GenomeNet

Database: UniProt
Entry: A0A0G1WFD9_9BACT
LinkDB: A0A0G1WFD9_9BACT
Original site: A0A0G1WFD9_9BACT 
ID   A0A0G1WFD9_9BACT        Unreviewed;       534 AA.
AC   A0A0G1WFD9;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE            EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN   ORFNames=UY57_C0016G0017 {ECO:0000313|EMBL:KKW17511.1};
OS   Candidatus Kaiserbacteria bacterium GW2011_GWB1_50_17.
OC   Bacteria; Candidatus Kaiserbacteria.
OX   NCBI_TaxID=1618673 {ECO:0000313|EMBL:KKW17511.1, ECO:0000313|Proteomes:UP000034120};
RN   [1] {ECO:0000313|EMBL:KKW17511.1, ECO:0000313|Proteomes:UP000034120}
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:KKW17511.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LCQM01000016; KKW17511.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1WFD9; -.
DR   PATRIC; fig|1618673.3.peg.259; -.
DR   Proteomes; UP000034120; 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..519
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
SQ   SEQUENCE   534 AA;  59676 MW;  48D61704D51E7630 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 VLLL
//
DBGET integrated database retrieval system