ID A0A1B8J750_9HELI Unreviewed; 431 AA.
AC A0A1B8J750;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=BA723_01505 {ECO:0000313|EMBL:OBV28778.1}, BKN38_00105
GN {ECO:0000313|EMBL:OHU85848.1};
OS Helicobacter sp. CLO-3.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=211 {ECO:0000313|EMBL:OBV28778.1, ECO:0000313|Proteomes:UP000092701};
RN [1] {ECO:0000313|EMBL:OBV28778.1, ECO:0000313|Proteomes:UP000092701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMC1 {ECO:0000313|EMBL:OBV28778.1,
RC ECO:0000313|Proteomes:UP000092701};
RA Greninger A.L., Bateman A., Jerome K., Fang F.;
RT "Genome sequence of Helicobacter sp. CLO-3.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:OHU85848.1, ECO:0000313|Proteomes:UP000179541}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLO-3 {ECO:0000313|EMBL:OHU85848.1,
RC ECO:0000313|Proteomes:UP000179541};
RA Greninger A.L., Bateman A.C., Fang F., Jerome K.;
RT "Genome sequence of Helicobacter sp. CLO-3 Fennel-37 strain.";
RL Submitted (OCT-2016) 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:OBV28778.1}.
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DR EMBL; MAMQ01000094; OBV28778.1; -; Genomic_DNA.
DR EMBL; MLQN01000001; OHU85848.1; -; Genomic_DNA.
DR RefSeq; WP_066457260.1; NZ_MLQN01000001.1.
DR AlphaFoldDB; A0A1B8J750; -.
DR STRING; 211.BKN38_00105; -.
DR OrthoDB; 9808936at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000092701; Unassembled WGS sequence.
DR Proteomes; UP000179541; 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; 3.
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 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; 2.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 2.
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:UP000092701};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00033}.
FT DOMAIN 2..48
FT /note="Glycosyltransferase family 28 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03033"
FT DOMAIN 105..192
FT /note="Glycosyltransferase family 28 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03033"
FT DOMAIN 221..373
FT /note="Glycosyl transferase family 28 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF04101"
FT REGION 66..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 9..11
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00033"
FT BINDING 174
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00033"
FT BINDING 227
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00033"
FT BINDING 327
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00033"
SQ SEQUENCE 431 AA; 45818 MW; 753BAC8FDC25708A CRC64;
MIVITGGGTG GHLSIAQSLG EELRKRGKKA VYIGSLSGQD RAWFGDAGAD SRAEFSLDSV
DSDAGVKSGA ESSAQNSTNA GSTNAESTNA DSADTNSTAL FEACYFLPTS GVVNKRGLSK
LASIFAQLSA LQKVREIFKR HKVRAVISVG GFSAGPASIG AIVFRKPLFI HEQNATMGRL
NELLAPFAKR VFSAFKEPFT PYPIKQEALQ KRRIRNKLES IIFIGGSQGA KAINDVALAL
APTLLSRGIS ITHQCGARDL ARVREAYQKL GLLDKITLFD FSKELISYLV RADVCVARAG
ASSVWENAAL AIPTLYIPYP HAAKNHQASN AQFFVSRGAG AMILERDLQS SLQGDLQKDL
SADSGALESS KMDSADSAKL DSTKNPVLDF IDSCTPSMLE STSQALASMI NINGASVIID
EVLSYLGASQ N
//