LPLA2_STRPG
ID LPLA2_STRPG Reviewed; 339 AA.
AC P0DN72;
DT 20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2016, sequence version 1.
DT 03-AUG-2022, entry version 23.
DE RecName: Full=Lipoate--protein ligase {ECO:0000303|PubMed:26166706};
DE EC=6.3.1.20 {ECO:0000269|PubMed:26166706};
DE AltName: Full=LplA2 {ECO:0000303|PubMed:26166706};
GN Name=lplA {ECO:0000312|EMBL:CAM30198.1};
GN OrderedLocusNames=SpyM50870 {ECO:0000312|EMBL:CAM30198.1};
OS Streptococcus pyogenes serotype M5 (strain Manfredo).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=160491;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Manfredo;
RX PubMed=17012393; DOI=10.1128/jb.01227-06;
RA Holden M.T.G., Scott A., Cherevach I., Chillingworth T., Churcher C.,
RA Cronin A., Dowd L., Feltwell T., Hamlin N., Holroyd S., Jagels K.,
RA Moule S., Mungall K., Quail M.A., Price C., Rabbinowitsch E., Sharp S.,
RA Skelton J., Whitehead S., Barrell B.G., Kehoe M., Parkhill J.;
RT "Complete genome of acute rheumatic fever-associated serotype M5
RT Streptococcus pyogenes strain Manfredo.";
RL J. Bacteriol. 189:1473-1477(2007).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ASP-128 AND LYS-134, AND
RP PATHWAY.
RC STRAIN=Manfredo;
RX PubMed=26166706; DOI=10.1016/j.molcel.2015.06.013;
RA Rack J.G., Morra R., Barkauskaite E., Kraehenbuehl R., Ariza A., Qu Y.,
RA Ortmayer M., Leidecker O., Cameron D.R., Matic I., Peleg A.Y., Leys D.,
RA Traven A., Ahel I.;
RT "Identification of a class of protein ADP-ribosylating sirtuins in
RT microbial pathogens.";
RL Mol. Cell 59:309-320(2015).
CC -!- FUNCTION: Catalyzes specifically the lipoylation of GcvH-L (SpyM50867),
CC likely via the ATP-dependent activation of lipoate to lipoyl-AMP and
CC the transfer of the activated lipoyl onto the lipoyl domain of the
CC target protein. {ECO:0000269|PubMed:26166706}.
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 Evidence={ECO:0000269|PubMed:26166706};
CC -!- PATHWAY: Protein modification; protein lipoylation via exogenous
CC pathway; protein N(6)-(lipoyl)lysine from lipoate: step 1/2.
CC {ECO:0000305|PubMed:26166706}.
CC -!- PATHWAY: Protein modification; protein lipoylation via exogenous
CC pathway; protein N(6)-(lipoyl)lysine from lipoate: step 2/2.
CC {ECO:0000305|PubMed:26166706}.
CC -!- SIMILARITY: Belongs to the LplA family. {ECO:0000305}.
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DR EMBL; AM295007; CAM30198.1; -; Genomic_DNA.
DR RefSeq; WP_011184541.1; NC_009332.1.
DR AlphaFoldDB; P0DN72; -.
DR SMR; P0DN72; -.
DR KEGG; spf:SpyM50870; -.
DR HOGENOM; CLU_022986_0_2_9; -.
DR OMA; NGAMTHG; -.
DR UniPathway; UPA00537; UER00594.
DR UniPathway; UPA00537; UER00595.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016979; F:lipoate-protein ligase activity; IDA:UniProtKB.
DR GO; GO:0009249; P:protein lipoylation; IDA:UniProtKB.
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 1: Evidence at protein level;
KW ATP-binding; Ligase; Nucleotide-binding.
FT CHAIN 1..339
FT /note="Lipoate--protein ligase"
FT /id="PRO_0000435348"
FT DOMAIN 31..221
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01067"
FT BINDING 73
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9HKT1"
FT BINDING 78..81
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9HKT1"
FT BINDING 135
FT /ligand="(R)-lipoate"
FT /ligand_id="ChEBI:CHEBI:83088"
FT /evidence="ECO:0000250|UniProtKB:Q9HKT1"
FT BINDING 135
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9HKT1"
FT BINDING 139
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9HKT1"
FT MUTAGEN 128
FT /note="D->A: Reduces enzymatic activity."
FT /evidence="ECO:0000269|PubMed:26166706"
FT MUTAGEN 134
FT /note="K->R: Reduces enzymatic activity."
FT /evidence="ECO:0000269|PubMed:26166706"
SQ SEQUENCE 339 AA; 38252 MW; 79508766202576E1 CRC64;
MYLIEPIRNG KRITDGAVAL AMQVYVQENL FLDDDILFPY YCDPKVEIGK FQNAVVETNQ
EYLKEHHIPV VRRDTGGGAV YVDSGAVNIC YLINDNGVFG DFKRTYQPAI EALHHLGATG
VEMSGRNDLV IDGKKVSGAA MTIANGRVYG GYSLLLDVDF EAMEKALKPN RKKIESKGIR
SVRSRVGNIR EHLAPQYQGI TIEEFKDLMI CQLLQIETIS QAKRYDLTEK DWQQIDALTE
RKYHNWEWNY GNAPQYRYHR DGRFTGGTVD IHLDIKKGYI AACRIYGDFF GKADIAELEG
HLIGTRMEKE DVLATLNAID LAPYLGAITA EELGDLIFS
