ID   MURI_ECOUT              Reviewed;         285 AA.
AC   Q1R3U0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   16-JUN-2009, entry version 25.
DE   RecName: Full=Glutamate racemase;
DE            EC=5.1.1.3;
GN   Name=murI; OrderedLocusNames=UTI89_C4562;
OS   Escherichia coli (strain UTI89 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=364106;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16585510; DOI=10.1073/pnas.0600938103;
RA   Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A.,
RA   Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R.,
RA   Fulton R.S., Latreille J.P., Spieth J., Hooton T.M., Mardis E.R.,
RA   Hultgren S.J., Gordon J.I.;
RT   "Identification of genes subject to positive selection in
RT   uropathogenic strains of Escherichia coli: a comparative genomics
RT   approach.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006).
CC   -!- FUNCTION: Provides the (R)-glutamate required for cell wall
CC       biosynthesis (By similarity).
CC   -!- CATALYTIC ACTIVITY: L-glutamate = D-glutamate.
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC   -!- SIMILARITY: Belongs to the aspartate/glutamate racemases family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000243; ABE09974.1; -; Genomic_DNA.
DR   RefSeq; YP_543505.1; -.
DR   GeneID; 3994352; -.
DR   GenomeReviews; CP000243_GR; UTI89_C4562.
DR   KEGG; eci:UTI89_C4562; -.
DR   HOGENOM; Q1R3U0; -.
DR   OMA; Q1R3U0; TQPCPGL.
DR   BioCyc; ECOL364106:UTI89_C4562-MON; -.
DR   GO; GO:0008881; F:glutamate racemase activity; IEA:HAMAP.
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   HAMAP; MF_00258; -; 1.
DR   InterPro; IPR015942; Asp/Glu/hydantoin_racemase.
DR   InterPro; IPR001920; Asp/Glu_race.
DR   InterPro; IPR018187; Asp/Glu_racemase_CS.
DR   InterPro; IPR004391; Glu_race.
DR   Gene3D; G3DSA:3.40.50.1860; Asp/Glu_race; 1.
DR   Pfam; PF01177; Asp_Glu_race; 1.
DR   TIGRFAMs; TIGR00067; glut_race; 1.
DR   PROSITE; PS00923; ASP_GLU_RACEMASE_1; 1.
DR   PROSITE; PS00924; ASP_GLU_RACEMASE_2; 1.
PE   3: Inferred from homology;
KW   Cell shape; Cell wall biogenesis/degradation; Complete proteome;
KW   Isomerase; Peptidoglycan synthesis.
FT   CHAIN         1    285       Glutamate racemase.
FT                                /FTId=PRO_1000047563.
SQ   SEQUENCE   285 AA;  31160 MW;  03B473A050719F36 CRC64;
     MATKLQDGNT PCLAATPSEP RPTVLVFDSG VGGLSVYDEI RHLLPDLHYI YAFDNVAFPY
     GEKSEVFIVE RVVEIVTAVQ ERYPLALAVV ACNTASTVSL PALREKFDFP VVGVVPAIKP
     AARLTANGIV GLLATRGTVK RSYTHELIAR FANECQIEML GSAEMVELAE AKLHGEDVSL
     DALKRILRPW LRMKEPPDTV VLGCTHFPLL QEELLQVLPE GTRLVDSGAA IARRTAWLLE
     HEAPDAKSAD ANIAFCMAMT PEAEQLLPVL QRYGFETLEK LAVLG
//