MURE_THEMA
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 03-AUG-2022, entry version 152.
DE RecName: Full=UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--LD-lysine ligase;
DE EC=6.3.2.37 {ECO:0000269|PubMed:16595662};
DE EC=6.3.2.7 {ECO:0000269|PubMed:16595662};
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 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA 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, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND BIOPHYSICOCHEMICAL
RP 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 unusual D-
RT 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 (UMAG)
CC in the biosynthesis of bacterial cell-wall peptidoglycan. Is also able
CC to use meso-diaminopimelate as the amino acid substrate in vitro,
CC although much less efficiently. {ECO:0000269|PubMed:16595662}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-lysine + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-
CC glutamate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-
CC alanyl-gamma-D-glutamyl-L-lysine; Xref=Rhea:RHEA:17969,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:32551,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:83900, ChEBI:CHEBI:83903,
CC ChEBI:CHEBI:456216; EC=6.3.2.7;
CC Evidence={ECO:0000269|PubMed:16595662};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-lysine + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-
CC glutamate = ADP + H(+) + N(6)-(UDP-N-acetyl-alpha-D-muramoyl-L-
CC alanyl-gamma-D-glutamyl)-D-lysine + phosphate; Xref=Rhea:RHEA:25273,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:32557,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:83900, ChEBI:CHEBI:83912,
CC ChEBI:CHEBI:456216; EC=6.3.2.37;
CC Evidence={ECO:0000269|PubMed:16595662};
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) {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) {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) {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 is 4-
CC fold and 10-fold higher than that for the D-lysine and meso-
CC 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 adding
CC activity. {ECO:0000269|PubMed:16595662};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- PTM: Carboxylation 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 contain
CC approximate amounts of both enantiomers of lysine and no
CC diaminopimelate.
CC -!- SIMILARITY: Belongs to the MurCDEF family. MurE subfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE000512; AAD35328.1; -; Genomic_DNA.
DR PIR; G72402; G72402.
DR RefSeq; NP_228051.1; NC_000853.1.
DR RefSeq; WP_004082936.1; NZ_CP011107.1.
DR PDB; 4BUB; X-ray; 2.90 A; A/B=1-490.
DR PDBsum; 4BUB; -.
DR AlphaFoldDB; Q9WY79; -.
DR SMR; Q9WY79; -.
DR STRING; 243274.THEMA_03540; -.
DR EnsemblBacteria; AAD35328; AAD35328; TM_0237.
DR KEGG; tma:TM0237; -.
DR eggNOG; COG0769; Bacteria.
DR InParanoid; Q9WY79; -.
DR OMA; FIPGRML; -.
DR OrthoDB; 1861122at2; -.
DR BioCyc; MetaCyc:MON-16146; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004326; F:tetrahydrofolylpolyglutamate synthase activity; IEA:InterPro.
DR GO; GO:0102195; F:UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--D-lysine ligase activity; IEA:UniProtKB-EC.
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-UniRule.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
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; IPR036565; Mur-like_cat_sf.
DR InterPro; IPR004101; Mur_ligase_C.
DR InterPro; IPR036615; Mur_ligase_C_dom_sf.
DR InterPro; IPR013221; Mur_ligase_cen.
DR InterPro; IPR000713; Mur_ligase_N.
DR InterPro; IPR035911; MurE/MurF_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; Cytoplasm; Ligase; Nucleotide-binding;
KW Peptidoglycan synthesis; Reference proteome.
