ID   MURE_STAHJ              Reviewed;         494 AA.
AC   Q4L525;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   16-JUN-2009, entry version 37.
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=SH1941;
OS   Staphylococcus haemolyticus (strain JCSC1435).
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=279808;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16237012; DOI=10.1128/JB.187.21.7292-7308.2005;
RA   Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA   Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S.,
RA   Lee J.C., Hiramatsu K.;
RT   "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT   extreme plasticity of its genome and the evolution of human-colonizing
RT   staphylococcal species.";
RL   J. Bacteriol. 187:7292-7308(2005).
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; AP006716; BAE05250.1; -; Genomic_DNA.
DR   RefSeq; YP_253856.1; -.
DR   GeneID; 3482035; -.
DR   GenomeReviews; AP006716_GR; SH1941.
DR   KEGG; sha:SH1941; -.
DR   NMPDR; fig|279808.3.peg.2144; -.
DR   HOGENOM; Q4L525; -.
DR   OMA; Q4L525; HTPDGIE.
DR   BioCyc; SHAE279808:SH1941-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_1000012384.
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;  54177 MW;  6FC7854CCA8EBF09 CRC64;
     MNANELFEKI RVKQVIGTLD INVTDITTDS RTASEGSIFV ASKGYTVDSH KFCQNVVDQG
     AKVIVVNHQQ DINGDVTQVI VPDTLRVASL LAHTLYDFPS HQLTTIGVTG TNGKTSIATM
     IHLIYRGLGK GSAYLGTNGF QINEHKTRGA NTTPETVSLT KKIKQAVDEN AEAMTMEVSS
     HGLSLGRLRG VEFDVAIFSN LTQDHLDFHG TMEAYGHAKS LLFSQLGEDL SKEKYAVLNN
     DDDFSKYLAS VTPYEIFTYG IDHDAQFMAK NIQESLQGVH FDFDTPIGTY SVKTPYVGKF
     NISNIMAAMI AVWSKGTSME DIVRVVENLE PVEGRLEVLD PSLPIDLIID YAHTADGMNK
     LIDAVKPFVK QKLIFLIGMA GERDLTKTPE MGAVACRADY VIFTPDNPAN DDPKMLTAEL
     AKGATHNHYV EFDDRAEGIK HAIDIAEPGD TVVLASKGRE PYQIMPGHIK VPHRDDLIGL
     EAAYKKFGGG PSEH
//