(data stored in ACNUC7421 zone)

SWISSPROT: MURD_ECO57

ID   MURD_ECO57              Reviewed;         438 AA.
AC   Q8X9Y9;
DT   30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   07-JUN-2017, entry version 107.
DE   RecName: Full=UDP-N-acetylmuramoylalanine--D-glutamate ligase;
DE            EC=6.3.2.9;
DE   AltName: Full=D-glutamic acid-adding enzyme;
DE   AltName: Full=UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase;
GN   Name=murD; OrderedLocusNames=Z0098, ECs0092;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Cell wall formation. Catalyzes the addition of glutamate
CC       to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: ATP + UDP-N-acetyl-alpha-D-muramoyl-L-alanine
CC       + D-glutamate = ADP + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-
CC       alanyl-D-glutamate.
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the MurCDEF family. {ECO:0000305}.
DR   EMBL; AE005174; AAG54392.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB33515.1; -; Genomic_DNA.
DR   PIR; D85491; D85491.
DR   PIR; D90640; D90640.
DR   RefSeq; NP_308119.1; NC_002695.1.
DR   RefSeq; WP_000796483.1; NZ_MKIV01000001.1.
DR   ProteinModelPortal; Q8X9Y9; -.
DR   SMR; Q8X9Y9; -.
DR   STRING; 155864.Z0098; -.
DR   EnsemblBacteria; AAG54392; AAG54392; Z0098.
DR   EnsemblBacteria; BAB33515; BAB33515; BAB33515.
DR   GeneID; 913546; -.
DR   KEGG; ece:Z0098; -.
DR   KEGG; ecs:ECs0092; -.
DR   PATRIC; fig|386585.9.peg.192; -.
DR   eggNOG; ENOG4105DMZ; Bacteria.
DR   eggNOG; COG0771; LUCA.
DR   HOGENOM; HOG000049427; -.
DR   KO; K01925; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008764; F:UDP-N-acetylmuramoylalanine-D-glutamate 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-UniPathway.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.1190.10; -; 1.
DR   HAMAP; MF_00639; MurD; 1.
DR   InterPro; IPR004101; Mur_ligase_C.
DR   InterPro; IPR013221; Mur_ligase_cen.
DR   InterPro; IPR005762; UDP-N-AcMur-Glu_ligase.
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   TIGRFAMs; TIGR01087; murD; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q8X9Y9.
DR   SWISS-2DPAGE; Q8X9Y9.
KW   ATP-binding; Cell cycle; Cell division; Cell shape;
KW   Cell wall biogenesis/degradation; Complete proteome; Cytoplasm;
KW   Ligase; Nucleotide-binding; Peptidoglycan synthesis.
FT   INIT_MET      1      1       Removed. {ECO:0000250}.
FT   CHAIN         2    438       UDP-N-acetylmuramoylalanine--D-glutamate
FT                                ligase.
FT                                /FTId=PRO_0000109014.
FT   NP_BIND     112    118       ATP. {ECO:0000255}.
SQ   SEQUENCE   438 AA;  47002 MW;  0ED6588DD098F776 CRC64;
     MADYQGKNVV IIGLGLTGLS CVDFFLARGV TPRVMDTRMT PPGLDKLPEA VERHTGSLND
     EWLMAADLIV ASPGIALAHP SLSAAADAGI EIVGDIELFC REAQAPIVAI TGSNGKSTVT
     TLVGEMAKAA GVNVGVGGNI GLPALMLLDD ECELYVLELS SFQLETTSSL QAVAATILNV
     TEDHMDRYPF GLQQYRAAKL RIYENAKVCV VNADDALTMP IRGADERCVS FGVNMGDYHL
     NHQQGETWLR VKGEKVLNVK EMKLSGQHNY TNALAALALA DAAGLPRASS LKALTTFTGL
     PHRFEVVLEH NGVRWINDSK ATNVGSTEAA LNGLHVDGTL HLLLGGDGKS ADFSPLARYL
     NGDNVRLYCF GRDGVQLAAL RPEVAEQTET MEQAMRLLAP RVQPGDMVLL SPACASLDQF
     KNFEQRGNEF ARLAKELG
//

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