ID   ISPE_NEIMB              Reviewed;         281 AA.
AC   Q9JZW4;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=4-diphosphocytidyl-2-C-methyl-D-erythritol kinase {ECO:0000255|HAMAP-Rule:MF_00061};
DE            Short=CMK {ECO:0000255|HAMAP-Rule:MF_00061};
DE            EC=2.7.1.148 {ECO:0000255|HAMAP-Rule:MF_00061};
DE   AltName: Full=4-(cytidine-5'-diphospho)-2-C-methyl-D-erythritol kinase {ECO:0000255|HAMAP-Rule:MF_00061};
GN   Name=ispE {ECO:0000255|HAMAP-Rule:MF_00061}; OrderedLocusNames=NMB0874;
OS   Neisseria meningitidis serogroup B (strain MC58).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=122586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC58;
RX   PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA   Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E.,
RA   Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA   Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H.,
RA   Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M.,
RA   Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA   Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V.,
RA   Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA   Moxon E.R., Rappuoli R., Venter J.C.;
RT   "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT   MC58.";
RL   Science 287:1809-1815(2000).
CC   -!- FUNCTION: Catalyzes the phosphorylation of the position 2 hydroxy group
CC       of 4-diphosphocytidyl-2C-methyl-D-erythritol. {ECO:0000255|HAMAP-
CC       Rule:MF_00061}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-CDP-2-C-methyl-D-erythritol + ATP = 4-CDP-2-C-methyl-D-
CC         erythritol 2-phosphate + ADP + H(+); Xref=Rhea:RHEA:18437,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57823,
CC         ChEBI:CHEBI:57919, ChEBI:CHEBI:456216; EC=2.7.1.148;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00061};
CC   -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis
CC       via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-
CC       phosphate: step 3/6. {ECO:0000255|HAMAP-Rule:MF_00061}.
CC   -!- SIMILARITY: Belongs to the GHMP kinase family. IspE subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00061}.
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; AE002098; AAF41285.1; -; Genomic_DNA.
DR   PIR; B81149; B81149.
DR   RefSeq; NP_273915.1; NC_003112.2.
DR   RefSeq; WP_002222667.1; NC_003112.2.
DR   AlphaFoldDB; Q9JZW4; -.
DR   SMR; Q9JZW4; -.
DR   STRING; 122586.NMB0874; -.
DR   PaxDb; Q9JZW4; -.
DR   EnsemblBacteria; AAF41285; AAF41285; NMB0874.
DR   KEGG; nme:NMB0874; -.
DR   PATRIC; fig|122586.8.peg.1090; -.
DR   HOGENOM; CLU_053057_3_0_4; -.
DR   OMA; RWPSPAK; -.
DR   UniPathway; UPA00056; UER00094.
DR   Proteomes; UP000000425; Chromosome.
DR   GO; GO:0050515; F:4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol kinase activity; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019288; P:isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway; IEA:UniProtKB-UniPathway.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.30.70.890; -; 1.
DR   HAMAP; MF_00061; IspE; 1.
DR   InterPro; IPR013750; GHMP_kinase_C_dom.
DR   InterPro; IPR036554; GHMP_kinase_C_sf.
DR   InterPro; IPR006204; GHMP_kinase_N_dom.
DR   InterPro; IPR004424; IspE.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR   PANTHER; PTHR43527:SF2; PTHR43527:SF2; 1.
DR   Pfam; PF08544; GHMP_kinases_C; 1.
DR   Pfam; PF00288; GHMP_kinases_N; 1.
DR   PIRSF; PIRSF010376; IspE; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   SUPFAM; SSF55060; SSF55060; 1.
DR   TIGRFAMs; TIGR00154; ispE; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Isoprene biosynthesis; Kinase; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   CHAIN           1..281
FT                   /note="4-diphosphocytidyl-2-C-methyl-D-erythritol kinase"
FT                   /id="PRO_0000189238"
FT   ACT_SITE        15
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00061"
FT   ACT_SITE        140
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00061"
FT   BINDING         98..108
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00061"
SQ   SEQUENCE   281 AA;  31316 MW;  FBFA5216CC2B7703 CRC64;
     MNIADGRQAF SAPAKLNLDL RITGRREDGY HNIESIFCLI DLQDTVYLKP RDDGKIILHN
     PVDGMPQEVD LSYRAASLLQ KYARNPAGVE IWLDKKIPTG AGLGGGSSDA ATVLLVLNRW
     WQCGLTQRQL IDSGAALGAD VPFFIFGKNA FARGIGDRLD EMDIPKQWYV IVKPPVHVST
     AKIFTHESLT RNSASSIMPT FQNLQPFRND MQAVVFKEYP EVWKAYSELS RYGFALMTGS
     GACVFTACQD RNSAYNIYRQ VSDLYEAYLA EGLSKHPLLS V