ID   KHSE_BACSU              Reviewed;         309 AA.
AC   P04948; O32121;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   03-AUG-2022, entry version 150.
DE   RecName: Full=Homoserine kinase;
DE            Short=HK;
DE            Short=HSK;
DE            EC=2.7.1.39;
GN   Name=thrB; OrderedLocusNames=BSU32240;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=3098560; DOI=10.1002/j.1460-2075.1986.tb04600.x;
RA   Parsot C.;
RT   "Evolution of biosynthetic pathways: a common ancestor for threonine
RT   synthase, threonine dehydratase and D-serine dehydratase.";
RL   EMBO J. 5:3013-3019(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
CC   -!- FUNCTION: Catalyzes the ATP-dependent phosphorylation of L-homoserine
CC       to L-homoserine phosphate. {ECO:0000250}.
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;
CC   -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC       from L-aspartate: step 4/5.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the GHMP kinase family. Homoserine kinase
CC       subfamily. {ECO:0000305}.
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DR   EMBL; X04603; CAA28271.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB15214.1; -; Genomic_DNA.
DR   PIR; H69722; H69722.
DR   RefSeq; NP_391104.1; NC_000964.3.
DR   RefSeq; WP_003228699.1; NZ_JNCM01000033.1.
DR   AlphaFoldDB; P04948; -.
DR   SMR; P04948; -.
DR   STRING; 224308.BSU32240; -.
DR   PaxDb; P04948; -.
DR   PRIDE; P04948; -.
DR   DNASU; 936665; -.
DR   EnsemblBacteria; CAB15214; CAB15214; BSU_32240.
DR   GeneID; 936665; -.
DR   KEGG; bsu:BSU32240; -.
DR   PATRIC; fig|224308.179.peg.3490; -.
DR   eggNOG; COG0083; Bacteria.
DR   InParanoid; P04948; -.
DR   OMA; CANRIPH; -.
DR   PhylomeDB; P04948; -.
DR   BioCyc; BSUB:BSU32240-MON; -.
DR   UniPathway; UPA00050; UER00064.
DR   Proteomes; UP000001570; 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; Reference proteome; Threonine biosynthesis;
KW   Transferase.
FT   CHAIN           1..309
FT                   /note="Homoserine kinase"
FT                   /id="PRO_0000156554"
FT   BINDING         91..101
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        57..58
FT                   /note="PA -> R (in Ref. 1; CAA28271)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   309 AA;  33324 MW;  0661A7DEFAA5FFAC CRC64;
     MNEADMLFSV TVPGSTANLG PGFDSVGMAL SRYLKLTVFE SDKWSFEAET ETVAGIPAGT
     DNLIYQVAKR TADLYGKEMP PVHVKVWSDI PLARGLGSSA AAIVAAIELA DELCGLKLSE
     ADKLHLASLE EGHPDNAGAS LVGGLVIGLH EDDETQMIRV PNADIDVVVV IPFYEVLTRD
     ARDVLPKEFP YADAVKASAV SNILIAAIMS KDWPLVGKIM KKDMFHQPYR AMLVPELSKV
     EHVAEMKGAY GTALSGAGPT ILVMTEKGKG EELKEQLALH FPHCEVDALT VPKEGSIIER
     NPLYQVKSV