ID   KHSE_STAAW              Reviewed;         304 AA.
AC   Q8NWV8;
DT   19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   19-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Homoserine kinase {ECO:0000255|HAMAP-Rule:MF_00384};
DE            Short=HK {ECO:0000255|HAMAP-Rule:MF_00384};
DE            Short=HSK {ECO:0000255|HAMAP-Rule:MF_00384};
DE            EC=2.7.1.39 {ECO:0000255|HAMAP-Rule:MF_00384};
GN   Name=thrB {ECO:0000255|HAMAP-Rule:MF_00384}; OrderedLocusNames=MW1217;
OS   Staphylococcus aureus (strain MW2).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=196620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MW2;
RX   PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA   Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA   Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT   "Genome and virulence determinants of high virulence community-acquired
RT   MRSA.";
RL   Lancet 359:1819-1827(2002).
CC   -!- FUNCTION: Catalyzes the ATP-dependent phosphorylation of L-homoserine
CC       to L-homoserine phosphate. {ECO:0000255|HAMAP-Rule:MF_00384}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-homoserine = ADP + H(+) + O-phospho-L-homoserine;
CC         Xref=Rhea:RHEA:13985, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:57476, ChEBI:CHEBI:57590, ChEBI:CHEBI:456216;
CC         EC=2.7.1.39; Evidence={ECO:0000255|HAMAP-Rule:MF_00384};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC       from L-aspartate: step 4/5. {ECO:0000255|HAMAP-Rule:MF_00384}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00384}.
CC   -!- SIMILARITY: Belongs to the GHMP kinase family. Homoserine kinase
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00384}.
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DR   EMBL; BA000033; BAB95082.1; -; Genomic_DNA.
DR   RefSeq; WP_000073182.1; NC_003923.1.
DR   AlphaFoldDB; Q8NWV8; -.
DR   SMR; Q8NWV8; -.
DR   EnsemblBacteria; BAB95082; BAB95082; BAB95082.
DR   KEGG; sam:MW1217; -.
DR   HOGENOM; CLU_041243_0_0_9; -.
DR   OMA; CANRIPH; -.
DR   UniPathway; UPA00050; UER00064.
DR   Proteomes; UP000000418; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004413; F:homoserine kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.30.70.890; -; 1.
DR   HAMAP; MF_00384; Homoser_kinase; 1.
DR   InterPro; IPR013750; GHMP_kinase_C_dom.
DR   InterPro; IPR036554; GHMP_kinase_C_sf.
DR   InterPro; IPR006204; GHMP_kinase_N_dom.
DR   InterPro; IPR006203; GHMP_knse_ATP-bd_CS.
DR   InterPro; IPR000870; Homoserine_kinase.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR   Pfam; PF08544; GHMP_kinases_C; 1.
DR   Pfam; PF00288; GHMP_kinases_N; 1.
DR   PIRSF; PIRSF000676; Homoser_kin; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   SUPFAM; SSF55060; SSF55060; 1.
DR   TIGRFAMs; TIGR00191; thrB; 1.
DR   PROSITE; PS00627; GHMP_KINASES_ATP; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; ATP-binding; Cytoplasm; Kinase;
KW   Nucleotide-binding; Threonine biosynthesis; Transferase.
FT   CHAIN           1..304
FT                   /note="Homoserine kinase"
FT                   /id="PRO_0000156609"
FT   BINDING         90..100
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00384"
SQ   SEQUENCE   304 AA;  33293 MW;  BB6FB6F501B9DAE9 CRC64;
     MSNVLELTIP ASTANLGVGF DSIGMALDKF LHLSVKETSG TKWEYIFHDD ASKQLPTDET
     NFIYHVAQQV ASKYSVDLPN LCIEMRSDIP LARGLGSSAS ALVGAIYIAN YFGDIQLSKH
     EVLQLATEIE GHPDNVAPTI YGGLIAGYYN DVSKETSVAH IDIPDVDVIV TIPTYELKTE
     ASRRALPQKL THSEAVKSSA ISNTMICALA QHNYELAGKL MQQDGFHEPY RQHLIAEFDE
     VKTIAIQHNA YATVISGAGP TILIFSRKEN SGELVRSLNS QVVSCHSELV DINISGVKER
     IVYQ