ID MURE_STAA8 Reviewed; 493 AA. AC Q2FZP6; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 21-MAR-2006, sequence version 1. DT 16-JUN-2009, entry version 27. DE RecName: Full=UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--L-lysine ligase; DE EC=6.3.2.7; DE AltName: Full=UDP-MurNAc-L-Ala-D-Glu:L-Lys ligase; DE AltName: Full=L-lysine-adding enzyme; DE AltName: Full=UDP-N-acetylmuramyl-tripeptide synthetase; DE AltName: Full=UDP-MurNAc-tripeptide synthetase; GN Name=murE; OrderedLocusNames=SAOUHSC_00954; OS Staphylococcus aureus (strain NCTC 8325). OC Bacteria; Firmicutes; Bacillales; Staphylococcus. OX NCBI_TaxID=93061; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., RA Iandolo J.J.; RT "The Staphylococcus aureus NCTC8325 genome."; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. RN [2] RP FUNCTION, CHARACTERIZATION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, RP AND BIOPHYSICOCHEMICAL PROPERTIES. RC STRAIN=Copenhagen; RX PubMed=14114846; RA Ito E., Strominger J.L.; RT "Enzymatic synthesis of the peptide in bacterial uridine nucleotides. RT III. Purification and properties of L-lysine-adding enzyme."; RL J. Biol. Chem. 239:210-214(1964). RN [3] RP FUNCTION. RX PubMed=10498701; RA Mengin-Lecreulx D., Falla T., Blanot D., van Heijenoort J., RA Adams D.J., Chopra I.; RT "Expression of the Staphylococcus aureus UDP-N-acetylmuramoyl-L- RT alanyl-D-glutamate:L-lysine ligase in Escherichia coli and effects on RT peptidoglycan biosynthesis and cell growth."; RL J. Bacteriol. 181:5909-5914(1999). RN [4] RP ROLE IN ANTIBIOTIC RESISTANCE. RX PubMed=14996801; DOI=10.1128/JB.186.6.1705-1713.2004; RA Gardete S., Ludovice A.M., Sobral R.G., Filipe S.R., de Lencastre H., RA Tomasz A.; RT "Role of murE in the expression of beta-lactam antibiotic resistance RT in Staphylococcus aureus."; RL J. Bacteriol. 186:1705-1713(2004). CC -!- FUNCTION: Catalyzes the addition of L-lysine to the nucleotide CC precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the CC biosynthesis of bacterial cell-wall peptidoglycan. Can not use CC diaminopimelate as substrate. Seems to have a role in beta-lactam CC antibiotic resistance. CC -!- CATALYTIC ACTIVITY: ATP + UDP-N-acetylmuramoyl-L-alanyl-D- CC glutamate + L-lysine = ADP + phosphate + UDP-N-acetylmuramoyl-L- CC alanyl-D-glutamyl-L-lysine. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.4 mM for UDP-N-acetylmuramoyl-L-Ala-D-Glu; CC KM=0.5 mM for L-lysine; CC KM=0.3 mM for ATP; CC pH dependence: CC Optimum pH is 8.4-9; CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- PTM: Carbamoylation is probably crucial for Mg(2+) binding and, CC consequently, for the gamma-phosphate positioning of ATP (By CC similarity). CC -!- MISCELLANEOUS: Expression of this protein in E.coli results in 50% CC incorporation of L-Lys into the peptidoglycan (which normally CC contains meso-diaminopimelate instead), leading to abnormal CC morphological changes and subsequent cell lysis. CC -!- SIMILARITY: Belongs to the murCDEF family. MurE subfamily. 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; CP000253; ABD30079.1; -; Genomic_DNA. DR RefSeq; YP_499507.1; -. DR GeneID; 3920665; -. DR GenomeReviews; CP000253_GR; SAOUHSC_00954. DR KEGG; sao:SAOUHSC_00954; -. DR HOGENOM; Q2FZP6; -. DR OMA; Q2FZP6; HTPDGIE. DR BioCyc; SAUR93061:SAOUHSC_00954-MON; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:HAMAP. DR GO; GO:0047482; F:UDP-N-acetylmuramoyl-L-alanyl-D-glutamate-L...; 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: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_00208; -; 1. DR InterPro; IPR004101; Mur_ligase_C. DR InterPro; IPR013221; Mur_ligase_cen. DR InterPro; IPR000713; Mur_ligase_N. DR InterPro; IPR005761; UDP-N-AcMur-Glu-dNH2Pim_ligase. DR Gene3D; G3DSA:3.90.190.20; Mur_ligase_C; 1. DR Gene3D; G3DSA:3.40.1190.10; Mur_ligase_cen; 1. DR Pfam; PF01225; Mur_ligase; 1. DR Pfam; PF02875; Mur_ligase_C; 1. DR Pfam; PF08245; Mur_ligase_M; 1. DR TIGRFAMs; TIGR01085; murE; 1. PE 1: Evidence at protein level; 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 1 493 UDP-N-acetylmuramoyl-L-alanyl-D- FT glutamate--L-lysine ligase. FT /FTId=PRO_1000012382. FT NP_BIND 110 116 ATP (Potential). FT REGION 152 153 UDP-MurNAc-L-Ala-D-Glu binding (By FT similarity). FT MOTIF 406 409 L-lysine recognition motif. FT BINDING 30 30 UDP-MurNAc-L-Ala-D-Glu (By similarity). FT BINDING 179 179 UDP-MurNAc-L-Ala-D-Glu (By similarity). FT BINDING 187 187 UDP-MurNAc-L-Ala-D-Glu (By similarity). FT MOD_RES 219 219 N6-carboxylysine (By similarity). SQ SEQUENCE 493 AA; 54105 MW; 0D224B23DA5A1390 CRC64; MDASTLFKKV KVKRVLGSLE QQIDDITTDS RTAREGSIFV ASVGYTVDSH KFCQNVADQG CKLVVVNKEQ SLPANVTQVV VPDTLRVASI LAHTLYDYPS HQLVTFGVTG TNGKTSIATM IHLIQRKLQK NSAYLGTNGF QINETKTKGA NTTPETVSLT KKIKEAVDAG AESMTLEVSS HGLVLGRLRG VEFDVAIFSN LTQDHLDFHG TMEAYGHAKS LLFSQLGEDL SKEKYVVLNN DDSFSEYLRT VTPYEVFSYG IDEEAQFMAK NIQESLQGVS FDFVTPFGTY PVKSPYVGKF NISNIMAAMI AVWSKGTSLE TIIKAVENLE PVEGRLEVLD PSLPIDLIID YAHTADGMNK LIDAVQPFVK QKLIFLVGMA GERDLTKTPE MGRVACRADY VIFTPDNPAN DDPKMLTAEL AKGATHQNYI EFDDRAEGIK HAIDIAEPGD TVVLASKGRE PYQIMPGHIK VPHRDDLIGL EAAYKKFGGG PVD //