ID   MURE_STRPD              Reviewed;         481 AA.
AC   Q1JID8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-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=MGAS10270_Spy0320;
OS   Streptococcus pyogenes serotype M2 (strain MGAS10270).
OC   Bacteria; Firmicutes; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=370552;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16636287; DOI=10.1073/pnas.0510279103;
RA   Beres S.B., Richter E.W., Nagiec M.J., Sumby P., Porcella S.F.,
RA   DeLeo F.R., Musser J.M.;
RT   "Molecular genetic anatomy of inter- and intraserotype variation in
RT   the human bacterial pathogen group A Streptococcus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:7059-7064(2006).
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.
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DR   EMBL; CP000260; ABF33385.1; -; Genomic_DNA.
DR   RefSeq; YP_597929.1; -.
DR   GeneID; 4064307; -.
DR   GenomeReviews; CP000260_GR; murE.
DR   KEGG; sph:MGAS10270_Spy0320; -.
DR   HOGENOM; Q1JID8; -.
DR   OMA; Q1JID8; HTPDGIE.
DR   BioCyc; SPYO370552:MGAS10270_SPY0320-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; 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; 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    481       UDP-N-acetylmuramoyl-L-alanyl-D-
FT                                glutamate--L-lysine ligase.
FT                                /FTId=PRO_1000012388.
FT   NP_BIND     118    124       ATP (Potential).
FT   REGION      160    161       UDP-MurNAc-L-Ala-D-Glu binding (By
FT                                similarity).
FT   MOTIF       404    407       L-lysine recognition motif.
FT   BINDING      42     42       UDP-MurNAc-L-Ala-D-Glu (By similarity).
FT   BINDING     158    158       UDP-MurNAc-L-Ala-D-Glu (By similarity).
FT   BINDING     187    187       UDP-MurNAc-L-Ala-D-Glu (By similarity).
FT   BINDING     195    195       UDP-MurNAc-L-Ala-D-Glu (By similarity).
FT   MOD_RES     229    229       N6-carboxylysine (By similarity).
SQ   SEQUENCE   481 AA;  53479 MW;  B630BA6E4E7F51E3 CRC64;
     MITIEQLLDI LKKDHNFREV LDADGYHYHY QGLSFERLSY DSRQVDGKTL FFAKGATFKA
     DYLKEAITNG LQLYISEVDY ELGIPVVLVT DIKKAMSLIA MAFYGNPQEK LKLLAFTGTK
     GKTTAAYFAY HMLKESYKPA MFSTMNTTLD GKTFFKSQLT TPESLDLFAM MAECVTNGMT
     HLIMEVSSQA YLVDRVYGLT FDVGVFLNIS PDHIGPIEHP TFEDYFYHKR LLMENSRAVV
     INSGMDHFSF LADQVADQEH VFYGPLSDNQ ITTSQAFSFE AKGQLAGHYD IQLIGHFNQE
     NAMAAGLACL RLGASLADIQ KGIAKTRVPG RMEVLTMTNH AKVFVDYAHN GDSLEKLLSV
     VEEHQTGKLM LILGAPGNKG ESRRADFGRV IHQHPNLTVI LTADDPNFED PEDISKEIAS
     HIARPVEIIS DREQAIQKAM SLCQGAKDAV IIAGKGADAY QIVKGQQVAY AGDLAIAKHY
     L
//