ID   MURD_BURCM              Reviewed;         502 AA.
AC   Q0BIK3;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   16-JUN-2009, entry version 24.
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=Bamb_0461;
OS   Burkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia
OS   cepacia (strain AMMD)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=339670;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Bruce D.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Kim E., Parke J., Coenye T.,
RA   Konstantinidis K., Ramette A., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Burkholderia cepacia AMMD.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000440; ABI86020.1; -; Genomic_DNA.
DR   RefSeq; YP_772354.1; -.
DR   GeneID; 4311150; -.
DR   GenomeReviews; CP000440_GR; Bamb_0461.
DR   KEGG; bam:Bamb_0461; -.
DR   NMPDR; fig|339670.3.peg.6104; -.
DR   OMA; Q0BIK3; SEDHLDR.
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    502       UDP-N-acetylmuramoylalanine--D-glutamate
FT                                ligase.
FT                                /FTId=PRO_0000301418.
FT   NP_BIND     129    135       ATP (Potential).
SQ   SEQUENCE   502 AA;  52794 MW;  5852F862D56A00FB CRC64;
     MFGDRQRPMV LVLGLGESGL AIARWCARHG CRLRIADTRE APPNLAALQA EGIDAEFVGG
     PFTPALLDGG VEIVGLSPGL SPLEPALAAL IAAANERAIA VWGELEFFAQ ALRALGTSGY
     QPKVLAITGT NGKTTTTNLT GLLCQRSGKK VAVAGNISPA MLDRLARAID ETALPDVWVL
     ELSSFQLETA RTFAPDAAAI LNITQDHLDW HGSFDAYAAA KGRIFGATTT RVLNRDDAAV
     MKFAPAAGAA DAARTVTFGL NEPAQQGDYG LSRDNGIAWL VEAVDRDAPD ETTSRRRKRD
     GAHTPDIAQK RLMPADALRI RGLHNAANAL AAFALARAID LPAAPLLHAL REYRGEAHRV
     EVIATIDDVD YVDDSKGTNV GATVAALDGL AQKIVLIAGG DGKGQDFAPL VAPVARWCRA
     VMLIGRDAPA IRDTLAETGV PLADHATLEA AVHAAAELAE PGDAVLLSPA CASLDMFRNY
     AHRADVFRAA VDEIAIDKGA TT
//