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Database: UniProt
Entry: A0A0G1Z3K0_9BACT
LinkDB: A0A0G1Z3K0_9BACT
Original site: A0A0G1Z3K0_9BACT 
ID   A0A0G1Z3K0_9BACT        Unreviewed;       496 AA.
AC   A0A0G1Z3K0;
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};
DE   Flags: Fragment;
GN   ORFNames=UY52_C0045G0005 {ECO:0000313|EMBL:KKW13374.1};
OS   Parcubacteria group bacterium GW2011_GWC2_49_9.
OC   Bacteria.
OX   NCBI_TaxID=1618934 {ECO:0000313|EMBL:KKW13374.1, ECO:0000313|Proteomes:UP000034059};
RN   [1] {ECO:0000313|EMBL:KKW13374.1, ECO:0000313|Proteomes:UP000034059}
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:KKW13374.1}.
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DR   EMBL; LCQH01000045; KKW13374.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1Z3K0; -.
DR   Proteomes; UP000034059; 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..35
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          70..239
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          330..473
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
FT   NON_TER         496
FT                   /evidence="ECO:0000313|EMBL:KKW13374.1"
SQ   SEQUENCE   496 AA;  55277 MW;  F8E07ABBEB3E3EF7 CRC64;
     MRRKILGIRK RYFKEAALVV IILGIFAVGS LFLWVSTFTI PDLSSFNERK VSQSTKIYDR
     TGTILLYDLN RGIKRTVVTD NEISRNIKNA TVAIEDSEFY THHGIRPTSI FRAILANIGA
     GGFSQGGSTI TQQVVKNSLL TTEKKISRKL KEWILALKLE RVLSKIEILN LYLNEAPYGG
     TVYGIEEAGQ TYFGKKAADL SIAESAYLAS LPNAPSYFSP YGNNKQKLED RKNLVLAKML
     EKKFINQEEY SRAINEKVVW KPQENLGIKA PHFVMFIRQY LEEKYGKAIV EQGGLKVITT
     LDYGLQEKAE AMAKQYASEN EKKFNAENVS LIALDPKTGQ ILAMVGSRDY FDKTIDGNFN
     VALAHRQPGS SFKPIVYAEA FKKGYTPETV VFDLQTEFST ECNPDGTPIT AGNEDRCYMP
     ENYDHVYRGP INLRNALAQS INIAAIKVLY LAGIKDSLRL AKDMGIKSLT NVGQYGLTLV
     LGGGEVSLLD LTGAYG
//
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