ID A0A0G0NES9_9BACT Unreviewed; 827 AA.
AC A0A0G0NES9;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=UT08_C0018G0020 {ECO:0000313|EMBL:KKQ84414.1};
OS Candidatus Woesebacteria bacterium GW2011_GWB1_38_8.
OC Bacteria; Candidatus Woesebacteria.
OX NCBI_TaxID=1618570 {ECO:0000313|EMBL:KKQ84414.1, ECO:0000313|Proteomes:UP000034081};
RN [1] {ECO:0000313|EMBL:KKQ84414.1, ECO:0000313|Proteomes:UP000034081}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-
CC Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-
CC (1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-
CC cis-undecaprenyl diphosphate = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-
CC D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans-octa-cis-undecaprenyl
CC diphosphate + di-trans,octa-cis-undecaprenyl diphosphate + H(+);
CC Xref=Rhea:RHEA:23708, Rhea:RHEA-COMP:9602, Rhea:RHEA-COMP:9603,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58405, ChEBI:CHEBI:60033,
CC ChEBI:CHEBI:78435; EC=2.4.1.129;
CC Evidence={ECO:0000256|ARBA:ARBA00023988};
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:KKQ84414.1}.
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DR EMBL; LBVL01000018; KKQ84414.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0NES9; -.
DR STRING; 1618570.UT08_C0018G0020; -.
DR PATRIC; fig|1618570.3.peg.1256; -.
DR Proteomes; UP000034081; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.10.3810.10; Biosynthetic peptidoglycan transglycosylase-like; 1.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR001264; Glyco_trans_51.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR036950; PBP_transglycosylase.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR NCBIfam; TIGR02074; PBP_1a_fam; 1.
DR PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF33; PEPTIDOGLYCAN GLYCOSYLTRANSFERASE; 1.
DR Pfam; PF00912; Transgly; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
PE 4: Predicted;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Transferase {ECO:0000313|EMBL:KKQ84414.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 96..119
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 147..320
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 409..725
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 827 AA; 92736 MW; 023FAB8A291E296D CRC64;
MLLILKRIIN NLLRESLVYF KKIKVKSEKL SWKAEVFLLT LEKLISKFFV ILKTKFTFFH
LLELLQIFLL AQKIKLLRLS YFLPKLRIRK FSILKFLTYI FTFSLIILGM AGAFFWFYVI
RDLPSPQNLI SRKMAVSTKI YDRNGGLLYN IYRNQNRTPV SLRNIPLEAR LATIAIEDAE
FYNHPGFSIK GIARASLKNL RQGELTGGST ITQQLVKNTL LSPEKTLVRK LKEIVLAVQV
ELTFSKDQIL EMYMNEVSYG GTAYGVQTAS LTYFGKDIKD LNLAEAALLA GLPKSPTYYS
PFGPNPEKAK ERQKEVLKLM KINGFITEKQ KKSAETHEIK FAQNQTSIKA PHYVFYVREL
LEQKYSKELV EAGGLEVTTS LDLQIQNLAE NIVKEEIEKL KSLNVTNAAV LVLNPKTGEV
LAMVGSKDYF SIAEDGNVNV TLRPRQPGSS IKVVNYANAL SNGLTPATIL NDAPFTFHVD
GQEPYTPKNY EGGYRGNISL RNALAESRNI PAVKTLALFG VESMIEMGQK MGITTWENPN
NYGLSLTLGG GEVKLLDLAT VYATLANYGK RPKLSALLKV TDTNQNVLEE FKCDSINEVD
LVKDPKDTDV VSAATESAFN NALNDVQDCQ GKQVLDPRIA FIITDILHDN NARSLSFGIN
SLLVIPNHKE VAVKTGTSND LRDNLAIGYT QDYVVAVWVG NNNNSPMARI SSGVTGATPI
WNKIMTALLA QQSNHDWPIP AGLIQVPICS FTGTLACQGC PAKMEWFLEE NKPKLACKQE
WFNQKAILTP PPQNQNVLLP TQGNDRRNQF LDPILNLRYG KEKKNRR
//
