ID   MURA2_STAS1             Reviewed;         421 AA.
AC   Q49Z47;
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 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; OrderedLocusNames=SSP0784;
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; BAE17929.1; -; Genomic_DNA.
DR   RefSeq; YP_300874.1; -.
DR   GeneID; 3615751; -.
DR   GenomeReviews; AP008934_GR; SSP0784.
DR   KEGG; ssp:SSP0784; -.
DR   NMPDR; fig|342451.4.peg.1369; -.
DR   HOGENOM; Q49Z47; -.
DR   OMA; Q49Z47; VSRVYHL.
DR   BioCyc; SSAP342451:SSP0784-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_0000231270.
FT   ACT_SITE    119    119       Proton donor (By similarity).
FT   BINDING     119    119       Phosphoenolpyruvate (covalent) (By
FT                                similarity).
SQ   SEQUENCE   421 AA;  45031 MW;  74C0552CFE6BF168 CRC64;
     MDMIEINGGN RLTGEVKVSG AKNAVLPVLT ASLLASEGVS KLMNVPALSD VETINNVIST
     LNAEVSYDKD EESVTVDATK ELNEEAPYEY VSKMRASILV MGPLLARLGH AKVALPGGCA
     IGSRPIEQHI KGFEELGADI HMDGGFIYAS TENGLKGTTI HLDFPSVGAT QNIIMAASLA
     EGKTVLENVA REPEIVDLAN YINEMGGNVS GAGTDTIIIH GVETLHGVEH AIIPDRIEAG
     TLLIAGAITR GDVLVNGAIK EHMTSLVYKL EEMGVNLDYQ DDAIRVRVED ELKPVDIKTL
     PHPGFPTDMQ SQMMALLLTA EGHKVVTETV FENRFMHVAE FKRMNAKISV EGRSAKIEGK
     SELQGAQVKA TDLRAAAALI LAGLVADGTT QVTELKHLDR GYVDLHGKLE ALGADIKRTQ
     A
//