ID A0A396S9W0_9BACI Unreviewed; 358 AA.
AC A0A396S9W0;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase {ECO:0000256|HAMAP-Rule:MF_00033};
DE EC=2.4.1.227 {ECO:0000256|HAMAP-Rule:MF_00033};
DE AltName: Full=Undecaprenyl-PP-MurNAc-pentapeptide-UDPGlcNAc GlcNAc transferase {ECO:0000256|HAMAP-Rule:MF_00033};
GN Name=murG {ECO:0000256|HAMAP-Rule:MF_00033};
GN ORFNames=D1B33_08555 {ECO:0000313|EMBL:RHW37571.1};
OS Lysinibacillus yapensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX NCBI_TaxID=2304605 {ECO:0000313|EMBL:RHW37571.1, ECO:0000313|Proteomes:UP000265692};
RN [1] {ECO:0000313|EMBL:RHW37571.1, ECO:0000313|Proteomes:UP000265692}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YLB-03 {ECO:0000313|EMBL:RHW37571.1,
RC ECO:0000313|Proteomes:UP000265692};
RA Yu L.;
RT "Lysinibacillus sp. YLB-03 draft genome sequence.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|HAMAP-Rule:MF_00033};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_00033}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00033};
CC Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_00033};
CC Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_00033}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 28 family. MurG
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_00033}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00033}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RHW37571.1}.
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DR EMBL; QWEI01000003; RHW37571.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A396S9W0; -.
DR OrthoDB; 9808936at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000265692; Unassembled WGS sequence.
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 CDD; cd03785; GT28_MurG; 1.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
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 NCBIfam; TIGR01133; murG; 1.
DR PANTHER; PTHR21015:SF27; UDP-N-ACETYLGLUCOSAMINE--N-ACETYLMURAMYL-(PENTAPEPTIDE) PYROPHOSPHORYL-UNDECAPRENOL N-ACETYLGLUCOSAMINE TRANSFERASE; 1.
DR PANTHER; PTHR21015; UDP-N-ACETYLGLUCOSAMINE--N-ACETYLMURAMYL-(PENTAPEPTIDE) PYROPHOSPHORYL-UNDECAPRENOL N-ACETYLGLUCOSAMINE TRANSFERASE 1; 1.
DR Pfam; PF04101; Glyco_tran_28_C; 1.
DR Pfam; PF03033; Glyco_transf_28; 1.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|HAMAP-
KW Rule:MF_00033};
KW Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000256|HAMAP-
KW Rule:MF_00033};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_00033};
KW Cell shape {ECO:0000256|ARBA:ARBA00022960, ECO:0000256|HAMAP-
KW Rule:MF_00033};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316,
KW ECO:0000256|HAMAP-Rule:MF_00033};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, ECO:0000256|HAMAP-
KW Rule:MF_00033};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00033};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984, ECO:0000256|HAMAP-
KW Rule:MF_00033}; Reference proteome {ECO:0000313|Proteomes:UP000265692};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00033}.
FT DOMAIN 6..145
FT /note="Glycosyltransferase family 28 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03033"
FT DOMAIN 191..341
FT /note="Glycosyl transferase family 28 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF04101"
FT BINDING 13..15
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00033"
FT BINDING 168
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00033"
FT BINDING 198
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00033"
FT BINDING 293
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00033"
SQ SEQUENCE 358 AA; 39440 MW; B0205DE882D72A84 CRC64;
MKHKSIILTG GGTAGHVSLN QAIIPSLRKE GYDVHYIGSY DGIEKELITQ SFPDVPYHHI
SSGKLRRYFS MKNFSDPFKV LAGVGQAYAV IRKVKPTMIF SKGGFVSVPV VIAAKLAKIP
VVIHESDVTP GLANKIALPF ASHIFTIFQD TLNYLPSEKA TCTGSIVREE LFSGNALKGK
KRCGFTDHKK VLLVMGGSLG SVVLNDSLRS NLPDLLKTYN VIHLCGKGNS DSSLDSLKGY
KQFEYVTNEL PDLLHAADFV VSRAGSNSIF EFLALKKPML LVPLSAAKSR GDQILNAKLF
EKQGFAHVLE EEMLSKSTFM KAIETLTKRS PEYLDAMEKA ERPKTPAEMV KLLLQYEK
//
