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MURG_RICCN
ID   MURG_RICCN              Reviewed;         376 AA.
AC   Q92I58;
DT   31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 125.
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=RC0562;
OS   Rickettsia conorii (strain ATCC VR-613 / Malish 7).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=272944;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-613 / Malish 7;
RX   PubMed=11557893; DOI=10.1126/science.1061471;
RA   Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V.,
RA   Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.;
RT   "Mechanisms of evolution in Rickettsia conorii and R. prowazekii.";
RL   Science 293:2093-2098(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}.
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DR   EMBL; AE006914; AAL03100.1; -; Genomic_DNA.
DR   PIR; B97770; B97770.
DR   RefSeq; WP_010977197.1; NC_003103.1.
DR   AlphaFoldDB; Q92I58; -.
DR   SMR; Q92I58; -.
DR   CAZy; GT28; Glycosyltransferase Family 28.
DR   EnsemblBacteria; AAL03100; AAL03100; RC0562.
DR   KEGG; rco:RC0562; -.
DR   PATRIC; fig|272944.4.peg.641; -.
DR   HOGENOM; CLU_037404_2_1_5; -.
DR   OMA; AADMMLC; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000000816; 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   InterPro; IPR022439; RPE4.
DR   Pfam; PF04101; Glyco_tran_28_C; 1.
DR   Pfam; PF03033; Glyco_transf_28; 1.
DR   TIGRFAMs; TIGR01133; murG; 1.
DR   TIGRFAMs; TIGR03777; RPE4; 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; Transferase.
FT   CHAIN           1..376
FT                   /note="UDP-N-acetylglucosamine--N-acetylmuramyl-
FT                   (pentapeptide) pyrophosphoryl-undecaprenol N-
FT                   acetylglucosamine transferase"
FT                   /id="PRO_0000109203"
FT   BINDING         11..13
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00033"
FT   BINDING         117
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00033"
FT   BINDING         160
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00033"
FT   BINDING         208
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00033"
FT   BINDING         310
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00033"
SQ   SEQUENCE   376 AA;  42036 MW;  F98A39FB795E674C CRC64;
     MKKIILVAGG TGGHFFPAVA LGEELIKRGY EVHFITDLRC KQYIKQDMKV IFHILDLKRS
     GNIFLFLPRL SIAVLKAIKL LYNMKPSVTV GFGGYPVIAP MFAAIFLRVP IIIHEQNSYL
     GKVNKFFASF AKKIAISYAK IKNLPEFAKS KIVVTGGVVR ENIRELKVIE MSSRGLTTGS
     KKSLIKALDS VVKPRNDKLF TIFIFGGSQG AKLFSELIPA SIQILMQKQP SLELNIIQQA
     ALDDQVKIKD IYSKLNITYA FAEFFDNMAL QYKEADLVIS RAGASTIEEL TYIGLPAIFI
     PLPSAADNHQ YYNAQLLEDE KTGWCLEQNN ISAGKLADKI LELISNPKIL EDASQNLLKR
     RKEGHKLLSN LIEEVI
 
 
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