ID J7T3U9_CLOS1 Unreviewed; 349 AA. AC J7T3U9; DT 31-OCT-2012, integrated into UniProtKB/TrEMBL. DT 31-OCT-2012, sequence version 1. DT 31-JUL-2019, entry version 31. DE RecName: Full=UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase {ECO:0000256|HAMAP-Rule:MF_00033, ECO:0000256|SAAS:SAAS00082867}; DE EC=2.4.1.227 {ECO:0000256|HAMAP-Rule:MF_00033, ECO:0000256|SAAS:SAAS00082938}; 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 ECO:0000313|EMBL:EDU36093.1}; GN ORFNames=CLOSPO_02261 {ECO:0000313|EMBL:EDU36093.1}; OS Clostridium sporogenes (strain ATCC 15579). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=471871 {ECO:0000313|EMBL:EDU36093.1, ECO:0000313|Proteomes:UP000006610}; RN [1] {ECO:0000313|Proteomes:UP000006610} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 15579 {ECO:0000313|Proteomes:UP000006610}; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J., Fulton L., Clifton S., Fulton B., Xu J., Minx P., RA Pepin K.H., Johnson M., Thiruvilangam P., Bhonagiri V., Nash W.E., RA Mardis E.R., Wilson R.K.; RT "Draft genome sequence of Clostridium sporogenes ATCC 15579."; RL Submitted (MAY-2008) 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, ECO:0000256|SAAS:SAAS00082940}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)- CC diphospho-di-trans,octa-cis-undecaprenol + UDP-N-acetyl-alpha-D- CC glucosamine = beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu- CC L-Lys-D-Ala-D-Ala)-diphospho-di-trans,octa-cis-undecaprenol + CC H(+) + UDP; Xref=Rhea:RHEA:23192, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:60032, CC ChEBI:CHEBI:60033; EC=2.4.1.227; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00033, ECO:0000256|SAAS:SAAS01209325}; CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. CC {ECO:0000256|HAMAP-Rule:MF_00033, ECO:0000256|SAAS:SAAS00082937}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP- CC Rule:MF_00033}; Peripheral membrane protein {ECO:0000256|HAMAP- CC Rule:MF_00033}. CC -!- SIMILARITY: Belongs to the glycosyltransferase 28 family. MurG CC subfamily. {ECO:0000256|HAMAP-Rule:MF_00033, CC ECO:0000256|SAAS:SAAS00569248}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EDU36093.1}. 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; ABKW02000004; EDU36093.1; -; Genomic_DNA. DR EnsemblBacteria; EDU36093; EDU36093; CLOSPO_02261. DR UniPathway; UPA00219; -. DR Proteomes; UP000006610; 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. DR TIGRFAMs; TIGR01133; murG; 1. PE 3: Inferred from homology; KW Cell cycle {ECO:0000256|HAMAP-Rule:MF_00033, KW ECO:0000256|SAAS:SAAS00458215}; KW Cell division {ECO:0000256|HAMAP-Rule:MF_00033, KW ECO:0000256|SAAS:SAAS00458169}; KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_00033, KW ECO:0000256|SAAS:SAAS00082922}; KW Cell shape {ECO:0000256|HAMAP-Rule:MF_00033, KW ECO:0000256|SAAS:SAAS00458137}; KW Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_00033, KW ECO:0000256|SAAS:SAAS00458192}; KW Complete proteome {ECO:0000313|Proteomes:UP000006610}; KW Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_00033, KW ECO:0000256|SAAS:SAAS00458141, ECO:0000313|EMBL:EDU36093.1}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_00033, KW ECO:0000256|SAAS:SAAS00458209}; KW Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_00033, KW ECO:0000256|SAAS:SAAS00458156}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00033, KW ECO:0000256|SAAS:SAAS00458181, ECO:0000313|EMBL:EDU36093.1}. FT DOMAIN 1 136 Glyco_transf_28. {ECO:0000259|Pfam: FT PF03033}. FT DOMAIN 183 340 Glyco_tran_28_C. {ECO:0000259|Pfam: FT PF04101}. SQ SEQUENCE 349 AA; 38888 MW; 19AFB38B3D9644D9 CRC64; MTGGGTAGHV TPNLALVPEL KKLGYEIKYI GSIEGIERKI IKKEGIEYFP ISSGKLRRYF DLKNFSDPFK VLKGVFQAKK IIKREKPDII FSKGGFVTVP VVIAAHLNKI PVIAHESDIT PGLANKLATP YCTKVCVTFP ESIKHIKGDK AVLTGTPIRK ELLEGSKVKG IELCGFKDDK PILLIIGGSL GSKIINEIVR KNLDDILLKF NIIHICGKSN LDENLENRKG YAQFEYVNEE LPDLMKASDL VISRAGANVI YELLALKKPN LLIPLSKKSS RGDQILNAGS FEKSGYSLVL KEEELSDKTL MEKLSYLYEN RNVYINNMSK SKMDNGVKNI TELIKKYTK //