ID A0A7U9A1N1_ECOLX Unreviewed; 355 AA. AC A0A7U9A1N1; DT 02-JUN-2021, integrated into UniProtKB/TrEMBL. DT 02-JUN-2021, sequence version 1. DT 14-DEC-2022, entry version 6. DE RecName: Full=UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase {ECO:0000256|HAMAP-Rule:MF_00033}; DE EC=2.4.1.227 {ECO:0000256|HAMAP-Rule:MF_00033}; DE AltName: Full=Undecaprenyl-PP-MurNAc-pentapeptide-UDPGlcNAc GlcNAc transferase {ECO:0000256|HAMAP-Rule:MF_00033}; GN Name=murG {ECO:0000256|HAMAP-Rule:MF_00033}; GN ORFNames=ECFG_03655 {ECO:0000313|EMBL:EFI22527.1}; OS Escherichia coli FVEC1302. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=656379 {ECO:0000313|EMBL:EFI22527.1, ECO:0000313|Proteomes:UP000002777}; RN [1] {ECO:0000313|Proteomes:UP000002777} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FVEC1302 {ECO:0000313|Proteomes:UP000002777}; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Feldgarden M., Gordon D.M., Johnson J.R., Johnston B.D., Young S., Zeng Q., RA Koehrsen M., Alvarado L., Berlin A.M., Borenstein D., Chapman S.B., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D., RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J., RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N., RA Walk T., White J., Yandava C., Haas B., Henn M.R., Nusbaum C., Birren B.; RT "The Genome Sequence of Escherichia coli FVEC 1302."; RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases. 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:0000256|HAMAP- CC Rule:MF_00033}. 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:0000256|HAMAP-Rule:MF_00033}; CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. CC {ECO:0000256|HAMAP-Rule:MF_00033}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00033}; CC Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_00033}; CC Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_00033}. CC -!- SIMILARITY: Belongs to the glycosyltransferase 28 family. MurG CC subfamily. {ECO:0000256|HAMAP-Rule:MF_00033}. 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; GG774899; EFI22527.1; -; Genomic_DNA. DR RefSeq; WP_000016559.1; NZ_GG774899.1. DR AlphaFoldDB; A0A7U9A1N1; -. DR SMR; A0A7U9A1N1; -. DR GeneID; 66671620; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000002777; Unassembled WGS sequence. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0050511; F:undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase activity; IEA:UniProtKB-UniRule. 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; IEA:UniProtKB-UniRule. 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 3: Inferred from homology; KW Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|HAMAP- KW Rule:MF_00033}; KW Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000256|HAMAP- KW Rule:MF_00033}; KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP- KW Rule:MF_00033}; KW Cell shape {ECO:0000256|ARBA:ARBA00022960, ECO:0000256|HAMAP- KW Rule:MF_00033}; KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316, KW ECO:0000256|HAMAP-Rule:MF_00033}; KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, ECO:0000256|HAMAP- KW Rule:MF_00033}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00033}; KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984, ECO:0000256|HAMAP- KW Rule:MF_00033}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00033}. FT DOMAIN 9..145 FT /note="Glyco_transf_28" FT /evidence="ECO:0000259|Pfam:PF03033" FT DOMAIN 185..343 FT /note="Glyco_tran_28_C" FT /evidence="ECO:0000259|Pfam:PF04101" FT BINDING 15..17 FT /ligand="UDP-N-acetyl-alpha-D-glucosamine" FT /ligand_id="ChEBI:CHEBI:57705" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00033" FT BINDING 127 FT /ligand="UDP-N-acetyl-alpha-D-glucosamine" FT /ligand_id="ChEBI:CHEBI:57705" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00033" FT BINDING 163 FT /ligand="UDP-N-acetyl-alpha-D-glucosamine" FT /ligand_id="ChEBI:CHEBI:57705" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00033" FT BINDING 191 FT /ligand="UDP-N-acetyl-alpha-D-glucosamine" FT /ligand_id="ChEBI:CHEBI:57705" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00033" FT BINDING 244 FT /ligand="UDP-N-acetyl-alpha-D-glucosamine" FT /ligand_id="ChEBI:CHEBI:57705" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00033" FT BINDING 263..268 FT /ligand="UDP-N-acetyl-alpha-D-glucosamine" FT /ligand_id="ChEBI:CHEBI:57705" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00033" FT BINDING 288 FT /ligand="UDP-N-acetyl-alpha-D-glucosamine" FT /ligand_id="ChEBI:CHEBI:57705" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00033" SQ SEQUENCE 355 AA; 37787 MW; DE34737EB7B9293A 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 RAARA //