ID MURE_THEMA Reviewed; 490 AA.
AC Q9WY79;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 01-MAY-2013, entry version 102.
DE RecName: Full=UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--LD-lysine ligase;
DE EC=6.3.2.37;
DE EC=6.3.2.7;
DE AltName: Full=D-lysine-adding enzyme;
DE AltName: Full=L-lysine-adding enzyme;
DE AltName: Full=UDP-MurNAc-L-Ala-D-Glu:LD-Lys ligase;
DE AltName: Full=UDP-MurNAc-tripeptide synthetase;
DE AltName: Full=UDP-N-acetylmuramyl-tripeptide synthetase;
GN Name=murE; OrderedLocusNames=TM_0237;
OS Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J.,
RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A.,
RA McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M.,
RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L.,
RA Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O.,
RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2]
RP FUNCTION, CHARACTERIZATION, SUBSTRATE SPECIFICITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=16595662; DOI=10.1074/jbc.M506311200;
RA Boniface A., Bouhss A., Mengin-Lecreulx D., Blanot D.;
RT "The MurE synthetase from Thermotoga maritima is endowed with an
RT unusual D-lysine adding activity.";
RL J. Biol. Chem. 281:15680-15686(2006).
CC -!- FUNCTION: Catalyzes the addition of both L- and D-lysine to the
CC nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate
CC (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan.
CC Is also able to use meso-diaminopimelate as the amino acid
CC substrate in vitro, although much less efficiently.
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 -!- CATALYTIC ACTIVITY: ATP + UDP-N-acetylmuramoyl-L-alanyl-D-
CC glutamate + D-lysine = ADP + phosphate + UDP-N-acetylmuramoyl-L-
CC alanyl-D-glutamyl-D-lysine.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.45 mM for UDP-N-acetylmuramoyl-L-Ala-D-Glu;
CC KM=2.8 mM for L-lysine (at pH 9.4);
CC KM=0.65 mM for L-lysine (at pH 8);
CC KM=1.7 mM for D-lysine (at pH 9.4);
CC KM=1.0 mM for D-lysine (at pH 8);
CC KM=4.8 mM for meso-diaminopimelate (at pH 9.4);
CC KM=27 mM for L-ornithine (at pH 9.4);
CC KM=3.6 mM for ATP;
CC Note=The catalytic efficiency for the L-lysine adding activity
CC is 4-fold and 10-fold higher than that for the D-lysine and
CC meso-diaminopimelate adding activity, respectively;
CC pH dependence:
CC Optimum pH is 9.4 for the L-lysine adding activity;
CC Temperature dependence:
CC Optimum temperature is 68 degrees Celsius for the L-lysine
CC adding activity;
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: The peptidoglycan of T.maritima was shown to
CC contain approximate amounts of both enantiomers of lysine and no
CC diaminopimelate.
CC -!- SIMILARITY: Belongs to the MurCDEF family. MurE subfamily.
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DR EMBL; AE000512; AAD35328.1; -; Genomic_DNA.
DR PIR; G72402; G72402.
DR RefSeq; NP_228051.1; NC_000853.1.
DR ProteinModelPortal; Q9WY79; -.
DR STRING; 243274.TM0237; -.
DR PRIDE; Q9WY79; -.
DR EnsemblBacteria; AAD35328; AAD35328; TM_0237.
DR GeneID; 897137; -.
DR KEGG; tma:TM0237; -.
DR PATRIC; 23935349; VBITheMar51294_0240.
DR eggNOG; COG0769; -.
DR KO; K01928; -.
DR OMA; RPLMGEA; -.
DR ProtClustDB; CLSK875045; -.
DR BioCyc; MetaCyc:MONOMER-16146; -.
DR UniPathway; UPA00219; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR GO; GO:0004326; F:tetrahydrofolylpolyglutamate synthase activity; IEA:InterPro.
DR GO; GO:0047482; F:UDP-N-acetylmuramoyl-L-alanyl-D-glutamate-L-lysine ligase activity; 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:0009252; P:peptidoglycan biosynthetic process; IEA:HAMAP.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR GO; GO:0046901; P:tetrahydrofolylpolyglutamate biosynthetic process; IEA:GOC.
DR Gene3D; 3.40.1190.10; -; 1.
DR Gene3D; 3.90.190.20; -; 1.
DR HAMAP; MF_00208; MurE; 1; -.
DR InterPro; IPR018109; Folylpolyglutamate_synth_CS.
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 Pfam; PF01225; Mur_ligase; 1.
DR Pfam; PF02875; Mur_ligase_C; 1.
DR Pfam; PF08245; Mur_ligase_M; 1.
DR SUPFAM; SSF53244; Mur_ligase_C; 1.
DR SUPFAM; SSF53623; Mur_ligase_cen; 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;
KW Reference proteome.
FT CHAIN 1 490 UDP-N-acetylmuramoyl-L-alanyl-D-
FT glutamate--LD-lysine ligase.
FT /FTId=PRO_0000101962.
FT NP_BIND 110 116 ATP (Potential).
FT REGION 152 153 UDP-MurNAc-L-Ala-D-Glu binding (By
FT similarity).
FT BINDING 32 32 UDP-MurNAc-L-Ala-D-Glu (By similarity).
FT BINDING 179 179 UDP-MurNAc-L-Ala-D-Glu (By similarity).
FT BINDING 185 185 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 490 AA; 54740 MW; 21A6FBE388D741A9 CRC64;
MNISTIVSNL KDLILEVRAP YDLEITGVSN HSSKVKKGDL FICRRGEKFD SHEIIPEVME
KGAVAVVVER EIDLDFPYIQ VFDSRYFEAK VASLFFEDPW KDVLTFGVTG TNGKTTTTMM
IYHMLTSLGE RGSVLTTAVK RILGNSYYDD ITTPDAITIL SAMKENREGG GKFFALEVSS
HALVQQRVEG VRFDVGIFTN ISRDHLDFHG TFENYLKAKL HLFDLLKDDG VAVLNESLAD
AFNRKSRKIT FGTSKNADYR LGNIEVSWEG TQFVLETPDG LLKVFTRAIG DFNAYNAAAA
IAALHQLGYD PKDLASSLET FTGVEGRFEV VRGAKKIGLN VVVDFAHSPD ALEKLLKNVR
KISQGRVIVV FGAGGNSDRG KRPMMSEVAS KLADVVILTT DDPRGEDPEQ IMEDLIKGID
KRKPYLVLFD RREAIETALT IANRGDSVVI AGRGHERYQI IDEEKKVPFQ DREVVEEIIR
DKLKGRKYAQ
//
