LPLA2_STAAM
ID LPLA2_STAAM Reviewed; 340 AA.
AC A0A0H3JX98;
DT 20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 03-AUG-2022, entry version 31.
DE RecName: Full=Lipoate--protein ligase 2 {ECO:0000303|PubMed:26166706};
DE EC=6.3.1.20 {ECO:0000269|PubMed:26166706};
DE AltName: Full=LplA2 {ECO:0000303|PubMed:26166706};
GN OrderedLocusNames=SAV0327 {ECO:0000312|EMBL:BAB56489.1};
OS Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158878;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mu50 / ATCC 700699;
RX PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA Hiramatsu K.;
RT "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL Lancet 357:1225-1240(2001).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, MUTAGENESIS OF ASP-129
RP AND LYS-135, AND PATHWAY.
RC STRAIN=Mu50 / ATCC 700699;
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 (SAV0324),
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. Can also utilize lipoamide as substrate for GcvH-L
CC modification. {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; BA000017; BAB56489.1; -; Genomic_DNA.
DR RefSeq; WP_000280799.1; NC_002758.2.
DR AlphaFoldDB; A0A0H3JX98; -.
DR SMR; A0A0H3JX98; -.
DR PaxDb; A0A0H3JX98; -.
DR EnsemblBacteria; BAB56489; BAB56489; SAV0327.
DR KEGG; sav:SAV0327; -.
DR HOGENOM; CLU_022986_0_2_9; -.
DR OMA; NGAMTHG; -.
DR PhylomeDB; A0A0H3JX98; -.
DR BioCyc; SAUR158878:SAV_RS01820-MON; -.
DR UniPathway; UPA00537; UER00594.
DR UniPathway; UPA00537; UER00595.
DR Proteomes; UP000002481; Chromosome.
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; Coiled coil; Ligase; Nucleotide-binding.
FT CHAIN 1..340
FT /note="Lipoate--protein ligase 2"
FT /id="PRO_0000435347"
FT DOMAIN 31..222
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01067"
FT COILED 293..321
FT /evidence="ECO:0000255"
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 136
FT /ligand="(R)-lipoate"
FT /ligand_id="ChEBI:CHEBI:83088"
FT /evidence="ECO:0000250|UniProtKB:Q9HKT1"
FT BINDING 136
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9HKT1"
FT BINDING 140
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9HKT1"
FT MUTAGEN 129
FT /note="D->A: Reduces enzymatic activity."
FT /evidence="ECO:0000269|PubMed:26166706"
FT MUTAGEN 135
FT /note="K->R: Reduces enzymatic activity."
FT /evidence="ECO:0000269|PubMed:26166706"
SQ SEQUENCE 340 AA; 38921 MW; D96FF9AFB7F3601D CRC64;
MYLIEPIRNG EYITDGAIAL AMQVYVNQHI FLDEDILFPY YCDPKVEIGR FQNTAIEVNQ
DYIDKHSIQV VRRDTGGGAV YVDKGAVNMC CILEQDTSIY GDFQRFYQPA IKALHTLGAT
DVIQSGRNDL TLNGKKVSGA AMTLMNNRIY GGYSLLLDVN YEAMDKVLKP NRKKIASKGI
KSVRARVGHL REALDEKYRD ITIEEFKNLM VTQILGIDDI KEAKRYELTD ADWEAIDELA
DKKYKNWDWN YGKSPKYEYN RSERLSSGTV DITISVEQNR IADCRIYGDF FGQGDIKDVE
EALQGTKMTR EDLMHQLKQL DIVYYFGNVT VESLVEMILS
