ID MURC_DICNV Reviewed; 478 AA. AC A5EY22; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 12-JUN-2007, sequence version 1. DT 16-OCT-2019, entry version 81. DE RecName: Full=UDP-N-acetylmuramate--L-alanine ligase {ECO:0000255|HAMAP-Rule:MF_00046}; DE EC=6.3.2.8 {ECO:0000255|HAMAP-Rule:MF_00046}; DE AltName: Full=UDP-N-acetylmuramoyl-L-alanine synthetase {ECO:0000255|HAMAP-Rule:MF_00046}; GN Name=murC {ECO:0000255|HAMAP-Rule:MF_00046}; GN OrderedLocusNames=DNO_0980; OS Dichelobacter nodosus (strain VCS1703A). OC Bacteria; Proteobacteria; Gammaproteobacteria; Cardiobacteriales; OC Cardiobacteriaceae; Dichelobacter. OX NCBI_TaxID=246195; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=VCS1703A; RX PubMed=17468768; DOI=10.1038/nbt1302; RA Myers G.S.A., Parker D., Al-Hasani K., Kennan R.M., Seemann T., RA Ren Q., Badger J.H., Selengut J.D., Deboy R.T., Tettelin H., RA Boyce J.D., McCarl V.P., Han X., Nelson W.C., Madupu R., Mohamoud Y., RA Holley T., Fedorova N., Khouri H., Bottomley S.P., Whittington R.J., RA Adler B., Songer J.G., Rood J.I., Paulsen I.T.; RT "Genome sequence and identification of candidate vaccine antigens from RT the animal pathogen Dichelobacter nodosus."; RL Nat. Biotechnol. 25:569-575(2007). CC -!- FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00046}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + CC H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine; CC Xref=Rhea:RHEA:23372, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57972, ChEBI:CHEBI:70757, CC ChEBI:CHEBI:83898, ChEBI:CHEBI:456216; EC=6.3.2.8; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00046}; CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_00046}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00046}. CC -!- SIMILARITY: Belongs to the MurCDEF family. {ECO:0000255|HAMAP- CC Rule:MF_00046}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000513; ABQ13874.1; -; Genomic_DNA. DR RefSeq; WP_012031293.1; NC_009446.1. DR SMR; A5EY22; -. DR STRING; 246195.DNO_0980; -. DR PRIDE; A5EY22; -. DR EnsemblBacteria; ABQ13874; ABQ13874; DNO_0980. DR KEGG; dno:DNO_0980; -. DR eggNOG; ENOG4105DFU; Bacteria. DR eggNOG; COG0773; LUCA. DR HOGENOM; HOG000256031; -. DR KO; K01924; -. DR OMA; DITYQLR; -. DR OrthoDB; 307881at2; -. DR BioCyc; DNOD246195:G1G7U-977-MONOMER; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000000248; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0008763; F:UDP-N-acetylmuramate-L-alanine ligase activity; IEA:UniProtKB-UniRule. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR Gene3D; 3.40.1190.10; -; 1. DR Gene3D; 3.90.190.20; -; 1. DR HAMAP; MF_00046; MurC; 1. DR InterPro; IPR036565; Mur-like_cat_sf. DR InterPro; IPR004101; Mur_ligase_C. DR InterPro; IPR036615; Mur_ligase_C_dom_sf. DR InterPro; IPR013221; Mur_ligase_cen. DR InterPro; IPR000713; Mur_ligase_N. DR InterPro; IPR005758; UDP-N-AcMur_Ala_ligase_murC. DR Pfam; PF01225; Mur_ligase; 1. DR Pfam; PF02875; Mur_ligase_C; 1. DR Pfam; PF08245; Mur_ligase_M; 1. DR SUPFAM; SSF53244; SSF53244; 1. DR SUPFAM; SSF53623; SSF53623; 1. DR TIGRFAMs; TIGR01082; murC; 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; KW Reference proteome. FT CHAIN 1 478 UDP-N-acetylmuramate--L-alanine ligase. FT /FTId=PRO_0000336831. FT NP_BIND 125 131 ATP. {ECO:0000255|HAMAP-Rule:MF_00046}. SQ SEQUENCE 478 AA; 52470 MW; E34B81D00796B3A5 CRC64; MNHEVHFGRI ERRHMRRVKN IFFVGIGGTG MSGIAEVLLN LGYSISGSDI KDSAVTQYLA QKGAQIFIGH AAENVEHADV VVVSSAIAEN NVEVKQARAL EIPVIRRAQM LAELMRFRFG IAIAGTHGKT TTTSLTASLL SDAGLDPTFV IGGILTAAGS NARLGEGHYL VAESDESDCS FWLLQPMISI VTNIDADHLE NYNGSYETLK AGFVRFLHNL PFYGLAVLCI DDAGVRSILP EVGRPVRTYG FSEDADVRAI NVRQKGLAMH FDVIAHDEDR CFSVTLNMAG KHNVLNALAA IIVGEELGID RETIIEGLAQ FKGVARRFTH HGRIAHDHGF ADVFEDYGHH PREIKAVLDA AMEGFAGRRI VAVFQPHRFT RTRDLLDDFA EVLAVCDCLV LTEVYAAGEE PIAGADARDL TRAIRAHGRV EPIFIADKEE IVPHLRHDIL QDDDVVIFFG AGDIGRVAKM MDELKIKE //