Y723_STAA1
ID Y723_STAA1 Reviewed; 305 AA.
AC A7WZL3;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Putative lipid kinase SAHV_0723;
DE EC=2.7.1.-;
GN OrderedLocusNames=SAHV_0723;
OS Staphylococcus aureus (strain Mu3 / ATCC 700698).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=418127;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mu3 / ATCC 700698;
RX PubMed=17954695; DOI=10.1128/aac.00534-07;
RA Neoh H.-M., Cui L., Yuzawa H., Takeuchi F., Matsuo M., Hiramatsu K.;
RT "Mutated response regulator graR is responsible for phenotypic conversion
RT of Staphylococcus aureus from heterogeneous vancomycin-intermediate
RT resistance to vancomycin-intermediate resistance.";
RL Antimicrob. Agents Chemother. 52:45-53(2008).
CC -!- FUNCTION: May catalyze the ATP-dependent phosphorylation of lipids
CC other than diacylglycerol (DAG). {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. This ion appears to have a
CC structural role and is required for catalytic activity. {ECO:0000250};
CC -!- SIMILARITY: Belongs to the diacylglycerol/lipid kinase family.
CC {ECO:0000305}.
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DR EMBL; AP009324; BAF77606.1; -; Genomic_DNA.
DR RefSeq; WP_000429006.1; NC_009782.1.
DR AlphaFoldDB; A7WZL3; -.
DR SMR; A7WZL3; -.
DR KEGG; saw:SAHV_0723; -.
DR HOGENOM; CLU_045532_1_0_9; -.
DR OMA; LPGGTCN; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003951; F:NAD+ kinase activity; IEA:InterPro.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.10330; -; 1.
DR InterPro; IPR017438; ATP-NAD_kinase_N.
DR InterPro; IPR005218; Diacylglycerol/lipid_kinase.
DR InterPro; IPR001206; Diacylglycerol_kinase_cat_dom.
DR InterPro; IPR016064; NAD/diacylglycerol_kinase_sf.
DR InterPro; IPR045540; YegS/DAGK_C.
DR Pfam; PF00781; DAGK_cat; 1.
DR Pfam; PF19279; YegS_C; 1.
DR SMART; SM00046; DAGKc; 1.
DR SUPFAM; SSF111331; SSF111331; 1.
DR TIGRFAMs; TIGR00147; TIGR00147; 1.
DR PROSITE; PS50146; DAGK; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Lipid biosynthesis; Lipid metabolism; Magnesium;
KW Metal-binding; Nucleotide-binding; Phospholipid biosynthesis;
KW Phospholipid metabolism; Transferase.
FT CHAIN 1..305
FT /note="Putative lipid kinase SAHV_0723"
FT /id="PRO_0000386505"
FT DOMAIN 3..139
FT /note="DAGKc"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT ACT_SITE 281
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 44
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT BINDING 74..80
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT BINDING 101
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT BINDING 220
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 223
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 225
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 305 AA; 33612 MW; E9231EF30BE43192 CRC64;
MENKYTHGVL FYHEHSGLKN INQGIGEVTT ALSSICKHLS IQLSENEGDI IKYCQEIKTK
NYAKDVDILF ILGGDGTVNE LINGVMSHDL QLPIGILPGG TFNDFTKTLN IAPNHKQASE
QMISAQVGTY DVIKINNQYA LNFVGLGLIV QNAENVQDGS KDIFGKLSYI GSTVKTLLNP
TQFNYQLSID DKTYSGETTM ILTANGPFIG GSRIPLTDLS PQDGELNTFI FNEQSFSILN
DIFKKRDSMN WNEITQGIEH IPGKKISLTT DPAMKVDIDG EISLETPIDI EVIPNAIQLL
TVNDL