MURG_ECOLI
ID MURG_ECOLI Reviewed; 355 AA.
AC P17443;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 198.
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, ECO:0000269|PubMed:10338150, ECO:0000269|PubMed:1649817};
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, ECO:0000303|PubMed:2187180};
GN OrderedLocusNames=b0090, JW0088;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2197603; DOI=10.1093/nar/18.13.4014;
RA Ikeda M., Wachi M., Jung H.K., Ishino F., Matsuhashi M.;
RT "Nucleotide sequence involving murG and murC in the mra gene cluster region
RT of Escherichia coli.";
RL Nucleic Acids Res. 18:4014-4014(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1630901; DOI=10.1093/nar/20.13.3305;
RA Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K.,
RA Mizobuchi K., Nakata A.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 0-
RT 2.4 min region.";
RL Nucleic Acids Res. 20:3305-3308(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 9-355.
RC STRAIN=K12;
RX PubMed=2187180; DOI=10.1093/nar/18.9.2810;
RA Mengin-Lecreulx D., Texier L., van Heijenoort J.;
RT "Nucleotide sequence of the cell-envelope murG gene of Escherichia coli.";
RL Nucleic Acids Res. 18:2810-2810(1990).
RN [6]
RP PROTEIN SEQUENCE OF 2-18, FUNCTION, CATALYTIC ACTIVITY, PATHWAY,
RP SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=1649817; DOI=10.1128/jb.173.15.4625-4636.1991;
RA Mengin-Lecreulx D., Texier L., Rousseau M., van Heijenoort J.;
RT "The murG gene of Escherichia coli codes for the UDP-N-acetylglucosamine:
RT N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-
RT acetylglucosamine transferase involved in the membrane steps of
RT peptidoglycan synthesis.";
RL J. Bacteriol. 173:4625-4636(1991).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=8449890; DOI=10.1128/jb.175.6.1841-1843.1993;
RA Bupp K., van Heijenoort J.;
RT "The final step of peptidoglycan subunit assembly in Escherichia coli
RT occurs in the cytoplasm.";
RL J. Bacteriol. 175:1841-1843(1993).
RN [8]
RP CATALYTIC ACTIVITY.
RC STRAIN=K12 / ATCC 35607 / JM83;
RX PubMed=10338150; DOI=10.1016/s0014-5793(99)00412-3;
RA Crouvoisier M., Mengin-Lecreulx D., van Heijenoort J.;
RT "UDP-N-acetylglucosamine:N-acetylmuramoyl-(pentapeptide) pyrophosphoryl
RT undecaprenol N-acetylglucosamine transferase from Escherichia coli:
RT overproduction, solubilization, and purification.";
RL FEBS Lett. 449:289-292(1999).
RN [9]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH MREB AND MRAY.
RX PubMed=17640276; DOI=10.1111/j.1365-2958.2007.05851.x;
RA Mohammadi T., Karczmarek A., Crouvoisier M., Bouhss A., Mengin-Lecreulx D.,
RA den Blaauwen T.;
RT "The essential peptidoglycan glycosyltransferase MurG forms a complex with
RT proteins involved in lateral envelope growth as well as with proteins
RT involved in cell division in Escherichia coli.";
RL Mol. Microbiol. 65:1106-1121(2007).
RN [10] {ECO:0007744|PDB:1F0K}
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RX PubMed=10892798; DOI=10.1110/ps.9.6.1045;
RA Ha S., Walker D., Shi Y., Walker S.;
RT "The 1.9 A crystal structure of Escherichia coli MurG, a membrane-
RT associated glycosyltransferase involved in peptidoglycan biosynthesis.";
RL Protein Sci. 9:1045-1052(2000).
RN [11] {ECO:0007744|PDB:1NLM}
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 2-355 IN COMPLEX WITH
RP UDP-N-ACETYL-ALPHA-D-GLUCOSAMINE, FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND MUTAGENESIS OF THR-15; HIS-18;
RP ASN-127; SER-191; GLU-268 AND GLN-288.
RX PubMed=12538870; DOI=10.1073/pnas.0235749100;
RA Hu Y., Chen L., Ha S., Gross B., Falcone B., Walker D., Mokhtarzadeh M.,
RA Walker S.;
RT "Crystal structure of the MurG:UDP-GlcNAc complex reveals common structural
RT principles of a superfamily of glycosyltransferases.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:845-849(2003).
