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MURG_MYCBT
ID   MURG_MYCBT              Reviewed;         410 AA.
AC   C1AQ69;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 71.
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=JTY_2164;
OS   Mycobacterium bovis (strain BCG / Tokyo 172 / ATCC 35737 / TMC 1019).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=561275;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BCG / Tokyo 172 / ATCC 35737 / TMC 1019;
RX   PubMed=19200449; DOI=10.1016/j.vaccine.2009.01.034;
RA   Seki M., Honda I., Fujita I., Yano I., Yamamoto S., Koyama A.;
RT   "Whole genome sequence analysis of Mycobacterium bovis bacillus Calmette-
RT   Guerin (BCG) Tokyo 172: a comparative study of BCG vaccine substrains.";
RL   Vaccine 27:1710-1716(2009).
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; AP010918; BAH26448.1; -; Genomic_DNA.
DR   RefSeq; WP_010950665.1; NZ_CP014566.1.
DR   AlphaFoldDB; C1AQ69; -.
DR   SMR; C1AQ69; -.
DR   CAZy; GT28; Glycosyltransferase Family 28.
DR   KEGG; mbt:JTY_2164; -.
DR   HOGENOM; CLU_037404_1_0_11; -.
DR   OMA; AADMMLC; -.
DR   UniPathway; UPA00219; -.
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..410
FT                   /note="UDP-N-acetylglucosamine--N-acetylmuramyl-
FT                   (pentapeptide) pyrophosphoryl-undecaprenol N-
FT                   acetylglucosamine transferase"
FT                   /id="PRO_1000192137"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         45..47
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00033"
FT   BINDING         167
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00033"
FT   BINDING         204
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00033"
FT   BINDING         238
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00033"
FT   BINDING         334
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00033"
SQ   SEQUENCE   410 AA;  41858 MW;  347DB45D34A4890B CRC64;
     MKDTVSQPAG GRGATAPRPA DAASPSCGSS PSADSLSVVL AGGGTAGHVE PAMAVADALV
     ALDPRVRITA LGTPRGLETR LVPQRGYHLE LITAVPMPRK PGGDLARLPS RVWRAVREAR
     DVLDDVDADV VVGFGGYVAL PAYLAARGLP LPPRRRRRIP VVIHEANARA GLANRVGAHT
     ADRVLSAVPD SGLRRAEVVG VPVRASIAAL DRAVLRAEAR AHFGFPDDAR VLLVFGGSQG
     AVSLNRAVSG AAADLAAAGV CVLHAHGPQN VLELRRRAQG DPPYVAVPYL DRMELAYAAA
     DLVICRAGAM TVAEVSAVGL PAIYVPLPIG NGEQRLNALP VVNAGGGMVV ADAALTPELV
     ARQVAGLLTD PARLAAMTAA AARVGHRDAA GQVARAALAV ATGAGARTTT
 
 
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