(data stored in ACNUC7421 zone)

SWISSPROT: MURG_ECODH

ID   MURG_ECODH              Reviewed;         355 AA.
AC   B1XC67;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   05-JUL-2017, entry version 62.
DE   RecName: Full=UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase {ECO:0000255|HAMAP-Rule:MF_00033};
DE            EC=2.4.1.227 {ECO:0000255|HAMAP-Rule:MF_00033};
DE   AltName: Full=Undecaprenyl-PP-MurNAc-pentapeptide-UDPGlcNAc GlcNAc transferase {ECO:0000255|HAMAP-Rule:MF_00033};
GN   Name=murG {ECO:0000255|HAMAP-Rule:MF_00033};
GN   OrderedLocusNames=ECDH10B_0072;
OS   Escherichia coli (strain K12 / DH10B).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=316385;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / DH10B;
RX   PubMed=18245285; DOI=10.1128/JB.01695-07;
RA   Durfee T., Nelson R., Baldwin S., Plunkett G. III, Burland V., Mau B.,
RA   Petrosino J.F., Qin X., Muzny D.M., Ayele M., Gibbs R.A., Csorgo B.,
RA   Posfai G., Weinstock G.M., Blattner F.R.;
RT   "The complete genome sequence of Escherichia coli DH10B: insights into
RT   the biology of a laboratory workhorse.";
RL   J. Bacteriol. 190:2597-2606(2008).
CC   -!- FUNCTION: Cell wall formation. Catalyzes the transfer of a GlcNAc
CC       subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid
CC       intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-
CC       (pentapeptide)GlcNAc (lipid intermediate II). {ECO:0000255|HAMAP-
CC       Rule:MF_00033}.
CC   -!- CATALYTIC ACTIVITY: UDP-N-acetylglucosamine + Mur2Ac(oyl-L-Ala-
CC       gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol = UDP +
CC       GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-
CC       diphosphoundecaprenol. {ECO:0000255|HAMAP-Rule:MF_00033}.
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00033}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00033}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_00033}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 28 family. MurG
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00033}.
DR   EMBL; CP000948; ACB01271.1; -; Genomic_DNA.
DR   RefSeq; WP_000016560.1; NC_010473.1.
DR   ProteinModelPortal; B1XC67; -.
DR   SMR; B1XC67; -.
DR   CAZy; GT28; Glycosyltransferase Family 28.
DR   EnsemblBacteria; ACB01271; ACB01271; ECDH10B_0072.
DR   KEGG; ecd:ECDH10B_0072; -.
DR   eggNOG; ENOG4105DVQ; Bacteria.
DR   eggNOG; COG0707; LUCA.
DR   HOGENOM; HOG000218321; -.
DR   KO; K02563; -.
DR   OMA; HQTKNAM; -.
DR   UniPathway; UPA00219; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0051991; F:UDP-N-acetyl-D-glucosamine:N-acetylmuramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimelyl-D-alanyl-D-alanine-diphosphoundecaprenol 4-beta-N-acetylglucosaminlytransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050511; F:undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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:0030259; P:lipid glycosylation; IEA:InterPro.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   CDD; cd03785; GT1_MurG; 1.
DR   HAMAP; MF_00033; MurG; 1.
DR   InterPro; IPR006009; GlcNAc_MurG.
DR   InterPro; IPR007235; Glyco_trans_28_C.
DR   InterPro; IPR004276; GlycoTrans_28_N.
DR   Pfam; PF04101; Glyco_tran_28_C; 1.
DR   Pfam; PF03033; Glyco_transf_28; 1.
DR   TIGRFAMs; TIGR01133; murG; 1.
PE   3: Inferred from homology;
DR   PRODOM; B1XC67.
DR   SWISS-2DPAGE; B1XC67.
KW   Cell cycle; Cell division; Cell inner membrane; Cell membrane;
KW   Cell shape; Cell wall biogenesis/degradation; Glycosyltransferase;
KW   Membrane; Peptidoglycan synthesis; Transferase.
FT   CHAIN         1    355       UDP-N-acetylglucosamine--N-acetylmuramyl-
FT                                (pentapeptide) pyrophosphoryl-
FT                                undecaprenol N-acetylglucosamine
FT                                transferase.
FT                                /FTId=PRO_1000090429.
SQ   SEQUENCE   355 AA;  37815 MW;  DE347361A7B9293A CRC64;
     MSGQGKRLMV MAGGTGGHVF PGLAVAHHLM AQGWQVRWLG TADRMEADLV PKHGIEIDFI
     RISGLRGKGI KALIAAPLRI FNAWRQARAI MKAYKPDVVL GMGGYVSGPG GLAAWSLGIP
     VVLHEQNGIA GLTNKWLAKI ATKVMQAFPG AFPNAEVVGN PVRTDVLALP LPQQRLAGRE
     GPVRVLVVGG SQGARILNQT MPQVAAKLGD SVTIWHQSGK GSQQSVEQAY AEAGQPQHKV
     TEFIDDMAAA YAWADVVVCR SGALTVSEIA AAGLPALFVP FQHKDRQQYW NALPLEKAGA
     AKIIEQPQLS VDAVANTLAG WSRETLLTMA ERARAASIPD ATERVANEVS RVARA
//

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