(data stored in ACNUC30630 zone)

SWISSPROT: MURE_DEIRA

ID   MURE_DEIRA              Reviewed;         490 AA.
AC   Q9RXL3;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   11-DEC-2019, entry version 129.
DE   RecName: Full=UDP-N-acetylmuramyl-tripeptide synthetase {ECO:0000255|HAMAP-Rule:MF_00208};
DE            EC=6.3.2.- {ECO:0000255|HAMAP-Rule:MF_00208};
DE   AltName: Full=UDP-MurNAc-tripeptide synthetase {ECO:0000255|HAMAP-Rule:MF_00208};
GN   Name=murE {ECO:0000255|HAMAP-Rule:MF_00208}; OrderedLocusNames=DR_0297;
OS   Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS   4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=243230;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC   9279 / R1 / VKM B-1422;
RX   PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA   White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA   Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA   Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA   Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA   Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA   Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA   Fraser C.M.;
RT   "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT   R1.";
RL   Science 286:1571-1577(1999).
CC   -!- FUNCTION: Catalyzes the addition of an amino acid to the nucleotide
CC       precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the
CC       biosynthesis of bacterial cell-wall peptidoglycan. {ECO:0000255|HAMAP-
CC       Rule:MF_00208}.
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00208}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00208}.
CC   -!- PTM: Carboxylation is probably crucial for Mg(2+) binding and,
CC       consequently, for the gamma-phosphate positioning of ATP.
CC       {ECO:0000255|HAMAP-Rule:MF_00208}.
CC   -!- SIMILARITY: Belongs to the MurCDEF family. MurE subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00208}.
DR   EMBL; AE000513; AAF09877.1; -; Genomic_DNA.
DR   PIR; B75538; B75538.
DR   RefSeq; NP_294020.1; NC_001263.1.
DR   RefSeq; WP_010886942.1; NZ_CP015081.1.
DR   SMR; Q9RXL3; -.
DR   STRING; 243230.DR_0297; -.
DR   EnsemblBacteria; AAF09877; AAF09877; DR_0297.
DR   GeneID; 1800174; -.
DR   KEGG; dra:DR_0297; -.
DR   PATRIC; fig|243230.17.peg.462; -.
DR   eggNOG; ENOG4107EEN; Bacteria.
DR   eggNOG; COG0769; LUCA.
DR   HOGENOM; HOG000268118; -.
DR   InParanoid; Q9RXL3; -.
DR   KO; K01928; -.
DR   OMA; CFMEVSS; -.
DR   OrthoDB; 1861122at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000002524; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016881; F:acid-amino acid ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
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; 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   3: Inferred from homology;
DR   PRODOM; Q9RXL3.
DR   SWISS-2DPAGE; Q9RXL3.
KW   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-acetylmuramyl-tripeptide synthetase"
FT                   /id="PRO_0000101892"
FT   NP_BIND         113..119
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00208"
FT   REGION          158..159
FT                   /note="UDP-MurNAc-L-Ala-D-Glu binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00208"
FT   BINDING         185
FT                   /note="UDP-MurNAc-L-Ala-D-Glu"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00208"
FT   BINDING         193
FT                   /note="UDP-MurNAc-L-Ala-D-Glu"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00208"
FT   MOD_RES         225
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00208"
SQ   SEQUENCE   490 AA;  52317 MW;  46C748E9768754CA CRC64;
     MRLSDLAAAL QLPAPETDPQ TDTEVTGVTH NAAWVQPGSA FVAIRGAKFD GHSFMEQAQA
     AGAVAVLGEG LADGQTSPLP YLTVPNARAA LADAAAALAG HPSRELKVVG VTGTDGKTTT
     SWLTRHLLRS AGLATGLLST VGYELPDGEL RHFPAHFTTP EAPQVQDTLR EMVAAGAQAT
     VLEASSHALS LDRVRGVDWD VAVWTHLSSE HLDFHGTLDN YFADKRKLVE RARFAVLNVD
     DPWTAQLRGI APGETTYSAE NQHADWRAQD IEERHSGLHF RVVSPAGDFQ AELPMIGRFN
     VANALAGMAA AHHLGATALQ LQAGLASFRG VPGRMELVPG GATSPRVIVD FAHTPPSLEK
     ALGTLRATTA GHLWVVIGSA GGPRDPYKRA PLGEVATRLA DHAILTEEDC RDTPLQDILN
     EMERGAREEG RSNFVSIGDR REAIRYAVTH AQPGDTVLLA GKGPEDTLER ATETLPWNEV
     AEARAVLAER
//

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