ID B3SF78_TRIAD Unreviewed; 352 AA.
AC B3SF78;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=Undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase {ECO:0008006|Google:ProtNLM};
GN ORFNames=TRIADDRAFT_62887 {ECO:0000313|EMBL:EDV18616.1};
OS Trichoplax adhaerens (Trichoplax reptans).
OC Eukaryota; Metazoa; Placozoa; Uniplacotomia; Trichoplacea; Trichoplacidae;
OC Trichoplax.
OX NCBI_TaxID=10228 {ECO:0000313|EMBL:EDV18616.1, ECO:0000313|Proteomes:UP000009022};
RN [1] {ECO:0000313|EMBL:EDV18616.1, ECO:0000313|Proteomes:UP000009022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Grell-BS-1999 {ECO:0000313|EMBL:EDV18616.1,
RC ECO:0000313|Proteomes:UP000009022};
RX PubMed=18719581; DOI=10.1038/nature07191;
RA Srivastava M., Begovic E., Chapman J., Putnam N.H., Hellsten U.,
RA Kawashima T., Kuo A., Mitros T., Salamov A., Carpenter M.L.,
RA Signorovitch A.Y., Moreno M.A., Kamm K., Grimwood J., Schmutz J.,
RA Shapiro H., Grigoriev I.V., Buss L.W., Schierwater B., Dellaporta S.L.,
RA Rokhsar D.S.;
RT "The Trichoplax genome and the nature of placozoans.";
RL Nature 454:955-960(2008).
CC -!- SIMILARITY: Belongs to the glycosyltransferase 28 family.
CC {ECO:0000256|ARBA:ARBA00006962}.
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DR EMBL; DS985980; EDV18616.1; -; Genomic_DNA.
DR RefSeq; XP_002118897.1; XM_002118861.1.
DR AlphaFoldDB; B3SF78; -.
DR STRING; 10228.B3SF78; -.
DR EnsemblMetazoa; TriadT62887; TriadP62887; TriadG62887.
DR GeneID; 6760112; -.
DR KEGG; tad:TRIADDRAFT_62887; -.
DR CTD; 6760112; -.
DR eggNOG; ENOG502QT0H; Eukaryota.
DR HOGENOM; CLU_037404_2_1_1; -.
DR InParanoid; B3SF78; -.
DR OMA; AADMMLC; -.
DR OrthoDB; 1275902at2759; -.
DR Proteomes; UP000009022; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0016757; F:glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0050511; F:undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase activity; IEA:InterPro.
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:InterPro.
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 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};
KW Cell division {ECO:0000256|ARBA:ARBA00022618};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW Reference proteome {ECO:0000313|Proteomes:UP000009022};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..131
FT /note="Glycosyltransferase family 28 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03033"
FT DOMAIN 176..327
FT /note="Glycosyl transferase family 28 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF04101"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EDV18616.1"
SQ SEQUENCE 352 AA; 40237 MW; BF88D78CF2B33B1C CRC64;
GTGGHVFPAQ AIADKLVSKN YSLHLVTDKR ALKYLDGAFL DMRKTVILAS GANEKFSSKL
LNFTLLIISS LKIMGKFFLQ KPKMVISFGG YPTLPASLYA IIFRVPLILH EQNSVLGQIN
RLFLPFAKKL FISFPNTKNI KEKYKNKIIL TGLPIRNKFI EAMNNKKIKR NRYLKILVVG
GSQGARIFSD VIPKSIQNLG KSLQERIYIT QQAREENIDE VISEYSKIKC KYNIKTFFDN
LEELYDRHDL VICRGGASSI AELMVFKKVA ILVPFAKAKD NHQLYNAKFL SENSKIILKT
EDEFCSKWLS LFIADLLNNP DKIQDIQKSY NNKYNDLHLN SVNKFVKELD NI
//
