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Database: UniProt
Entry: Q9WY79
LinkDB: Q9WY79
Original site: Q9WY79 
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   29-OCT-2014, entry version 113.
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       {ECO:0000269|PubMed:16595662}.
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         {ECO:0000269|PubMed:16595662};
CC         KM=2.8 mM for L-lysine (at pH 9.4)
CC         {ECO:0000269|PubMed:16595662};
CC         KM=0.65 mM for L-lysine (at pH 8) {ECO:0000269|PubMed:16595662};
CC         KM=1.7 mM for D-lysine (at pH 9.4)
CC         {ECO:0000269|PubMed:16595662};
CC         KM=1.0 mM for D-lysine (at pH 8) {ECO:0000269|PubMed:16595662};
CC         KM=4.8 mM for meso-diaminopimelate (at pH 9.4)
CC         {ECO:0000269|PubMed:16595662};
CC         KM=27 mM for L-ornithine (at pH 9.4)
CC         {ECO:0000269|PubMed:16595662};
CC         KM=3.6 mM for ATP {ECO:0000269|PubMed:16595662};
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         {ECO:0000269|PubMed:16595662};
CC       Temperature dependence:
CC         Optimum temperature is 68 degrees Celsius for the L-lysine
CC         adding activity. {ECO:0000269|PubMed:16595662};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- PTM: Carbamoylation is probably crucial for Mg(2+) binding and,
CC       consequently, for the gamma-phosphate positioning of ATP.
CC       {ECO:0000250}.
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.
CC       {ECO:0000305}.
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DR   EMBL; AE000512; AAD35328.1; -; Genomic_DNA.
DR   PIR; G72402; G72402.
DR   RefSeq; NP_228051.1; NC_000853.1.
DR   RefSeq; YP_007976586.1; NC_021214.1.
DR   RefSeq; YP_008990789.1; NC_023151.1.
DR   PDB; 4BUB; X-ray; 2.90 A; A/B=1-490.
DR   PDBsum; 4BUB; -.
DR   ProteinModelPortal; Q9WY79; -.
DR   STRING; 243274.TM0237; -.
DR   PRIDE; Q9WY79; -.
DR   EnsemblBacteria; AAD35328; AAD35328; TM_0237.
DR   GeneID; 18092562; -.
DR   GeneID; 897137; -.
DR   KEGG; tma:TM0237; -.
DR   KEGG; tmi:THEMA_03540; -.
DR   KEGG; tmm:Tmari_0235; -.
DR   PATRIC; 23935349; VBITheMar51294_0240.
DR   eggNOG; COG0769; -.
DR   InParanoid; Q9WY79; -.
DR   KO; K01928; -.
DR   OMA; KIAVDYA; -.
DR   OrthoDB; EOG6PKFCR; -.
DR   BioCyc; MetaCyc:MONOMER-16146; -.
DR   UniPathway; UPA00219; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-HAMAP.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-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:UniProtKB-EC.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.1190.10; -; 1.
DR   Gene3D; 3.40.1390.10; -; 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; SSF53244; 1.
DR   SUPFAM; SSF53623; SSF53623; 1.
DR   SUPFAM; SSF63418; SSF63418; 1.
DR   TIGRFAMs; TIGR01085; murE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; 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. {ECO:0000255}.
FT   REGION      152    153       UDP-MurNAc-L-Ala-D-Glu binding.
FT                                {ECO:0000250}.
FT   BINDING      32     32       UDP-MurNAc-L-Ala-D-Glu. {ECO:0000250}.
FT   BINDING     179    179       UDP-MurNAc-L-Ala-D-Glu. {ECO:0000250}.
FT   BINDING     185    185       UDP-MurNAc-L-Ala-D-Glu. {ECO:0000250}.
FT   BINDING     187    187       UDP-MurNAc-L-Ala-D-Glu. {ECO:0000250}.
FT   MOD_RES     219    219       N6-carboxylysine. {ECO:0000250}.
FT   HELIX         3      9
FT   TURN         10     13
FT   STRAND       14     19
FT   STRAND       27     32
FT   STRAND       37     43
FT   HELIX        54     60
FT   STRAND       64     70
FT   STRAND       74     76
FT   STRAND       78     82
FT   HELIX        84     95
FT   TURN         99    102
FT   STRAND      103    112
FT   HELIX       114    126
FT   STRAND      133    135
FT   HELIX       156    168
FT   STRAND      172    177
FT   HELIX       182    185
FT   TURN        186    188
FT   STRAND      193    198
FT   STRAND      203    207
FT   STRAND      209    211
FT   HELIX       212    220
FT   HELIX       221    223
FT   STRAND      226    235
FT   HELIX       236    238
FT   TURN        239    241
FT   STRAND      246    254
FT   STRAND      257    261
FT   STRAND      272    276
FT   STRAND      282    285
FT   HELIX       293    305
FT   TURN        306    308
FT   HELIX       311    315
FT   TURN        316    320
FT   STRAND      327    330
FT   HELIX       332    334
FT   TURN        335    338
FT   STRAND      340    343
FT   HELIX       349    362
FT   STRAND      367    371
FT   HELIX       383    392
FT   STRAND      394    398
FT   STRAND      404    406
FT   HELIX       409    416
FT   STRAND      425    427
FT   HELIX       431    441
FT   STRAND      447    450
FT   STRAND      458    462
FT   STRAND      465    468
FT   HELIX       471    484
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
//
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