ID   KHSE_STRR6              Reviewed;         289 AA.
AC   P0A3L8; P72535;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Homoserine kinase;
DE            Short=HK;
DE            Short=HSK;
DE            EC=2.7.1.39;
GN   Name=thrB; OrderedLocusNames=spr1218;
OS   Streptococcus pneumoniae (strain ATCC BAA-255 / R6).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=171101;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8755589; DOI=10.1073/pnas.93.15.7985;
RA   Wizemann T.M., Moskovitz J., Pearce B.J., Cundell D., Arvidson C.G., So M.,
RA   Weissbach H., Brot N., Masure H.R.;
RT   "Peptide methionine sulfoxide reductase contributes to the maintenance of
RT   adhesins in three major pathogens.";
RL   Proc. Natl. Acad. Sci. U.S.A. 93:7985-7990(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-255 / R6;
RX   PubMed=11544234; DOI=10.1128/jb.183.19.5709-5717.2001;
RA   Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S.,
RA   DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C.,
RA   Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E., LeBlanc D.J.,
RA   Lee L.N., Lefkowitz E.J., Lu J., Matsushima P., McAhren S.M., McHenney M.,
RA   McLeaster K., Mundy C.W., Nicas T.I., Norris F.H., O'Gara M., Peery R.B.,
RA   Robertson G.T., Rockey P., Sun P.-M., Winkler M.E., Yang Y.,
RA   Young-Bellido M., Zhao G., Zook C.A., Baltz R.H., Jaskunas S.R.,
RA   Rosteck P.R. Jr., Skatrud P.L., Glass J.I.;
RT   "Genome of the bacterium Streptococcus pneumoniae strain R6.";
RL   J. Bacteriol. 183:5709-5717(2001).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U41735; AAC44297.1; -; Genomic_DNA.
DR   EMBL; AE007317; AAL00022.1; -; Genomic_DNA.
DR   PIR; A98024; A98024.
DR   RefSeq; NP_358811.1; NC_003098.1.
DR   RefSeq; WP_000692438.1; NC_003098.1.
DR   AlphaFoldDB; P0A3L8; -.
DR   SMR; P0A3L8; -.
DR   STRING; 171101.spr1218; -.
DR   EnsemblBacteria; AAL00022; AAL00022; spr1218.
DR   GeneID; 60233312; -.
DR   GeneID; 66806477; -.
DR   KEGG; spr:spr1218; -.
DR   PATRIC; fig|171101.6.peg.1323; -.
DR   eggNOG; COG0083; Bacteria.
DR   HOGENOM; CLU_041243_0_0_9; -.
DR   OMA; CANRIPH; -.
DR   UniPathway; UPA00050; UER00064.
DR   Proteomes; UP000000586; 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..289
FT                   /note="Homoserine kinase"
FT                   /id="PRO_0000156620"
FT   BINDING         79..89
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        32
FT                   /note="C -> S (in Ref. 1; AAC44297)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        58
FT                   /note="K -> T (in Ref. 1; AAC44297)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   289 AA;  31548 MW;  BA1BBA895A72BD18 CRC64;
     MKIIVPATSA NIGPGFDSVG VAVTKYLQIE VCEERDEWLI EHQIGKWIPH DERNLLLKIA
     LQIVPDLQPR RLKMTSDVPL ARGLGSSSSV IVAGIELANQ LGQLNLSDHE KLQLATKIEG
     HPDNVAPAIY GNLVIASSVE GQVSAIVADF PECDFLAYIP NYELRTRDSR SVLPKKLSYK
     EAVAASSIAN VAVAALLAGD MVTAGQAIEG DLFHERYRQD LVREFAMIKQ VTKENGAYAT
     YLSGAGPTVM VLASHDKMPT IKAELEKQPF KGKLHDLRVD TQGVRVEAK