MURG_CLOP1
ID MURG_CLOP1 Reviewed; 357 AA.
AC Q0TNP7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 96.
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=CPF_2320;
OS Clostridium perfringens (strain ATCC 13124 / DSM 756 / JCM 1290 / NCIMB
OS 6125 / NCTC 8237 / Type A).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=195103;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / S 107 /
RC Type A;
RX PubMed=16825665; DOI=10.1101/gr.5238106;
RA Myers G.S.A., Rasko D.A., Cheung J.K., Ravel J., Seshadri R., DeBoy R.T.,
RA Ren Q., Varga J., Awad M.M., Brinkac L.M., Daugherty S.C., Haft D.H.,
RA Dodson R.J., Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A.,
RA Khouri H., Dimitrov G.I., Watkins K.L., Mulligan S., Benton J., Radune D.,
RA Fisher D.J., Atkins H.S., Hiscox T., Jost B.H., Billington S.J.,
RA Songer J.G., McClane B.A., Titball R.W., Rood J.I., Melville S.B.,
RA Paulsen I.T.;
RT "Skewed genomic variability in strains of the toxigenic bacterial pathogen,
RT Clostridium perfringens.";
RL Genome Res. 16:1031-1040(2006).
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=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: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; CP000246; ABG83915.2; -; Genomic_DNA.
DR RefSeq; WP_003451085.1; NC_008261.1.
DR AlphaFoldDB; Q0TNP7; -.
DR SMR; Q0TNP7; -.
DR STRING; 195103.CPF_2320; -.
DR CAZy; GT28; Glycosyltransferase Family 28.
DR PRIDE; Q0TNP7; -.
DR EnsemblBacteria; ABG83915; ABG83915; CPF_2320.
DR GeneID; 29570573; -.
DR KEGG; cpf:CPF_2320; -.
DR eggNOG; COG0707; Bacteria.
DR HOGENOM; CLU_037404_0_0_9; -.
DR OrthoDB; 1165736at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000001823; 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.
DR TIGRFAMs; TIGR01133; murG; 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..357
FT /note="UDP-N-acetylglucosamine--N-acetylmuramyl-
FT (pentapeptide) pyrophosphoryl-undecaprenol N-
FT acetylglucosamine transferase"
FT /id="PRO_0000315086"
FT BINDING 13..15
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00033"
FT BINDING 166
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00033"
FT BINDING 196
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00033"
FT BINDING 291
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00033"
SQ SEQUENCE 357 AA; 39786 MW; 98715339150B5ECA CRC64;
MKKYKIIMTG GGSAGHVTPN LALVPKLKEL GFEIKYIGSK NGIEKEIITK ENIPYYSISS
GKLRRYFDIK NFTDPFKVLK GVMDASRILS KEKPDVIFSK GGFVTVPVVI AASMKKIPVV
SHESDLTPGL ANKIASPFCD TLCVTFPESL KYIKDNKGEL TGTPIREDLL KGDKERGRKF
CNFKENKKVL MIIGGSLGSK VINESVRKIL NEILKEYNVI HLCGKGNLDE SLKNLDGYRQ
YEYISEELPD LMALADLVIS RAGANTIFEL LALRKLNILI PLSANASRGD QVLNANSFEK
SGYSMVIKEE ELNSELLLKS IKDLEKNREK YLNSMKMSKI GNGVNNIIDI IKKSAHM
