ID E9L1F7_9ZZZZ Unreviewed; 369 AA.
AC E9L1F7;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 13-SEP-2023, entry version 30.
DE RecName: Full=Undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase {ECO:0008006|Google:ProtNLM};
GN ORFNames=CA37-13 {ECO:0000313|EMBL:ADU56036.1};
OS uncultured organism CA37.
OC unclassified sequences; environmental samples.
OX NCBI_TaxID=941420 {ECO:0000313|EMBL:ADU56036.1};
RN [1] {ECO:0000313|EMBL:ADU56036.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=20945895; DOI=10.1021/ja105825a;
RA Banik J.J., Craig J.W., Calle P.Y., Brady S.F.;
RT "Tailoring enzyme-rich environmental DNA clones: a source of enzymes for
RT generating libraries of unnatural natural products.";
RL J. Am. Chem. Soc. 132:15661-15670(2010).
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DR EMBL; HM486074; ADU56036.1; -; Genomic_DNA.
DR AlphaFoldDB; E9L1F7; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
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 Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 6..145
FT /note="Glycosyltransferase family 28 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03033"
FT DOMAIN 191..349
FT /note="Glycosyl transferase family 28 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF04101"
SQ SEQUENCE 369 AA; 38290 MW; BEF8D6FF706978CF CRC64;
MTGPRVVVAG GHSAGHIEPT MNFADALRRL EPAAEITALG TVRGLDTTLI PARGYPLELI
PPVPLPRKLS LALMQTPGRL RDSVLAAEAV LDRVRAEVVV GFGGYVAAPA YLAARRRGLP
IVVHEANARP GVANQLAARM TTHVFTAAPG VRLAHATAIG IPLRPAITGL DRPALRDAAR
QRFGLRPDGP VLMVTGGSQG AEAINAAVSG AAPALRAAGV QVLHIAGPQR VVEVPDGDPA
DPPYVVMPYV DEMQYAYAAA DFVICRSGAM TCAELAAVGL PAAYVPLPLR GAEQRLNAEP
VVAAGGALLV DNARLDPAWI ETTLIPVLTD PERIAAMSAH AAAAGAPDAD VVLARHVLTT
VAERRRCAS
//
