LPLA1_STAAM
ID LPLA1_STAAM Reviewed; 328 AA.
AC A0A0H3JR16;
DT 20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 03-AUG-2022, entry version 33.
DE RecName: Full=Lipoate--protein ligase 1 {ECO:0000303|PubMed:26166706};
DE EC=6.3.1.20 {ECO:0000269|PubMed:26166706};
DE AltName: Full=LplA1 {ECO:0000303|PubMed:26166706};
GN OrderedLocusNames=SAV1028 {ECO:0000312|EMBL:BAB57190.1};
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 {ECO:0000312|Proteomes:UP000002481};
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, AND CATALYTIC ACTIVITY.
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 the lipoylation of proteins, such as GcvH (SAV0833)
CC and GcvH-L (SAV0324), likely via the ATP-dependent activation of
CC lipoate to lipoyl-AMP and the transfer of the activated lipoyl onto the
CC lipoyl domain of the 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}.
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DR EMBL; BA000017; BAB57190.1; -; Genomic_DNA.
DR RefSeq; WP_000668818.1; NC_002758.2.
DR AlphaFoldDB; A0A0H3JR16; -.
DR SMR; A0A0H3JR16; -.
DR PaxDb; A0A0H3JR16; -.
DR EnsemblBacteria; BAB57190; BAB57190; SAV1028.
DR KEGG; sav:SAV1028; -.
DR HOGENOM; CLU_022986_0_2_9; -.
DR OMA; RTCPEDD; -.
DR PhylomeDB; A0A0H3JR16; -.
DR BioCyc; SAUR158878:SAV_RS05550-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; Ligase; Nucleotide-binding.
FT CHAIN 1..328
FT /note="Lipoate--protein ligase 1"
FT /id="PRO_0000435346"
FT DOMAIN 27..214
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01067"
FT BINDING 69
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9HKT1"
FT BINDING 74..77
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9HKT1"
FT BINDING 131
FT /ligand="(R)-lipoate"
FT /ligand_id="ChEBI:CHEBI:83088"
FT /evidence="ECO:0000250|UniProtKB:Q9HKT1"
FT BINDING 131
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9HKT1"
SQ SEQUENCE 328 AA; 37870 MW; F68B80FFEC42589A CRC64;
MKFISNNNIT DPTLNLAMEE YVLKNLPAEE SYFLFYINRP SIIVGKNQNT IEEVNQTYID
AHNIDVVRRI SGGGAVYHDT GNLNFSFITD DDGNSFHNFQ KFTEPIVQAL QSLGVNAELT
GRNDIQVGQA KISGNAMVKV KNRMFSHGTL MLNSDLDEVQ NALKVNPAKI KSKGIKSVRK
RVANIQEFLN DPLEIEEFKK IILKTIFGET EVEEYKLTDE DWENIEKLSN DKYRTWAWNY
GRNPKYNFER EEKFEKGFVQ IKFDVKRGKI EHAKIFGDFF GVGDVTDLEN ALVGCLHDFE
HIEEALSEYD LYHYFGDIDR HELIRLMS
