ID E4UB29_LIBSC Unreviewed; 383 AA.
AC E4UB29;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 08-NOV-2023, entry version 71.
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 OrderedLocusNames=CKC_03355 {ECO:0000313|EMBL:ADR52420.1};
OS Liberibacter solanacearum (strain CLso-ZC1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Liberibacter.
OX NCBI_TaxID=658172 {ECO:0000313|EMBL:ADR52420.1, ECO:0000313|Proteomes:UP000007038};
RN [1] {ECO:0000313|Proteomes:UP000007038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLso-ZC1 {ECO:0000313|Proteomes:UP000007038};
RA Lin H., Doddapaneni H.V., Lou B., Civerolo E.L., Chen C., Duan Y., Zhou L.,
RA Glynn J.;
RT "Complete genome sequence of Candidatus Liberibacter solanacearum CLso-
RT ZC1.";
RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CLso-ZC1;
RA Lin H., Doddapaneni H.V., Lou B., Civerolo E.L., Chen C., Duan Y., Zhou L.,
RA Glynn J.;
RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ADR52420.1, ECO:0000313|Proteomes:UP000007038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLso-ZC1 {ECO:0000313|EMBL:ADR52420.1,
RC ECO:0000313|Proteomes:UP000007038};
RX PubMed=21552483; DOI=10.1371/journal.pone.0019135;
RA Lin H., Lou B., Glynn J.M., Doddapaneni H., Civerolo E.L., Chen C.,
RA Duan Y., Zhou L., Vahling C.M.;
RT "The Complete Genome Sequence of 'Candidatus Liberibacter solanacearum',
RT the Bacterium Associated with Potato Zebra Chip Disease.";
RL PLoS ONE 6:E19135-E19135(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: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 inner membrane {ECO:0000256|HAMAP-
CC Rule:MF_00033}; Peripheral membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_00033}; 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}.
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DR EMBL; CP002371; ADR52420.1; -; Genomic_DNA.
DR RefSeq; WP_013462076.1; NC_014774.1.
DR AlphaFoldDB; E4UB29; -.
DR STRING; 658172.CKC_03355; -.
DR CAZy; GT28; Glycosyltransferase Family 28.
DR KEGG; lso:CKC_03355; -.
DR eggNOG; COG0707; Bacteria.
DR HOGENOM; CLU_037404_2_1_5; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000007038; 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 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}; Cell inner membrane {ECO:0000256|HAMAP-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}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 77..96
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 103..122
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 14..147
FT /note="Glycosyltransferase family 28 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03033"
FT DOMAIN 195..357
FT /note="Glycosyl transferase family 28 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF04101"
FT BINDING 21..23
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00033"
FT BINDING 132
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00033"
FT BINDING 173
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00033"
FT BINDING 201
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00033"
FT BINDING 276..281
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00033"
FT BINDING 302
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00033"
SQ SEQUENCE 383 AA; 42582 MW; 597CEE5A9A6AC268 CRC64;
MTKYDYNLAK KNAILLVAGG TGGHVFPAVA LSHELKKRGY PVYLAIDHRA QCFVEDFSPE
EIYVVPSSQI RLSNPVVIFR SLMALWKGFI VSLRLIRKLK PKVIVGFGGY HTLSPMLAGI
ILQIPSMIHE QNAVMGRANR LLSWGVKVIA GGLLSSKKGL LSHKIIITGN PVRNAFIKMA
NIPYQASYSN QPFRLLIFGG SQGAKVFSDI IPKSIALIPK EQRQRLIITQ QVKEDEKEIV
QKIYDDLGLK AHISSFFKDI EKYIFEANLL ICRSGALTVS EIAVIGRPVI LIPYPHSINQ
DQLHNAWFLQ EGGGAKVITQ NFLSPERLAN EISSAMKNPE SLVQMAKQVS MKGKYKAVLL
LSDLVEQLAR KESVSSLGRK YTC
//
