ID   MURE_STAES              Reviewed;         494 AA.
AC   Q8CPR2;
DT   30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   16-JUN-2009, entry version 48.
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=SE_0718;
OS   Staphylococcus epidermidis (strain ATCC 12228).
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=176280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=22832016; PubMed=12950922;
RX   DOI=10.1046/j.1365-2958.2003.03671.x;
RA   Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J.,
RA   Qin Z.-Q., Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z.,
RA   Yuan Z.-H., Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT   "Genome-based analysis of virulence genes in a non-biofilm-forming
RT   Staphylococcus epidermidis strain (ATCC 12228).";
RL   Mol. Microbiol. 49:1577-1593(2003).
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 (By similarity).
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   -!- 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   -!- 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; AE015929; AAO04315.1; -; Genomic_DNA.
DR   RefSeq; NP_764273.1; -.
DR   GeneID; 1055759; -.
DR   GenomeReviews; AE015929_GR; SE_0718.
DR   KEGG; sep:SE0718; -.
DR   HOGENOM; Q8CPR2; -.
DR   OMA; Q8CPR2; HTPDGIE.
DR   BioCyc; SEPI176280:SE_0718-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   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    494       UDP-N-acetylmuramoyl-L-alanyl-D-
FT                                glutamate--L-lysine ligase.
FT                                /FTId=PRO_0000101946.
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   494 AA;  54277 MW;  F76DB876D7F89621 CRC64;
     MNASALFKKI RVKNVIGTLD IQVDDITTDS RTAKEGSLFV ASKGYTVDSH KFCQNVVDQG
     CGIVVVNREL ELKGNVTQVV VPDTLRVASL LAHELYEFPS HQLTTYGVTG TNGKTSIATM
     IHLIYRKLNK NSAYLGTNGF QVNETKTKGA NTTPETVALT KKIKEAVDAN AEAMTMEVSS
     HGLALGRLRG VEFDVAIFSN LTQDHLDFHG TMEAYGHAKS LLFSQLGEDL SKEKYVVLNN
     DDDFSDYLAS VTPYEVFTYG ITHEAQFMAK NIKESLQGVE FEFCTPFGSF PVKSPYVGRF
     NISNIMAAMI AVWSKGTNLN EIINAVTELE PVEGRLEVLD PSLPIDLIID YAHTADGMNK
     LIDAVQPFVK QKLIFLVGMA GERDLTKTPE MGRVACRADY VIFTPDNPAN DDPKMLTAEL
     AKGATHNNYI EFDDRAEGIR HAIDIAEPGD TVVLASKGRE PYQIMPGHVK VPHRDDLIGL
     KAAYQKFGGG PLED
//