MURG_NOSS1
ID MURG_NOSS1 Reviewed; 357 AA.
AC Q8YZI3;
DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2002, sequence version 2.
DT 03-AUG-2022, entry version 120.
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=alr0477;
OS Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=103690;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT "Complete genomic sequence of the filamentous nitrogen-fixing
RT cyanobacterium Anabaena sp. strain PCC 7120.";
RL DNA Res. 8:205-213(2001).
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 inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00033}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_00033}; 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB72435.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BA000019; BAB72435.1; ALT_INIT; Genomic_DNA.
DR PIR; AD1866; AD1866.
DR RefSeq; WP_044520653.1; NZ_RSCN01000024.1.
DR AlphaFoldDB; Q8YZI3; -.
DR SMR; Q8YZI3; -.
DR STRING; 103690.17129822; -.
DR CAZy; GT28; Glycosyltransferase Family 28.
DR EnsemblBacteria; BAB72435; BAB72435; BAB72435.
DR KEGG; ana:alr0477; -.
DR eggNOG; COG0707; Bacteria.
DR OMA; AADMMLC; -.
DR OrthoDB; 1165736at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000002483; 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 inner membrane; Cell membrane; Cell shape;
KW Cell wall biogenesis/degradation; Glycosyltransferase; Membrane;
KW Peptidoglycan synthesis; Reference proteome; Transferase.
FT CHAIN 1..357
FT /note="UDP-N-acetylglucosamine--N-acetylmuramyl-
FT (pentapeptide) pyrophosphoryl-undecaprenol N-
FT acetylglucosamine transferase"
FT /id="PRO_0000109136"
FT BINDING 15..17
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00033"
FT BINDING 124
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00033"
FT BINDING 165
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00033"
FT BINDING 194
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00033"
FT BINDING 288
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; 37961 MW; B95CA8BFA5044C44 CRC64;
MVNAPIKLLI AASGTGGHLF PAIALAEKLP DYEIEWLGVP NRLETQLVPK QYPLNTIAVE
GFQQGLGISS LVILGKLIGS ILKVRRLLKQ GNFQGVVTTG GYIAGPAVIA ARSLGLPVIF
HESNALPGKV TRFFGPWCSV VALGFDVATK YLPRATSVCV GTPVRSQFLN LGNNSQLDLA
IPGDVPVIVV FGGSQGAVAV NQLVRQAAPA WFEAGAYVVH LTGDRDPDVD SLKHPQYIEL
PFYDNMAALL QRANLAISRS GAGSLTELTV CGTPAILIPY PFAAEDHQSY NAEVFTKAGA
ALTFKQSDLT AELLQTQVLN LLQSPTELAK MGENAKAIAV PDSADKLATL VREVVER
