ID   Y2167_STAHJ             Reviewed;         308 AA.
AC   Q4L4E9;
DT   13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Putative lipid kinase SH2167;
DE            EC=2.7.1.-;
GN   OrderedLocusNames=SH2167;
OS   Staphylococcus haemolyticus (strain JCSC1435).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=279808;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCSC1435;
RX   PubMed=16237012; DOI=10.1128/jb.187.21.7292-7308.2005;
RA   Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA   Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA   Hiramatsu K.;
RT   "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT   extreme plasticity of its genome and the evolution of human-colonizing
RT   staphylococcal species.";
RL   J. Bacteriol. 187:7292-7308(2005).
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; AP006716; BAE05476.1; -; Genomic_DNA.
DR   RefSeq; WP_011276429.1; NC_007168.1.
DR   AlphaFoldDB; Q4L4E9; -.
DR   SMR; Q4L4E9; -.
DR   STRING; 279808.SH2167; -.
DR   EnsemblBacteria; BAE05476; BAE05476; SH2167.
DR   KEGG; sha:SH2167; -.
DR   eggNOG; COG1597; Bacteria.
DR   HOGENOM; CLU_045532_1_0_9; -.
DR   OMA; LPGGTCN; -.
DR   OrthoDB; 869726at2; -.
DR   Proteomes; UP000000543; Chromosome.
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..308
FT                   /note="Putative lipid kinase SH2167"
FT                   /id="PRO_0000386521"
FT   DOMAIN          1..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   308 AA;  34054 MW;  621BAE42528BBE8E CRC64;
     MGQKFNHGVL FYHEHSGLKD IYEGLGEVTK SLTTMCKHLS IQLSENEGDI IKYCERIKNQ
     EYSSDVDIVF ILGGDGTVNE LVNGVLANDL NVPIGIIPGG TFNDFTKTLN LNPNFSKASE
     QLKTSHLESY DVMKVNGTYV LNFVGLGLIV QNAENVQEGR KDIFGKLSYV GSTVKTLMNP
     EDFDYTLTVD DKELNGNTSM LVVANGPNIG GSRIPLMDLS PQDGKLNSFI FDKQSFTILN
     DVFKKRDSMD WNEITNGIDH IAGKHITLST DPVMKVDIDG EISLETPITI EVLPKALQIL
     TFPENAEQ