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Database: UniProt
Entry: A0A0G1VNR0_9BACT
LinkDB: A0A0G1VNR0_9BACT
Original site: A0A0G1VNR0_9BACT 
ID   A0A0G1VNR0_9BACT        Unreviewed;       607 AA.
AC   A0A0G1VNR0;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE            EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN   ORFNames=UY39_C0004G0004 {ECO:0000313|EMBL:KKW07940.1};
OS   Candidatus Kaiserbacteria bacterium GW2011_GWC2_49_12.
OC   Bacteria; Candidatus Kaiserbacteria.
OX   NCBI_TaxID=1618675 {ECO:0000313|EMBL:KKW07940.1, ECO:0000313|Proteomes:UP000034589};
RN   [1] {ECO:0000313|EMBL:KKW07940.1, ECO:0000313|Proteomes:UP000034589}
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:KKW07940.1}.
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DR   EMBL; LCPV01000004; KKW07940.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1VNR0; -.
DR   PATRIC; fig|1618675.3.peg.74; -.
DR   Proteomes; UP000034589; 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   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   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          74..243
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          335..587
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
SQ   SEQUENCE   607 AA;  67529 MW;  4644C6F1A2813679 CRC64;
     MGWYRKLFRR LFSWFEVVAI VGIAIALFVF GVGVIWATLS PLPAIENFES RRVAESTKIY
     DRTGNIILYD VHGSMRRTEV PIENISRYIR NATVAIEDDT FYQHNGFRPL SFIRAVLVNL
     HLRGGIAGQG GSTITQQVVK NALLTKDKTI VRKAKEIILA LRLERIYTKD EILQTYLNEA
     PYGGTLYGAE EASRYFFGVS AADVTLAQSA YLAALPQAPT RYSPYGTRRS ELDDRKNLVL
     RRMYELGYIR EEEYRAARDE TVVFQSREET GIKAAHFVFY VREYLEDTYG PDVVTNGGLQ
     VITTLDYDLQ KKAEEIVRER ALENKTKFNA ENAGLVAIDP KTGQILAMVG SRGFFDPDID
     GMVNVTVMPR QPGSAFKPFV YATAFEKGYT PETVVFDLKT QFTAHCAPND LETHDDCYAP
     GNYDNVFRGP MTLRDALAQS VNVPAVKTLY LAGVEASIGL ARRVGITTLA DAGRYGLTLV
     LGGGEVYLLD MTAAYATFAN DGIKNPPVAI LRITDDVKKT LEEYKAKSER VTDAQVARSV
     SDILSDNRAR IPAFGETSAL SFYDHAVAVK TGTTNDYRDA WIIGYTPTLA VGAGKAGRRI
     YHRPPMA
//
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