ID MURC_HELP2 Reviewed; 449 AA. AC B6JLL1; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 16-DEC-2008, sequence version 1. DT 31-MAY-2011, entry version 19. DE RecName: Full=UDP-N-acetylmuramate--L-alanine ligase; DE EC=6.3.2.8; DE AltName: Full=UDP-N-acetylmuramoyl-L-alanine synthetase; GN Name=murC; OrderedLocusNames=HPP12_0636; OS Helicobacter pylori (strain P12). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=570508; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=P12; RA Fischer W., Windhager L., Karnholz A., Zeiller M., Zimmer R., Haas R.; RT "The complete genome sequence of Helicobacter pylori strain P12."; RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Cell wall formation (By similarity). CC -!- CATALYTIC ACTIVITY: ATP + UDP-N-acetylmuramate + L-alanine = ADP + CC phosphate + UDP-N-acetylmuramoyl-L-alanine. 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 https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP001217; ACJ07789.1; -; Genomic_DNA. DR RefSeq; YP_002301269.1; NC_011498.1. DR GeneID; 7009770; -. DR GenomeReviews; CP001217_GR; HPP12_0636. DR KEGG; hpp:HPP12_0636; -. DR HOGENOM; HBG476594; -. DR OMA; YQPHRYS; -. DR ProtClustDB; PRK00421; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008763; F:UDP-N-acetylmuramate-L-alanine ligase activity; IEA:EC. 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:cellular cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR HAMAP; MF_00046; MurC; 1; -. DR InterPro; IPR004101; Mur_ligase_C. DR InterPro; IPR013221; Mur_ligase_cen. DR InterPro; IPR000713; Mur_ligase_N. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR005758; UDP-N-AcMur_Ala_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; PF01225; Mur_ligase; 1. DR Pfam; PF02875; Mur_ligase_C; 1. DR Pfam; PF08245; Mur_ligase_M; 1. DR SUPFAM; SSF53244; Mur_ligase_C; 1. DR SUPFAM; SSF53623; Mur_ligase_cen; 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. FT CHAIN 1 449 UDP-N-acetylmuramate--L-alanine ligase. FT /FTId=PRO_1000091106. FT NP_BIND 121 127 ATP (Potential). SQ SEQUENCE 449 AA; 50816 MW; 082AE395DD227B10 CRC64; MLETPKVLLK NLQDCKIHFI GIGGIGISGL AKYLKAQGAT ISGSDIAISP SVKYLKALGV EINIPHDPKA INNQDVIIHS AIIKEDNTEI QRAKELEIPI LSRKDALYSI LKDKRVFSVC GAHGKSSITA MLSAICPAFG AIIGAHSKEF DSNVRESAND SLVFEADESD SSFLFSNPFC AIVPNTEPEH LEHYDHDLER FFFAYEYFLD HAQKRVIYKE DPFLKNYSKD AIVLEKKDIY NIQYILKDGE PYTSFELKDL GAFLVWGLGE HNATNASLAI LSALDELNLE EIRNNLLNFK GIKKRFDILQ KNALILIDDY AHHPTEISAT LKSARIYADL LDTQEKIVVI WQAHKYSRLM DNLEEFKKCF LEHCDRLIIL PVYSASEVKR DIDLKAHFKH YNPTFIDRVR KKGDFLELLV NDNVVETIEK GFVIGFGAGD ITYQLRGEM //