UniProt: E3GE13

Database: UniProt
Entry: E3GE13_9FIRM

LinkDB:  E3GE13_9FIRM 
Original site:  E3GE13_9FIRM

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Ontology (11)   
   GO (10)   
   CAZY (1)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (3)   
   EMBL (3)   
Protein domain (5)   
   InterPro (3)   
   Pfam (2)   
Literature (1)   
   PubMed (1)   
All databases (24)   

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ID   E3GE13_9FIRM            Unreviewed;       368 AA.
AC   E3GE13; A0A1M7H205;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   24-JAN-2024, entry version 72.
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:NZA39212.1};
GN   OrderedLocusNames=ELI_2526 {ECO:0000313|EMBL:ADO37508.1};
GN   ORFNames=H0N91_14020 {ECO:0000313|EMBL:NZA39212.1},
GN   SAMN04487888_104378 {ECO:0000313|EMBL:SFO74713.1};
OS   Eubacterium callanderi.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC   Eubacterium.
OX   NCBI_TaxID=53442 {ECO:0000313|EMBL:ADO37508.1, ECO:0000313|Proteomes:UP000006873};
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=KIST612;
RA   Roh H., Ko H.-J., Kim D., Choi D.G., Park S., Kim S., Kim K.H., Chang I.S.,
RA   Choi I.-G.;
RL   Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADO37508.1, ECO:0000313|Proteomes:UP000006873}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KIST612 {ECO:0000313|EMBL:ADO37508.1,
RC   ECO:0000313|Proteomes:UP000006873};
RX   PubMed=21036996; DOI=10.1128/JB.01217-10;
RA   Roh H., Ko H.J., Kim D., Choi D.G., Park S., Kim S., Chang I.S., Choi I.G.;
RT   "Complete genome sequence of a carbon monoxide-utilizing acetogen,
RT   Eubacterium limosum KIST612.";
RL   J. Bacteriol. 193:307-308(2011).
RN   [3] {ECO:0000313|EMBL:SFO74713.1, ECO:0000313|Proteomes:UP000199443}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NLAE-zl-G225 {ECO:0000313|EMBL:SFO74713.1,
RC   ECO:0000313|Proteomes:UP000199443};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:NZA39212.1, ECO:0000313|Proteomes:UP000586254}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AMC0717 {ECO:0000313|EMBL:NZA39212.1,
RC   ECO:0000313|Proteomes:UP000586254};
RA   Marsh A.J., Azcarate-Peril M.A.;
RT   "Organ Donor 1.";
RL   Submitted (JUL-2020) 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}.
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DR   EMBL; CP002273; ADO37508.1; -; Genomic_DNA.
DR   EMBL; JACCKS010000017; NZA39212.1; -; Genomic_DNA.
DR   EMBL; FOWI01000004; SFO74713.1; -; Genomic_DNA.
DR   RefSeq; WP_013380829.1; NZ_QYRZ01000034.1.
DR   AlphaFoldDB; E3GE13; -.
DR   CAZy; GT28; Glycosyltransferase Family 28.
DR   GeneID; 68363595; -.
DR   KEGG; elm:ELI_2526; -.
DR   eggNOG; COG0707; Bacteria.
DR   HOGENOM; CLU_037404_0_1_9; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000006873; Chromosome.
DR   Proteomes; UP000199443; Unassembled WGS sequence.
DR   Proteomes; UP000586254; 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: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          3..143
FT                   /note="Glycosyltransferase family 28 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03033"
FT   DOMAIN          189..353
FT                   /note="Glycosyl transferase family 28 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF04101"
FT   BINDING         10..12
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00033"
FT   BINDING         124
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00033"
FT   BINDING         165
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00033"
FT   BINDING         195
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00033"
FT   BINDING         300
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00033"
SQ   SEQUENCE   368 AA;  39846 MW;  B73559ABCA0AC2C7 CRC64;
     MKILVAAGGT GGHIYPGLAI ADKLKERLPG AEILFIGSQV GMEKNIVPKE GYPIEYIRVR
     GFERELSLET LAAVKGIFDG ISDSKKVLKR HQPDLVVGTG GFTCGPLLLE AAKRGIPTMI
     HEQNAYPGKT NRMLGKRVDR VAISFKEAAE YFPEDKTFLA GNPVRDVFKQ TDRNALRDKL
     GLKENQRLVV IMGGSQGAGS INNAAASFIA RNADNPEMVV YHLTGRGQYD KVLEKLKENG
     VKLDDCRNIN VLAYSNDVHT LIGAGDLVVS RSGAMSVAEI AAVGIPSILV PYPMAAGNHQ
     EFNARVITDN GGGILIHDAE LTPDLLAETI PALLRDEKGL EKMRRATKER AILDAGDRIC
     AEALKLIK
//

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