ID   MURD_BLOPB              Reviewed;         440 AA.
AC   Q493Q3;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   16-JUN-2009, entry version 34.
DE   RecName: Full=UDP-N-acetylmuramoylalanine--D-glutamate ligase;
DE            EC=6.3.2.9;
DE   AltName: Full=UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase;
DE   AltName: Full=D-glutamic acid-adding enzyme;
GN   Name=murD; OrderedLocusNames=BPEN_144;
OS   Blochmannia pennsylvanicus (strain BPEN).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; ant endosymbionts; Candidatus Blochmannia.
OX   NCBI_TaxID=291272;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16077009; DOI=10.1101/gr.3771305;
RA   Degnan P.H., Lazarus A.B., Wernegreen J.J.;
RT   "Genome sequence of Blochmannia pennsylvanicus indicates parallel
RT   evolutionary trends among bacterial mutualists of insects.";
RL   Genome Res. 15:1023-1033(2005).
CC   -!- FUNCTION: Cell wall formation. Catalyzes the addition of glutamate
CC       to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA)
CC       (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + UDP-N-acetylmuramoyl-L-alanine +
CC       glutamate = ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-
CC       glutamate.
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the murCDEF family.
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DR   EMBL; CP000016; AAZ40784.1; -; Genomic_DNA.
DR   RefSeq; YP_277657.1; -.
DR   GeneID; 3562866; -.
DR   GenomeReviews; CP000016_GR; BPEN_144.
DR   KEGG; bpn:BPEN_144; -.
DR   HOGENOM; Q493Q3; -.
DR   OMA; Q493Q3; LWVNDTK.
DR   BioCyc; CBLO291272:BPEN_144-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0008764; F:UDP-N-acetylmuramoylalanine-D-glutamate lig...; 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   HAMAP; MF_00639; -; 1.
DR   InterPro; IPR004101; Mur_ligase_C.
DR   InterPro; IPR013221; Mur_ligase_cen.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR005762; UDP-N-AcMur-Glu_ligase.
DR   Gene3D; G3DSA:3.90.190.20; Mur_ligase_C; 1.
DR   Gene3D; G3DSA:3.40.1190.10; Mur_ligase_cen; 1.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Pfam; PF02875; Mur_ligase_C; 1.
DR   Pfam; PF08245; Mur_ligase_M; 1.
DR   TIGRFAMs; TIGR01087; murD; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell cycle; Cell division; Cell shape;
KW   Cell wall biogenesis/degradation; Complete proteome; Cytoplasm;
KW   Ligase; Nucleotide-binding; Peptidoglycan synthesis.
FT   CHAIN         1    440       UDP-N-acetylmuramoylalanine--D-glutamate
FT                                ligase.
FT                                /FTId=PRO_0000257167.
FT   NP_BIND     112    118       ATP (Potential).
SQ   SEQUENCE   440 AA;  49313 MW;  A45C39BDCEFCDA1C CRC64;
     MRNYRGSKVV IIGLGITGLS CVNFFLDRGV IPKVIDTRIY PPGIKKIPHV VQCYLGAFND
     IWLLSATLIV VSPGVRLDHP VLIEALKLGI EIIGDIELFT REATAPIIAI TGSNGKSTVT
     QLVSRMARIA GWHVGVAGNI GVPVLSLLNK SYQLYILEIS SFQLDTTYSL RAIAAAILNV
     SEDHMDHYPG GLKQYWFSKQ RIYKNAKICV MNALDFLTIP IYHEYDYCIS FGENEDSADY
     YLKYYKGHTW IVAYNEYVLN CSEMRINNRI NYINALSALA LSDIIKIPRS VSLKVLCQFS
     GLAHRCQLIY KNHGVSWIND SKATNVSATK EAINNLKLCG TLHLILGGDG KLADFSSLKH
     LIKQHEIHLY CFGKDGLLLT TLGFSDVILT NTMIQAMRII NRRIKAKDIV LLSPACSSLD
     QFKSFEMRGL IFTCFAREFR
//