CC -!- FUNCTION: Cell wall formation (PubMed:1649817). Catalyzes the transfer
CC of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide
CC (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-
CC (pentapeptide)GlcNAc (lipid intermediate II) (PubMed:1649817,
CC PubMed:12538870). Strongly prefers UDP to CDP, GDP, ADP and TDP
CC (PubMed:12538870). {ECO:0000269|PubMed:12538870,
CC ECO:0000269|PubMed:1649817}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=di-trans-octa-cis-undecaprenyl diphospho-N-acetyl-alpha-D-
CC muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-
CC alanine + UDP-N-acetyl-alpha-D-glucosamine = di-trans-octa-cis-
CC undecaprenyl diphospho-[N-acetyl-alpha-D-glucosaminyl-(1->4)]-N-
CC acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-
CC D-alanyl-D-alanine + H(+) + UDP; Xref=Rhea:RHEA:31227,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:61387, ChEBI:CHEBI:61388; EC=2.4.1.227;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00033,
CC ECO:0000269|PubMed:10338150, ECO:0000269|PubMed:12538870,
CC ECO:0000269|PubMed:1649817};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.053 mM for lipid I {ECO:0000269|PubMed:12538870};
CC KM=0.053 mM for UDP-N-acetyl-alpha-D-glucosamine
CC {ECO:0000269|PubMed:12538870};
CC Note=kcat is 837 min(-1). {ECO:0000269|PubMed:12538870};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00033, ECO:0000269|PubMed:1649817}.
CC -!- SUBUNIT: Homodimer (PubMed:12538870). Associates with MreB and MraY
CC (PubMed:17640276). {ECO:0000269|PubMed:12538870,
CC ECO:0000269|PubMed:17640276}.
CC -!- INTERACTION:
CC P17443; P0AGJ5: yfiF; NbExp=3; IntAct=EBI-554881, EBI-547368;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00033, ECO:0000269|PubMed:1649817, ECO:0000269|PubMed:17640276,
CC ECO:0000269|PubMed:8449890}; Peripheral membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_00033, ECO:0000269|PubMed:1649817,
CC ECO:0000269|PubMed:17640276, ECO:0000269|PubMed:8449890}; Cytoplasmic
CC side {ECO:0000255|HAMAP-Rule:MF_00033, ECO:0000269|PubMed:8449890}.
CC Note=Randomly distributed in the cell envelope with a higher intensity
CC at the division site. Mid-cell localization requires divisome
CC components. {ECO:0000269|PubMed:17640276}.
CC -!- DISRUPTION PHENOTYPE: Inactivation of the gene rapidly inhibits
CC peptidoglycan synthesis in exponentially growing cells.
CC {ECO:0000269|PubMed:1649817}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 28 family. MurG
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00033}.
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DR EMBL; X52644; CAA36867.1; -; Genomic_DNA.
DR EMBL; X52540; CAA36776.1; -; Genomic_DNA.
DR EMBL; X55034; CAA38867.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73201.1; -; Genomic_DNA.
DR EMBL; AP009048; BAB96658.1; -; Genomic_DNA.
DR PIR; JQ0544; BVECMG.
DR RefSeq; NP_414632.1; NC_000913.3.
DR RefSeq; WP_000016560.1; NZ_SSZK01000004.1.
DR PDB; 1F0K; X-ray; 1.90 A; A/B=1-355.
DR PDB; 1NLM; X-ray; 2.50 A; A/B=2-355.
DR PDBsum; 1F0K; -.
DR PDBsum; 1NLM; -.
DR AlphaFoldDB; P17443; -.
DR SMR; P17443; -.
DR BioGRID; 4261859; 572.
DR BioGRID; 850678; 1.
DR DIP; DIP-10282N; -.
DR IntAct; P17443; 27.
DR STRING; 511145.b0090; -.
DR ChEMBL; CHEMBL3596078; -.
DR DrugBank; DB02196; Uridine-Diphosphate-N-Acetylgalactosamine.
DR DrugCentral; P17443; -.
DR SwissLipids; SLP:000001814; -.
DR CAZy; GT28; Glycosyltransferase Family 28.
DR jPOST; P17443; -.
DR PaxDb; P17443; -.
DR PRIDE; P17443; -.
DR EnsemblBacteria; AAC73201; AAC73201; b0090.
DR EnsemblBacteria; BAB96658; BAB96658; BAB96658.
DR GeneID; 946321; -.
DR KEGG; ecj:JW0088; -.
DR KEGG; eco:b0090; -.
DR PATRIC; fig|1411691.4.peg.2190; -.
DR EchoBASE; EB0618; -.
DR eggNOG; COG0707; Bacteria.
DR HOGENOM; CLU_037404_2_0_6; -.
DR InParanoid; P17443; -.
DR OMA; AADMMLC; -.
DR PhylomeDB; P17443; -.
DR BioCyc; EcoCyc:NACGLCTRANS-MON; -.
DR BioCyc; MetaCyc:NACGLCTRANS-MON; -.
DR BRENDA; 2.4.1.227; 2026.
DR SABIO-RK; P17443; -.
DR UniPathway; UPA00219; -.
DR EvolutionaryTrace; P17443; -.
DR PRO; PR:P17443; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016757; F:glycosyltransferase activity; IBA:GO_Central.
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; IDA:EcoliWiki.