FT CHAIN 1..490
FT /note="UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--LD-lysine
FT ligase"
FT /id="PRO_0000101962"
FT BINDING 32
FT /ligand="UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-
FT glutamate"
FT /ligand_id="ChEBI:CHEBI:83900"
FT /evidence="ECO:0000250"
FT BINDING 110..116
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 152..153
FT /ligand="UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-
FT glutamate"
FT /ligand_id="ChEBI:CHEBI:83900"
FT /evidence="ECO:0000250"
FT BINDING 179
FT /ligand="UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-
FT glutamate"
FT /ligand_id="ChEBI:CHEBI:83900"
FT /evidence="ECO:0000250"
FT BINDING 185
FT /ligand="UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-
FT glutamate"
FT /ligand_id="ChEBI:CHEBI:83900"
FT /evidence="ECO:0000250"
FT BINDING 187
FT /ligand="UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-
FT glutamate"
FT /ligand_id="ChEBI:CHEBI:83900"
FT /evidence="ECO:0000250"
FT MOD_RES 219
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000250"
FT HELIX 3..9
FT /evidence="ECO:0007829|PDB:4BUB"
FT TURN 10..13
FT /evidence="ECO:0007829|PDB:4BUB"
FT STRAND 14..19
FT /evidence="ECO:0007829|PDB:4BUB"
FT STRAND 27..32
FT /evidence="ECO:0007829|PDB:4BUB"
FT STRAND 37..43
FT /evidence="ECO:0007829|PDB:4BUB"
FT HELIX 54..60
FT /evidence="ECO:0007829|PDB:4BUB"
FT STRAND 64..70
FT /evidence="ECO:0007829|PDB:4BUB"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:4BUB"
FT STRAND 78..82
FT /evidence="ECO:0007829|PDB:4BUB"
FT HELIX 84..95
FT /evidence="ECO:0007829|PDB:4BUB"
FT TURN 99..102
FT /evidence="ECO:0007829|PDB:4BUB"
FT STRAND 103..112
FT /evidence="ECO:0007829|PDB:4BUB"
FT HELIX 114..126
FT /evidence="ECO:0007829|PDB:4BUB"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:4BUB"
FT HELIX 156..168
FT /evidence="ECO:0007829|PDB:4BUB"
FT STRAND 172..177
FT /evidence="ECO:0007829|PDB:4BUB"
FT HELIX 182..185
FT /evidence="ECO:0007829|PDB:4BUB"
FT TURN 186..188
FT /evidence="ECO:0007829|PDB:4BUB"
FT STRAND 193..198
FT /evidence="ECO:0007829|PDB:4BUB"
FT STRAND 203..207
FT /evidence="ECO:0007829|PDB:4BUB"
FT STRAND 209..211
FT /evidence="ECO:0007829|PDB:4BUB"
FT HELIX 212..220
FT /evidence="ECO:0007829|PDB:4BUB"
FT HELIX 221..223
FT /evidence="ECO:0007829|PDB:4BUB"
FT STRAND 226..235
FT /evidence="ECO:0007829|PDB:4BUB"
FT HELIX 236..238
FT /evidence="ECO:0007829|PDB:4BUB"
FT TURN 239..241
FT /evidence="ECO:0007829|PDB:4BUB"
FT STRAND 246..254
FT /evidence="ECO:0007829|PDB:4BUB"
FT STRAND 257..261
FT /evidence="ECO:0007829|PDB:4BUB"
FT STRAND 272..276
FT /evidence="ECO:0007829|PDB:4BUB"
FT STRAND 282..285
FT /evidence="ECO:0007829|PDB:4BUB"
FT HELIX 293..305
FT /evidence="ECO:0007829|PDB:4BUB"
FT TURN 306..308
FT /evidence="ECO:0007829|PDB:4BUB"
FT HELIX 311..315
FT /evidence="ECO:0007829|PDB:4BUB"
FT TURN 316..320
FT /evidence="ECO:0007829|PDB:4BUB"
FT STRAND 327..330
FT /evidence="ECO:0007829|PDB:4BUB"
FT HELIX 332..334
FT /evidence="ECO:0007829|PDB:4BUB"
FT TURN 335..338
FT /evidence="ECO:0007829|PDB:4BUB"
FT STRAND 340..343
FT /evidence="ECO:0007829|PDB:4BUB"
FT HELIX 349..362
FT /evidence="ECO:0007829|PDB:4BUB"
FT STRAND 367..371
FT /evidence="ECO:0007829|PDB:4BUB"
FT HELIX 383..392
FT /evidence="ECO:0007829|PDB:4BUB"
FT STRAND 394..398
FT /evidence="ECO:0007829|PDB:4BUB"
FT STRAND 404..406
FT /evidence="ECO:0007829|PDB:4BUB"
FT HELIX 409..416
FT /evidence="ECO:0007829|PDB:4BUB"
FT STRAND 425..427
FT /evidence="ECO:0007829|PDB:4BUB"
FT HELIX 431..441
FT /evidence="ECO:0007829|PDB:4BUB"
FT STRAND 447..450
FT /evidence="ECO:0007829|PDB:4BUB"
FT STRAND 458..462
FT /evidence="ECO:0007829|PDB:4BUB"
FT STRAND 465..468
FT /evidence="ECO:0007829|PDB:4BUB"
FT HELIX 471..484
FT /evidence="ECO:0007829|PDB:4BUB"
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
