MURG_BRUSU
ID MURG_BRUSU Reviewed; 379 AA.
AC Q8CY39; G0KBJ1;
DT 07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 112.
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};
GN OrderedLocusNames=BR1431, BS1330_I1425;
OS Brucella suis biovar 1 (strain 1330).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=204722;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1330;
RX PubMed=12271122; DOI=10.1073/pnas.192319099;
RA Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F.,
RA Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J.,
RA Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA Nelson W.C., Ayodeji B., Kraul M., Shetty J., Malek J.A., Van Aken S.E.,
RA Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L.,
RA Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M.;
RT "The Brucella suis genome reveals fundamental similarities between animal
RT and plant pathogens and symbionts.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1330;
RX PubMed=22038969; DOI=10.1128/jb.06181-11;
RA Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R.;
RT "Revised genome sequence of Brucella suis 1330.";
RL J. Bacteriol. 193:6410-6410(2011).
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; AE014291; AAN30344.1; -; Genomic_DNA.
DR EMBL; CP002997; AEM18760.1; -; Genomic_DNA.
DR RefSeq; WP_006190601.1; NZ_KN046804.1.
DR AlphaFoldDB; Q8CY39; -.
DR SMR; Q8CY39; -.
DR CAZy; GT28; Glycosyltransferase Family 28.
DR EnsemblBacteria; AEM18760; AEM18760; BS1330_I1425.
DR GeneID; 45052442; -.
DR KEGG; bms:BR1431; -.
DR KEGG; bsi:BS1330_I1425; -.
DR PATRIC; fig|204722.21.peg.918; -.
DR HOGENOM; CLU_037404_2_1_5; -.
DR OMA; AADMMLC; -.
DR PhylomeDB; Q8CY39; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000007104; Chromosome I.
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; Transferase.
FT CHAIN 1..379
FT /note="UDP-N-acetylglucosamine--N-acetylmuramyl-
FT (pentapeptide) pyrophosphoryl-undecaprenol N-
FT acetylglucosamine transferase"
FT /id="PRO_0000109152"
FT BINDING 17..19
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00033"
FT BINDING 128
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00033"
FT BINDING 169
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00033"
FT BINDING 197
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00033"
FT BINDING 298
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00033"
SQ SEQUENCE 379 AA; 40236 MW; 705EE98D96F30177 CRC64;
MDNLANQGVI VLAAGGTGGH LFPAEALAHE LRARGWDVHL ATDARAQRFV GAFAQDHVHV
IRSATIAGRN PVALLKTFWS LWQGNLDSRK LFRRLKPKLV VGFGGYPTLP PLYAASNMGI
PTLIHEQNAV MGRANKGLAG RVKAIAGGFL PENSGAYAAK TVITGNPVRP PVLVAAATPY
TPAGKDDRFR LLVFGGSQGA QFFSQAIPAA VALLPEHERA RLLITQQARK EDEASARQAY
EKLGVPADVA PFFNDMPARM ADAHFVIARS GASTVSEITV IGRPAMLVPF PHALDHDQAA
NAAALAAAGG AEVVRQADLS PQRLAEMLQS AMNEPERLEQ QAKAAKSVGK PDAARLLADL
AEAIVSGKTV QEFKEGNRP
