ID J7T3U9_CLOSG Unreviewed; 349 AA. AC J7T3U9; DT 31-OCT-2012, integrated into UniProtKB/TrEMBL. DT 31-OCT-2012, sequence version 1. DT 04-FEB-2015, entry version 12. 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 ECO:0000313|EMBL:EDU36093.1}; GN ORFNames=CLOSPO_02261 {ECO:0000313|EMBL:EDU36093.1}; OS Clostridium sporogenes ATCC 15579. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=471871 {ECO:0000313|EMBL:EDU36093.1}; RN [1] {ECO:0000313|EMBL:EDU36093.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 15579 {ECO:0000313|EMBL:EDU36093.1}; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., RA Liep D., Gordon J.; RT "Draft genome sequence of Clostridium sporogenes ATCC 15579."; RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EDU36093.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 15579 {ECO:0000313|EMBL:EDU36093.1}; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., RA Wilson R.K.; 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: 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:0000256|HAMAP-Rule:MF_00033, CC ECO:0000256|SAAS:SAAS00082927}. 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 -!- 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 GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro. 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-HAMAP. 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-HAMAP. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR GO; GO:0019277; P:UDP-N-acetylgalactosamine biosynthetic process; IEA:InterPro. DR HAMAP; MF_00033; MurG; 1. DR InterPro; IPR006009; GlcNAc_MurG. DR InterPro; IPR004276; Glyco_trans_28. DR InterPro; IPR007235; Glyco_trans_28_C. 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:SAAS00082900}; KW Cell division {ECO:0000256|HAMAP-Rule:MF_00033, KW ECO:0000256|SAAS:SAAS00082883}; 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:SAAS00082936}; KW Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_00033, KW ECO:0000256|SAAS:SAAS00082861}; KW Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_00033, KW ECO:0000256|SAAS:SAAS00082834}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_00033, KW ECO:0000256|SAAS:SAAS00082910}; KW Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_00033, KW ECO:0000256|SAAS:SAAS00082885}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00033, KW ECO:0000256|SAAS:SAAS00082939}. 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 //