ID   MURA2_STAHJ             Reviewed;         421 AA.
AC   Q4L7Y1;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   16-JUN-2009, entry version 32.
DE   RecName: Full=UDP-N-acetylglucosamine 1-carboxyvinyltransferase 2;
DE            EC=2.5.1.7;
DE   AltName: Full=Enoylpyruvate transferase 2;
DE   AltName: Full=UDP-N-acetylglucosamine enolpyruvyl transferase 2;
DE            Short=EPT 2;
GN   Name=murA2; Synonyms=murA; OrderedLocusNames=SH0935;
OS   Staphylococcus haemolyticus (strain JCSC1435).
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=279808;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16237012; DOI=10.1128/JB.187.21.7292-7308.2005;
RA   Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA   Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S.,
RA   Lee J.C., Hiramatsu K.;
RT   "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT   extreme plasticity of its genome and the evolution of human-colonizing
RT   staphylococcal species.";
RL   J. Bacteriol. 187:7292-7308(2005).
CC   -!- FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-
CC       acetylglucosamine (By similarity).
CC   -!- CATALYTIC ACTIVITY: Phosphoenolpyruvate + UDP-N-acetyl-D-
CC       glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-D-
CC       glucosamine.
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Probable).
CC   -!- SIMILARITY: Belongs to the EPSP synthase family. MurA subfamily.
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DR   EMBL; AP006716; BAE04244.1; -; Genomic_DNA.
DR   RefSeq; YP_252850.1; -.
DR   GeneID; 3482070; -.
DR   GenomeReviews; AP006716_GR; SH0935.
DR   KEGG; sha:SH0935; -.
DR   NMPDR; fig|279808.3.peg.1287; -.
DR   HOGENOM; Q4L7Y1; -.
DR   OMA; Q4L7Y1; VSRVYHL.
DR   BioCyc; SHAE279808:SH0935-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008760; F:UDP-N-acetylglucosamine 1-carboxyvinyltrans...; IEA:HAMAP.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007047; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:HAMAP.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   GO; GO:0019277; P:UDP-N-acetylgalactosamine biosynthetic process; IEA:InterPro.
DR   HAMAP; MF_00111; -; 1.
DR   InterPro; IPR001986; EPSP_synthase_core.
DR   InterPro; IPR005750; UDP_GlcNAc_COvinyl_MurA.
DR   Gene3D; G3DSA:3.65.10.10; EPSP_synthase; 1.
DR   PANTHER; PTHR21090:SF4; AcGlu_Tran_MurA; 1.
DR   Pfam; PF00275; EPSP_synthase; 1.
DR   ProDom; PD001867; EPSP_synth; 1.
DR   TIGRFAMs; TIGR01072; murA; 1.
PE   3: Inferred from homology;
KW   Cell cycle; Cell division; Cell shape;
KW   Cell wall biogenesis/degradation; Complete proteome; Cytoplasm;
KW   Peptidoglycan synthesis; Transferase.
FT   CHAIN         1    421       UDP-N-acetylglucosamine 1-
FT                                carboxyvinyltransferase 2.
FT                                /FTId=PRO_0000231267.
FT   ACT_SITE    119    119       Proton donor (By similarity).
FT   BINDING     119    119       Phosphoenolpyruvate (covalent) (By
FT                                similarity).
SQ   SEQUENCE   421 AA;  45236 MW;  94F97448C28A9CCB CRC64;
     MDKIVIKGGN RLTGEVKVEG AKNAVLPVLT ASLLASEGQS KLVNVPDLSD VVTINNVLST
     LNANVEYNKE EGAVLVDAST TLKEEAPYEY VSKMRASILV MGPLLARLGH AIVALPGGCA
     IGARPIEQHI KGFEALGAEI HLENGNIYAS TKDGLKGTDI HLDFPSVGAT QNIIMAASLA
     KGKTVIENVA KEPEIVDLAN YINEMGGKVT GAGTDTITIH GVEKLRGVEH SIIPDRIEAG
     TLIIAAAITR GDVFVRDAVK EHMTSLIYKL EEMGVNLDFQ EDGVRVTAED ELKPVDVKTL
     PHPGFPTDMQ SQMIALLLTA EGHKVITETV FENRFMHVAE FRRMNANITV EGRSAKIQGK
     SQLQGAQVKA TDLRAAAALI LAGLVAEGTT QVTELKHLDR GYVNFHEKLK SLGANIERVN
     Y
//