ID   MURA1_STAS1             Reviewed;         419 AA.
AC   Q49Z71;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   16-JUN-2009, entry version 30.
DE   RecName: Full=UDP-N-acetylglucosamine 1-carboxyvinyltransferase 1;
DE            EC=2.5.1.7;
DE   AltName: Full=Enoylpyruvate transferase 1;
DE   AltName: Full=UDP-N-acetylglucosamine enolpyruvyl transferase 1;
DE            Short=EPT 1;
GN   Name=murA1; OrderedLocusNames=SSP0760;
OS   Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 /
OS   DSM 20229).
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=342451;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16135568; DOI=10.1073/pnas.0502950102;
RA   Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K.,
RA   Higashide M., Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S.,
RA   Hattori M., Ohta T.;
RT   "Whole genome sequence of Staphylococcus saprophyticus reveals the
RT   pathogenesis of uncomplicated urinary tract infection.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(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; AP008934; BAE17905.1; -; Genomic_DNA.
DR   RefSeq; YP_300850.1; -.
DR   GeneID; 3615825; -.
DR   GenomeReviews; AP008934_GR; SSP0760.
DR   KEGG; ssp:SSP0760; -.
DR   NMPDR; fig|342451.4.peg.1275; -.
DR   HOGENOM; Q49Z71; -.
DR   OMA; Q49Z71; LESFICK.
DR   BioCyc; SSAP342451:SSP0760-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; 2.
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    419       UDP-N-acetylglucosamine 1-
FT                                carboxyvinyltransferase 1.
FT                                /FTId=PRO_0000231269.
FT   ACT_SITE    118    118       Proton donor (By similarity).
FT   BINDING     118    118       Phosphoenolpyruvate (covalent) (By
FT                                similarity).
SQ   SEQUENCE   419 AA;  44527 MW;  FE032B0A1C3B85C8 CRC64;
     MAQEVIKIRG GQTLKGEVNN HGAKNSAVAI IPAAILAEDK VTIEGLPEIS DVETLVSLLG
     DLNIKTELDG MTLNVDPNEI ENAPLPNNKV ESLRASYYMM GAMLGRFKKC VIGLPGGCPL
     GPRPIDQHIK GFKALGAKID ESSSTSMKIE ADKLTGANIF LDIVSVGATI NIMLAAVRAE
     GQTVIENAAK EPEVVDVANF LTSLGADIKG AGTSTIKING VEHLHGSHHQ VIPDRIEAGT
     YMCIAAACGE DITINNIIPT HVEPLTVKLK ELGVDIQVGD DSAVIQRSTP YASVDIKTLV
     YPGFATDLQQ PITPLLFMAD GVSFVTETIY PARFRHVDEL KNMGADISAD NGTATIKPSK
     LTGAEVYASD LRAGACLIVA GLLAEGVTTI YNVKHIYRGY TNIVSTLKSL GADIWTEEV
//