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MURG_STRT2
ID   MURG_STRT2              Reviewed;         356 AA.
AC   Q5M4Y1;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 107.
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};
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}; OrderedLocusNames=stu0732;
OS   Streptococcus thermophilus (strain ATCC BAA-250 / LMG 18311).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=264199;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-250 / LMG 18311;
RX   PubMed=15543133; DOI=10.1038/nbt1034;
RA   Bolotin A., Quinquis B., Renault P., Sorokin A., Ehrlich S.D.,
RA   Kulakauskas S., Lapidus A., Goltsman E., Mazur M., Pusch G.D., Fonstein M.,
RA   Overbeek R., Kyprides N., Purnelle B., Prozzi D., Ngui K., Masuy D.,
RA   Hancy F., Burteau S., Boutry M., Delcour J., Goffeau A., Hols P.;
RT   "Complete sequence and comparative genome analysis of the dairy bacterium
RT   Streptococcus thermophilus.";
RL   Nat. Biotechnol. 22:1554-1558(2004).
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:0000255|HAMAP-
CC       Rule:MF_00033}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-
CC         cis-undecaprenyl diphosphate + UDP-N-acetyl-alpha-D-glucosamine =
CC         beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-
CC         di-trans,octa-cis-undecaprenyl diphosphate + H(+) + UDP;
CC         Xref=Rhea:RHEA:23192, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705,
CC         ChEBI:CHEBI:58223, ChEBI:CHEBI:60032, ChEBI:CHEBI:60033;
CC         EC=2.4.1.227; Evidence={ECO:0000255|HAMAP-Rule:MF_00033};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00033}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00033};
CC       Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_00033};
CC       Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_00033}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 28 family. MurG
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00033}.
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DR   EMBL; CP000023; AAV60425.1; -; Genomic_DNA.
DR   RefSeq; WP_011225775.1; NC_006448.1.
DR   AlphaFoldDB; Q5M4Y1; -.
DR   SMR; Q5M4Y1; -.
DR   STRING; 264199.stu0732; -.
DR   CAZy; GT28; Glycosyltransferase Family 28.
DR   EnsemblBacteria; AAV60425; AAV60425; stu0732.
DR   GeneID; 66898631; -.
DR   KEGG; stl:stu0732; -.
DR   eggNOG; COG0707; Bacteria.
DR   HOGENOM; CLU_037404_0_0_9; -.
DR   OMA; AGNEQAH; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000001170; Chromosome.
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; Cell division; Cell membrane; Cell shape;
KW   Cell wall biogenesis/degradation; Glycosyltransferase; Membrane;
KW   Peptidoglycan synthesis; Reference proteome; Transferase.
FT   CHAIN           1..356
FT                   /note="UDP-N-acetylglucosamine--N-acetylmuramyl-
FT                   (pentapeptide) pyrophosphoryl-undecaprenol N-
FT                   acetylglucosamine transferase"
FT                   /id="PRO_0000225103"
FT   BINDING         198
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00033"
FT   BINDING         289
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00033"
SQ   SEQUENCE   356 AA;  40156 MW;  9410E076DCEFE983 CRC64;
     MAKSKKIVFT GGGTVGHVTL NLILIPKFLK DGWEVHYIGD KHGVEHEQID KSGLDVTFHS
     IATGKLRRYF SWQNMLDVFK VGWGILQSIA IIAKIRPQAL FSKGGFVSVP PVIASKLLRV
     PVYVHESDLS MGLANKIAYK FATTMFTTFE QSKTLVKTRH VGAITKVGMT RFDNSDQLDK
     IKEQFDEKLK TVLFIGGSAG AKVFNDFISK TPELIENYNI INISGDSSLN TLERHLYRVD
     YVTDLYQPLM DMADLVVTRG GSNTIFELLA MKKLHLIVPL GKEASRGDQL ENADYFERKG
     YARQLQEPEL SWETLKHELE QLVEHAETYK EAMAKSEEIT SPDDFYNLLV TSISNK
 
 
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