ID A0A090IIW5_9GAMM Unreviewed; 354 AA.
AC A0A090IIW5;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 44.
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 ECO:0000313|EMBL:CED70491.1};
GN ORFNames=AWOD_I_0397 {ECO:0000313|EMBL:CED70491.1};
OS Aliivibrio wodanis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Aliivibrio.
OX NCBI_TaxID=80852 {ECO:0000313|EMBL:CED70491.1, ECO:0000313|Proteomes:UP000032427};
RN [1] {ECO:0000313|Proteomes:UP000032427}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=06/09/139 {ECO:0000313|Proteomes:UP000032427};
RA Hjerde E.;
RL Submitted (SEP-2014) 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}.
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DR EMBL; LN554846; CED70491.1; -; Genomic_DNA.
DR RefSeq; WP_045101193.1; NZ_LN554846.1.
DR AlphaFoldDB; A0A090IIW5; -.
DR STRING; 80852.AWOD_I_0397; -.
DR GeneID; 28539930; -.
DR KEGG; awd:AWOD_I_0397; -.
DR PATRIC; fig|80852.17.peg.404; -.
DR HOGENOM; CLU_037404_2_0_6; -.
DR OrthoDB; 9808936at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000032427; Chromosome 1 complete 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:SF22; GLYCOSYLTRANSFERASE; 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};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00033}.
FT DOMAIN 9..145
FT /note="Glycosyltransferase family 28 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03033"
FT DOMAIN 185..342
FT /note="Glycosyl transferase family 28 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF04101"
FT BINDING 15..17
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00033"
FT BINDING 127
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00033"
FT BINDING 163
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00033"
FT BINDING 191
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00033"
FT BINDING 244
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00033"
FT BINDING 263..268
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00033"
FT BINDING 288
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00033"
SQ SEQUENCE 354 AA; 38167 MW; 8160BF06D1036BC7 CRC64;
MKNKNKRLLV MAGGTGGHVF PGLAVAKQLQ SEGWDIRWLG TEDRMEADLV PKHGIEIDFI
KVKGLRGQGF KKLLAAPFQI LGAISQAKKH IQAWQPDVVL GMGGYVSGPG GIAAWLSGIP
VVLHEQNAVA GLTNQWLSKI AKRVFQAFPG AFPNADVVGN PVREDVCQLP HPSERFAERS
GPIRVLIMGG SQGARILNTT LPEALPKLNH SVEIWHQAGK GNQETVHQAY CDNGITDANV
TEFIDDVAAA YAWADLLVCR SGALTVSEVS AAGVGSVFIP FMHKDRQQAL NADHLVQCDA
AKMIEQQDLT VQGLVDVLNG LERKELLEMA SNARKSAITD ADVRVANAIK DLAK
//
