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MURG_STRP2
ID   MURG_STRP2              Reviewed;         352 AA.
AC   Q04LK0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 93.
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=SPD_0599;
OS   Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=373153;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D39 / NCTC 7466;
RX   PubMed=17041037; DOI=10.1128/jb.01148-06;
RA   Lanie J.A., Ng W.-L., Kazmierczak K.M., Andrzejewski T.M., Davidsen T.M.,
RA   Wayne K.J., Tettelin H., Glass J.I., Winkler M.E.;
RT   "Genome sequence of Avery's virulent serotype 2 strain D39 of Streptococcus
RT   pneumoniae and comparison with that of unencapsulated laboratory strain
RT   R6.";
RL   J. Bacteriol. 189:38-51(2007).
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; CP000410; ABJ54267.1; -; Genomic_DNA.
DR   RefSeq; WP_000724838.1; NC_008533.2.
DR   AlphaFoldDB; Q04LK0; -.
DR   SMR; Q04LK0; -.
DR   STRING; 373153.SPD_0599; -.
DR   CAZy; GT28; Glycosyltransferase Family 28.
DR   EnsemblBacteria; ABJ54267; ABJ54267; SPD_0599.
DR   GeneID; 60233774; -.
DR   KEGG; spd:SPD_0599; -.
DR   eggNOG; COG0707; Bacteria.
DR   HOGENOM; CLU_037404_0_0_9; -.
DR   OMA; AGNEQAH; -.
DR   OrthoDB; 1165736at2; -.
DR   BioCyc; SPNE373153:G1G6V-664-MON; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000001452; 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; Transferase.
FT   CHAIN           1..352
FT                   /note="UDP-N-acetylglucosamine--N-acetylmuramyl-
FT                   (pentapeptide) pyrophosphoryl-undecaprenol N-
FT                   acetylglucosamine transferase"
FT                   /id="PRO_0000315176"
FT   BINDING         195
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00033"
FT   BINDING         287
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00033"
SQ   SEQUENCE   352 AA;  39448 MW;  A5D8AA3BDFBD6FF1 CRC64;
     MKKIVFTGGG TVGHVTLNLL LMPKFIEDGW EVHYIGDKRG IEHQEILKSG LDVTFHSIAT
     GKLRRYFSWQ NMLDVFKVGW GIVQSLFIML RLRPQTLFSK GGFVSVPPVI AARVSGVPVF
     IHESDLSMGL ANKIAYKFAT KMYSTFEQAS SLSKVEHVGA VTKVSDQKNP EPDELVDIQT
     HFNHKLPTVL FVGGSAGARV FNQLVTDHKK ELTERYNIIN LTGDSSLNEL SQNLFRVDYV
     TDLYQPLMEL ADIVVTRGGA NTIFELLAIA KLHVIVPLGR EASRGDQIEN AAYFVKKGYA
     EDLQESDLTL DSLEEKLSHL LSHKEDYQAK MKASKELKSL ADFYQLLKKD LS
 
 
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