ID MURD_BORA1 Reviewed; 508 AA. AC Q2KVF5; DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 07-MAR-2006, sequence version 1. DT 16-JUN-2009, entry version 31. 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=BAV2881; OS Bordetella avium (strain 197N). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Alcaligenaceae; Bordetella. OX NCBI_TaxID=360910; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16885469; DOI=10.1128/JB.01927-05; RA Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., RA King N.D., Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., RA Goble A., Lord A., Murphy L., Quail M.A., Rutter S., Squares R., RA Squares S., Woodward J., Parkhill J., Temple L.M.; RT "Comparison of the genome sequence of the poultry pathogen Bordetella RT avium with those of B. bronchiseptica, B. pertussis, and B. RT parapertussis reveals extensive diversity in surface structures RT associated with host interaction."; RL J. Bacteriol. 188:6002-6015(2006). 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. 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; AM167904; CAJ50491.1; -; Genomic_DNA. DR RefSeq; YP_787377.1; -. DR GeneID; 6267041; -. DR GenomeReviews; AM167904_GR; BAV2881. DR KEGG; bav:BAV2881; -. DR NMPDR; fig|521.1.peg.453; -. DR HOGENOM; Q2KVF5; -. DR OMA; Q2KVF5; 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 1 508 UDP-N-acetylmuramoylalanine--D-glutamate FT ligase. FT /FTId=PRO_0000257168. FT NP_BIND 138 144 ATP (Potential). SQ SEQUENCE 508 AA; 53709 MW; 8BB3FE665391C7A1 CRC64; MNTELTSRAD APLVLILGLG ETGVAAARWC AREGARLRVA DTRMQPGGLE GLRAVLQEAQ VEYHLGCGSH FDPALLDGVT QLVLSPGLAP GQEPAASLLA AAVSRGIEVL GEVELFARAL ASLAEARAYH PRLLAVTGTN GKTTVTALTR QLIEACGLSA RAAGNISPAA LASLMEALDQ DALPDVWVLE LSSFQLETTH SLQADAAVVL NVTQDHLDWH GDMQAYAQAK ARLLKMARVA IVNRDDPLTL AMVADVNGLN VRSFGRDLPQ RVGDMGLELG QGVAWLVACE PSDFDEPVVR RKKDAPPPQR GEGRMSRLMP VDALRIRGVH NALNALAALQ LARVLELGWG PMLRALRDYA GEPHRAAFVR SIGGVDYIND SKGTNVGATV AALEGLGQTV VLIAGGQGKG QDFSPLRSAV SRHARAVVLI GADGPAIGQV LESTGVALVV AADMREAVRR AAEIAQAGEA VLLSPACASL DMYRNYPHRG QVFVEEVEEL ALDRGEVL //