Y675_STAAB
ID Y675_STAAB Reviewed; 305 AA.
AC Q2YSK5;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Putative lipid kinase SAB0675c;
DE EC=2.7.1.-;
GN OrderedLocusNames=SAB0675c;
OS Staphylococcus aureus (strain bovine RF122 / ET3-1).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=273036;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=bovine RF122 / ET3-1;
RX PubMed=17971880; DOI=10.1371/journal.pone.0001120;
RA Herron-Olson L., Fitzgerald J.R., Musser J.M., Kapur V.;
RT "Molecular correlates of host specialization in Staphylococcus aureus.";
RL PLoS ONE 2:E1120-E1120(2007).
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; AJ938182; CAI80363.1; -; Genomic_DNA.
DR RefSeq; WP_000429019.1; NC_007622.1.
DR AlphaFoldDB; Q2YSK5; -.
DR SMR; Q2YSK5; -.
DR KEGG; sab:SAB0675c; -.
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 SAB0675c"
FT /id="PRO_0000386510"
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; 33575 MW; C1A312B7DEBBED20 CRC64;
MENKYTHGVL FYHEHSGLKN INQGIGEVTT ALSSICKHLS IQLSENEGDI IKYCQEIKTK
NYAKDVDILF ILGGDGTVNE LINGVMTNDL QLPIGILPGG TFNDFTKTLN IAPNHKQASE
QMISAQVGTY DVIKINNQYA LNFVGLGLIV QNAENVQDGS KDIFGKLSYI GSTVKTLLNP
TQFNYQLSID DKTYSGETSM ILSANGPFIG GSRIPLTDLS PQDGELNTFI FNEQSFSILN
DIFKKRDSMN WNEITQGIEH IPGKKISLTT DPAMKVDIDG EISLETPIDI EVIPNAIQLL
TVNDL