ID   MURE_STRR6              Reviewed;         481 AA.
AC   Q8CWQ5;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   16-JUN-2009, entry version 44.
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=spr1384;
OS   Streptococcus pneumoniae (strain ATCC BAA-255 / R6).
OC   Bacteria; Firmicutes; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=171101;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=21429245; PubMed=11544234;
RX   DOI=10.1128/JB.183.19.5709-5717.2001;
RA   Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S.,
RA   DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C.,
RA   Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E.,
RA   LeBlanc D.J., Lee L.N., Lefkowitz E.J., Lu J., Matsushima P.,
RA   McAhren S.M., McHenney M., McLeaster K., Mundy C.W., Nicas T.I.,
RA   Norris F.H., O'Gara M., Peery R.B., Robertson G.T., Rockey P.,
RA   Sun P.-M., Winkler M.E., Yang Y., Young-Bellido M., Zhao G.,
RA   Zook C.A., Baltz R.H., Jaskunas S.R., Rosteck P.R. Jr., Skatrud P.L.,
RA   Glass J.I.;
RT   "Genome of the bacterium Streptococcus pneumoniae strain R6.";
RL   J. Bacteriol. 183:5709-5717(2001).
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; AE007317; AAL00188.1; -; Genomic_DNA.
DR   PIR; G98044; G98044.
DR   RefSeq; NP_358977.1; -.
DR   GeneID; 934603; -.
DR   GenomeReviews; AE007317_GR; spr1384.
DR   KEGG; spr:spr1384; -.
DR   HOGENOM; Q8CWQ5; -.
DR   OMA; Q8CWQ5; HTPDGIE.
DR   BioCyc; SPNE171101:SPR1384-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_0000101954.
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     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;  53828 MW;  9A668127E05341E5 CRC64;
     MIKIETVLDI LKKDGLFREI IDQGHYHYNY SKVIFDSISY DSRKVTEDTL FFAKGAAFKK
     EYLLSAITQG LAWYVAEKDY EVDIPVIIVN DIKKAMSLIA MEFYGNPQEK LKLLAFTGTK
     GKTTATYFAY NILSQGHRPA MLSTMNTTLD GETFFKSALT TPESIDLFDM MNQAVQNDRT
     HLIMEVSSQA YLVHRVYGLT FDVGVFLNIT PDHIGPIEHP SFEDYFYHKR LLMENSRAVI
     INSDMDHFSV LKEQVEDQDH DFYGSQFDNQ IENSKAFSFS ATGKLAGDYD IQLIGNFNQE
     NAVAAGLACL RLGASLEDIK KGIAATRVPG RMEVLTQKNG AKVFIDYAHN GDSLKKLINV
     VETHQTGKIA LVLGSTGNKG ESRRKDFGLL LNQHPEIQVF LTADDPNYED PMAIADEISS
     YINHPVEKIA DRQEAIKAAM AITNHELDAV IIAGKGADCY QIIQGKKESY PGDTAVAENY
     L
//