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Database: UniProt/SWISS-PROT
Entry: ISPE_STAAS
LinkDB: ISPE_STAAS
Original site: ISPE_STAAS 
ID   ISPE_STAAS              Reviewed;         282 AA.
AC   Q6GBZ3;
DT   21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   14-MAY-2014, entry version 62.
DE   RecName: Full=4-diphosphocytidyl-2-C-methyl-D-erythritol kinase;
DE            Short=CMK;
DE            EC=2.7.1.148;
DE   AltName: Full=4-(cytidine-5'-diphospho)-2-C-methyl-D-erythritol kinase;
GN   Name=ispE; OrderedLocusNames=SAS0452;
OS   Staphylococcus aureus (strain MSSA476).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus.
OX   NCBI_TaxID=282459;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MSSA476;
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T.,
RA   Churcher C., Clark L., Corton C., Cronin A., Doggett J., Dowd L.,
RA   Feltwell T., Hance Z., Harris B., Hauser H., Holroyd S., Jagels K.,
RA   James K.D., Lennard N., Line A., Mayes R., Moule S., Mungall K.,
RA   Ormond D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Sanders M.,
RA   Sharp S., Simmonds M., Stevens K., Whitehead S., Barrell B.G.,
RA   Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains:
RT   evidence for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
CC   -!- FUNCTION: Catalyzes the phosphorylation of the position 2 hydroxy
CC       group of 4-diphosphocytidyl-2C-methyl-D-erythritol (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + 4-(cytidine 5'-diphospho)-2-C-methyl-D-
CC       erythritol = ADP + 2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-
CC       D-erythritol.
CC   -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate
CC       biosynthesis via DXP pathway; isopentenyl diphosphate from 1-
CC       deoxy-D-xylulose 5-phosphate: step 3/6.
CC   -!- SIMILARITY: Belongs to the GHMP kinase family. IspE subfamily.
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DR   EMBL; BX571857; CAG42227.1; -; Genomic_DNA.
DR   RefSeq; YP_042580.1; NC_002953.3.
DR   ProteinModelPortal; Q6GBZ3; -.
DR   SMR; Q6GBZ3; 6-250.
DR   STRING; 282459.SAS0452; -.
DR   GeneID; 2861827; -.
DR   KEGG; sas:SAS0452; -.
DR   PATRIC; 19550276; VBIStaAur96780_0472.
DR   eggNOG; COG1947; -.
DR   HOGENOM; HOG000019600; -.
DR   KO; K00919; -.
DR   OMA; YHEIRTI; -.
DR   OrthoDB; EOG62VNQ2; -.
DR   UniPathway; UPA00056; UER00094.
DR   GO; GO:0050515; F:4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol kinase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0019288; P:isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway; IEA:UniProtKB-UniPathway.
DR   GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-HAMAP.
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; 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; PTHR20861:SF2; PTHR20861: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; Complete proteome; Isoprene biosynthesis; Kinase;
KW   Nucleotide-binding; Transferase.
FT   CHAIN         1    282       4-diphosphocytidyl-2-C-methyl-D-
FT                                erythritol kinase.
FT                                /FTId=PRO_0000189265.
FT   NP_BIND      93    103       ATP (Potential).
FT   ACT_SITE      9      9       By similarity.
FT   ACT_SITE    135    135       By similarity.
SQ   SEQUENCE   282 AA;  31442 MW;  C8A851AFCC4385AE CRC64;
     MIYETAPAKI NFTLDTLFKR NDGYHEIEMI MTTVDLNDRL TFHKRKDRKI VVEIEHNYVP
     SNHKNLAYRA AQLFIEQYQL KQGVTISIDK EIPVSAGLAG GSADAAATLR GLNRLFDIGA
     SLEELALLGS KIGTDIPFCI YNKTALCTGR GEKIEFLNKP PSAWVILAKP NLGISSPDIF
     KLINLDKRYD VHTKMCYEAL ENRDYQQLCQ SLSNRLEPIS VSKHPQIDKL KNNMLKSGAD
     GALMSGSGPT VYGLARKESQ AKNIYNAVNG CCNEVYLVRL LG
//
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