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Database: UniProt
Entry: A0A0G1REJ0_9BACT
LinkDB: A0A0G1REJ0_9BACT
Original site: A0A0G1REJ0_9BACT 
ID   A0A0G1REJ0_9BACT        Unreviewed;       722 AA.
AC   A0A0G1REJ0;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE            EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN   ORFNames=UX77_C0010G0037 {ECO:0000313|EMBL:KKU55546.1};
OS   Parcubacteria group bacterium GW2011_GWA1_47_11.
OC   Bacteria.
OX   NCBI_TaxID=1618792 {ECO:0000313|EMBL:KKU55546.1, ECO:0000313|Proteomes:UP000034505};
RN   [1] {ECO:0000313|EMBL:KKU55546.1, ECO:0000313|Proteomes:UP000034505}
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:KKU55546.1}.
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DR   EMBL; LCNL01000010; KKU55546.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1REJ0; -.
DR   PATRIC; fig|1618792.3.peg.430; -.
DR   Proteomes; UP000034505; 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        21..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          74..247
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          338..628
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
SQ   SEQUENCE   722 AA;  79849 MW;  2175CB5012F9969C CRC64;
     MKASSNQSFT VTRIKKPRWR SVGMFLVWVI VLGAIAFFSL FIYLAQTLPD PETIAARKIS
     ESTKIYDRTG EVLLYDIHGE EKRTIVAWDR ISDNLKKATL AAEDSNFYNH GGFDVRGIAR
     SLFKDIASLN LSQGGSTITQ QLVKLALLGS EKTPIRKIKE LVLSIEIERR FSKDQIFWMY
     LNQIPYGSNA YGIQAASKTF FDKDASALTI SESAILAALP QAPSRYSPYG NYVPELIGRR
     NNILRRMENL GYISEEEYRL ALEEKPVFRK STESITAPHF VLMVKDYLAK KYGEDAIESA
     GLKVVTTLDA SLQEMAEASV EKYSAVNAQR YKSSNSSLVS VNPKNGDVLA LVGSKNYFDV
     ANQGNYNIAT AQRQPGSAFK PFTYATAFQK GYPDSTILFD ARTEFNPNCS PDSSQLRDQY
     GLACYHPRNY DGLFRGPVTL RQALSQSLNV PSVKTLYLAG IGDTMALAKS MGITTLNEPE
     RYGLSLVLGG AEVRPIDLVS AYGVFANDGI RNPWRIILKI EDVNGNILEE SSDQPRRVID
     EQIARLMNNV LSDNSARAPV FGYNNSLYLP GYDVAAKTGT TQDNRDGWVV GYSPSLATVV
     WSGNNNNDPM TAAGAGISAS GPMWNDFMVK ALATLPRDNF PEPNPVNSPK IMLNGNYVYT
     APDGTQEIHE ILKYVDRNDP SGPFPENPGR DPLFSNWEWP VSKIYGSAEQ SPSPEPSPSP
     TP
//
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