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Database: UniProt
Entry: A0A0G0X687_9BACT
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ID   A0A0G0X687_9BACT        Unreviewed;       664 AA.
AC   A0A0G0X687;
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=UU78_C0059G0003 {ECO:0000313|EMBL:KKS20574.1};
OS   Candidatus Roizmanbacteria bacterium GW2011_GWC2_41_7.
OC   Bacteria; Candidatus Roizmanbacteria.
OX   NCBI_TaxID=1618487 {ECO:0000313|EMBL:KKS20574.1, ECO:0000313|Proteomes:UP000034371};
RN   [1] {ECO:0000313|EMBL:KKS20574.1, ECO:0000313|Proteomes:UP000034371}
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:KKS20574.1}.
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DR   EMBL; LCBY01000059; KKS20574.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G0X687; -.
DR   PATRIC; fig|1618487.3.peg.756; -.
DR   Proteomes; UP000034371; 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        18..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          64..240
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          327..575
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
SQ   SEQUENCE   664 AA;  74116 MW;  00004008E1B66C57 CRC64;
     MRKIHLFSRD TQIHIRSFFI GIVAAIVFLF LPYFIYSWLK VLPNPSMLTR RDLEVSTKIY
     DRNGSLLYEI YADQNRNPIP IGEIPKNIIQ ATIAIEDRDF YRHNGFSLKG ISRSLWEIIV
     HHRIQGGSTI TQQLIKSALL TPDVTIVRKI KEIILAFWAE RMYTKNQILE MYFNQVPYGG
     TAWGIESASH TYFGKSIKEL TLAESALLAG LPAAPSEYSP FGSHPEKAFF RQIEVLRRMK
     EDGYVTQEEM DAAYKETIHF TTPNVSMRAP HFVMYIKDIL EKRYGTRLVQ QGGLRVVTSL
     DVTIQEKMQD IVTSQINNLS YLQVGNGAAL VTNPKTGEIL AMVGSRNYFD TKQDGNVNVT
     TSLRQPGSSI KVVTYALALE NGFTPATILD DSPVVYTYPG YPSYAPVNYD GKFHGPTPLR
     YALGNSYNIP AVKLAAKLGV KQIIEKGRLM GIGSWIDESR YGLSITLGGG EVFMTDLAEV
     FGTLANNGKR MDLIPILEVT DYTGKVYERI KEQRGIQAVK PEVAWIMSNI LSDNAARTNA
     FGAQSTLVIP GKTVSVKTGT SNDKRDNWTI GYTQSVLAAV WVGNNDNTPM NPYLSSGVTG
     AAPIWHDMMV ELLKDKQDEI PQRQDSIVSL PCYFGKPEYF IRGTEPAGGR CAPLPTITPT
     PTPK
//
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