=MPN_389; ORFNames=MP449;
OS   Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS   pneumoniae).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=272634;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29342 / M129;
RX   PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA   Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT   "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT   pneumoniae.";
RL   Nucleic Acids Res. 24:4420-4449(1996).
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; U00089; AAB96097.1; -; Genomic_DNA.
DR   PIR; S73775; S73775.
DR   RefSeq; NP_110077.1; NC_000912.1.
DR   RefSeq; WP_010874745.1; NC_000912.1.
DR   AlphaFoldDB; P75394; -.
DR   SMR; P75394; -.
DR   STRING; 272634.MPN_389; -.
DR   EnsemblBacteria; AAB96097; AAB96097; MPN_389.
DR   KEGG; mpn:MPN_389; -.
DR   PATRIC; fig|272634.6.peg.420; -.
DR   HOGENOM; CLU_022986_0_2_14; -.
DR   OMA; RTCPEDD; -.
DR   BioCyc; MPNE272634:G1GJ3-616-MON; -.
DR   UniPathway; UPA00537; UER00594.
DR   UniPathway; UPA00537; UER00595.
DR   Proteomes; UP000000808; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0009249; P:protein lipoylation; IEA:InterPro.
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..339
FT                   /note="Probable lipoate-protein ligase A"
FT                   /id="PRO_0000209568"
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   339 AA;  39194 MW;  DE2C78A4924E4FEA CRC64;
     MKTYILTSPK NIPYFNAALE EWLLTEFKKG EEIKVIYFWQ NANTIVVGRN QNTYAEVNLS
     EVEKDKVNLF RRFSGGGAVF HDMGNICFSI ILPKAKKEME NAYEETTRNV VKFLNSVGVP
     AQFHGRNDLE IEGKKFSGLA EYLSKDRVLV HGTLLFDTDF TKLAKYLNVD KTKMVSKGIE
     SVQKRVVNVK EYLPNLSTPT FLEKMVQFFT ETEHAETIHL DESSIKMVEK RAQEHFQSWD
     WNFGKTADYN FKNKKRFEGA GIFECNVQVD QGKVVDIKFY GDFLSVIDIT PVTQQLVGQK
     YDYQTFAKIL GNIDNFKEYF GTLTPQQMLE VIFDNKKDE