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:UniProtKB-UniRule.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IMP:EcoCyc.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
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 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Cell inner membrane;
KW Cell membrane; Cell shape; Cell wall biogenesis/degradation;
KW Direct protein sequencing; Glycosyltransferase; Membrane;
KW Peptidoglycan synthesis; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1649817"
FT CHAIN 2..355
FT /note="UDP-N-acetylglucosamine--N-acetylmuramyl-
FT (pentapeptide) pyrophosphoryl-undecaprenol N-
FT acetylglucosamine transferase"
FT /id="PRO_0000109170"
FT BINDING 15..17
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00033,
FT ECO:0000269|PubMed:12538870, ECO:0007744|PDB:1NLM"
FT BINDING 127
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00033,
FT ECO:0000269|PubMed:12538870, ECO:0007744|PDB:1NLM"
FT BINDING 163
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00033,
FT ECO:0000269|PubMed:12538870, ECO:0007744|PDB:1NLM"
FT BINDING 191
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00033"
FT BINDING 244
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00033,
FT ECO:0000269|PubMed:12538870, ECO:0007744|PDB:1NLM"
FT BINDING 263..268
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00033,
FT ECO:0000269|PubMed:12538870, ECO:0007744|PDB:1NLM"
FT BINDING 287..288
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000269|PubMed:12538870,
FT ECO:0007744|PDB:1NLM"
FT MUTAGEN 15
FT /note="T->A: 387-fold decrease in kcat."
FT /evidence="ECO:0000269|PubMed:12538870"
FT MUTAGEN 18
FT /note="H->A: Almost loss of activity."
FT /evidence="ECO:0000269|PubMed:12538870"
FT MUTAGEN 127
FT /note="N->A: 64-fold decrase in kcat."
FT /evidence="ECO:0000269|PubMed:12538870"
FT MUTAGEN 191
FT /note="S->A: 40-fold decrease in kcat."
FT /evidence="ECO:0000269|PubMed:12538870"
FT MUTAGEN 268
FT /note="E->A: 1.6-fold decrease in kcat."
FT /evidence="ECO:0000269|PubMed:12538870"
FT MUTAGEN 268
FT /note="E->D: 1.4-fold decrease in kcat."
FT /evidence="ECO:0000269|PubMed:12538870"
FT MUTAGEN 288
FT /note="Q->A: 114-fold decrease in kcat."
FT /evidence="ECO:0000269|PubMed:12538870"
FT STRAND 7..11
FT /evidence="ECO:0007829|PDB:1F0K"
FT HELIX 16..30
FT /evidence="ECO:0007829|PDB:1F0K"
FT TURN 31..33
FT /evidence="ECO:0007829|PDB:1F0K"
FT STRAND 35..40
FT /evidence="ECO:0007829|PDB:1F0K"
FT HELIX 46..49
FT /evidence="ECO:0007829|PDB:1F0K"
FT HELIX 50..53
FT /evidence="ECO:0007829|PDB:1F0K"
FT STRAND 56..59
FT /evidence="ECO:0007829|PDB:1F0K"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:1NLM"
FT HELIX 70..74
FT /evidence="ECO:0007829|PDB:1F0K"
FT HELIX 77..94
FT /evidence="ECO:0007829|PDB:1F0K"
FT STRAND 97..101
FT /evidence="ECO:0007829|PDB:1F0K"
FT HELIX 107..116
FT /evidence="ECO:0007829|PDB:1F0K"
FT STRAND 121..125
FT /evidence="ECO:0007829|PDB:1F0K"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:1F0K"
FT HELIX 132..137
FT /evidence="ECO:0007829|PDB:1F0K"
FT TURN 138..140
FT /evidence="ECO:0007829|PDB:1F0K"
FT STRAND 142..148
FT /evidence="ECO:0007829|PDB:1F0K"
FT STRAND 151..154
FT /evidence="ECO:0007829|PDB:1F0K"
FT HELIX 164..167
FT /evidence="ECO:0007829|PDB:1F0K"
FT HELIX 172..176
FT /evidence="ECO:0007829|PDB:1F0K"
FT STRAND 181..188
FT /evidence="ECO:0007829|PDB:1F0K"
FT TURN 190..192
FT /evidence="ECO:0007829|PDB:1F0K"
FT HELIX 195..208
FT /evidence="ECO:0007829|PDB:1F0K"
FT HELIX 209..211
FT /evidence="ECO:0007829|PDB:1F0K"
FT STRAND 212..217
FT /evidence="ECO:0007829|PDB:1F0K"
FT HELIX 223..232
FT /evidence="ECO:0007829|PDB:1F0K"
FT STRAND 238..242
FT /evidence="ECO:0007829|PDB:1F0K"
FT HELIX 247..253
FT /evidence="ECO:0007829|PDB:1F0K"
FT STRAND 255..259
FT /evidence="ECO:0007829|PDB:1F0K"
FT HELIX 263..272
FT /evidence="ECO:0007829|PDB:1F0K"
FT STRAND 276..278
FT /evidence="ECO:0007829|PDB:1F0K"
FT HELIX 287..297
FT /evidence="ECO:0007829|PDB:1F0K"
FT STRAND 300..303
FT /evidence="ECO:0007829|PDB:1F0K"
FT HELIX 306..308
FT /evidence="ECO:0007829|PDB:1F0K"
FT HELIX 311..319
FT /evidence="ECO:0007829|PDB:1F0K"
FT HELIX 323..335
FT /evidence="ECO:0007829|PDB:1F0K"
FT HELIX 341..353
FT /evidence="ECO:0007829|PDB:1F0K"
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
