ID A0A7W9IBB9_9ACTN Unreviewed; 389 AA. AC A0A7W9IBB9; DT 02-JUN-2021, integrated into UniProtKB/TrEMBL. DT 02-JUN-2021, sequence version 1. DT 03-AUG-2022, entry version 4. 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=F4562_000641 {ECO:0000313|EMBL:MBB5817579.1}; OS Streptosporangium becharense. OC Bacteria; Actinobacteria; Streptosporangiales; Streptosporangiaceae; OC Streptosporangium. OX NCBI_TaxID=1816182 {ECO:0000313|EMBL:MBB5817579.1, ECO:0000313|Proteomes:UP000540685}; RN [1] {ECO:0000313|EMBL:MBB5817579.1, ECO:0000313|Proteomes:UP000540685} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 46887 {ECO:0000313|EMBL:MBB5817579.1, RC ECO:0000313|Proteomes:UP000540685}; RA Klenk H.-P.; RT "Sequencing the genomes of 1000 actinobacteria strains."; RL Submitted (AUG-2020) 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 -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00033}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:MBB5817579.1}. 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; JACHMP010000001; MBB5817579.1; -; Genomic_DNA. DR UniPathway; UPA00219; -. DR Proteomes; UP000540685; Unassembled WGS sequence. 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-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. 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}; Reference proteome {ECO:0000313|Proteomes:UP000540685}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00033}. FT DOMAIN 12..158 FT /note="Glyco_transf_28" FT /evidence="ECO:0000259|Pfam:PF03033" FT DOMAIN 208..372 FT /note="Glyco_tran_28_C" FT /evidence="ECO:0000259|Pfam:PF04101" FT REGION 18..20 FT /note="UDP-N-acetyl-alpha-D-glucosamine binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00033" FT BINDING 184 FT /ligand="UDP-N-acetyl-alpha-D-glucosamine" FT /ligand_id="ChEBI:CHEBI:57705" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00033" FT BINDING 316 FT /ligand="UDP-N-acetyl-alpha-D-glucosamine" FT /ligand_id="ChEBI:CHEBI:57705" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00033" SQ SEQUENCE 389 AA; 41238 MW; 3136C5ED291707BB CRC64; MMAGERRTLR LLVTGGGTGG HTYPALTTVM ALRDYAVGRG FDFDVLWVGT ESGLEARVSA EHGIPFRAIK AGKLRRSPNL RELATNVADM FRVPIGVLQA FGVAARYRPD VVLSTGGYVC VPLGVASRLL GRPLVMHEQI TALGLANRIL SRFARRIALT HPSSIEHLPA GARERAVVTG NPIRPHLLRG NVDAARRHFG LAHGFPLVYV TGGAQGSRQI NTLIEEILPA LLTRAQVIHQ CGPDWIGRFT EAAAALPAEL RDRYRPVAYV GGELPHVFAA ADVVVSRSGA GTVAELTAVG KASVLIPLVP SAADEQRQNA RYLAEAGAAR ALLDDKPTAD RLLAELDLLL RDPATRAAMA GAAQSLGRVD AADALAQVLL AEAEAVKAG //