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Database: UniProt
Entry: A0A0G0M851_9BACT
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ID   A0A0G0M851_9BACT        Unreviewed;       885 AA.
AC   A0A0G0M851;
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=US90_C0010G0002 {ECO:0000313|EMBL:KKQ69864.1};
OS   Candidatus Shapirobacteria bacterium GW2011_GWE2_38_30.
OC   Bacteria; Candidatus Shapirobacteria.
OX   NCBI_TaxID=1618490 {ECO:0000313|EMBL:KKQ69864.1, ECO:0000313|Proteomes:UP000034406};
RN   [1] {ECO:0000313|EMBL:KKQ69864.1, ECO:0000313|Proteomes:UP000034406}
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:KKQ69864.1}.
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DR   EMBL; LBUT01000010; KKQ69864.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G0M851; -.
DR   STRING; 1618490.US90_C0010G0002; -.
DR   PATRIC; fig|1618490.4.peg.456; -.
DR   Proteomes; UP000034406; 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   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR001264; Glyco_trans_51.
DR   InterPro; IPR013783; Ig-like_fold.
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; PF17957; Big_7; 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        39..65
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          90..266
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          345..632
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
SQ   SEQUENCE   885 AA;  98794 MW;  B177C876CF60F02E CRC64;
     MKRKLKLFYF RFKKRCEQLK WNLSEYMRKK GIKLNKKRLA YWFVLAFFGL TIVGFLGSFI
     VFAWFSKDLP TPSKVVRREG YASRIYDRNG ELLYDVYKDS KRTPVESIDD IPKYLREAVV
     AVEDKDFYKH QGFDPLAPFR IIKNVFVLHR LTGGSTLTQQ LVKNVLLTSD RTITRKIKEF
     ILAVQIEKKY SKDEILLMYL NESPYGGPFW GVGTASEQYF DKKVKDLDLV ESVILAGIPQ
     RPNVYSPFSG TPQAYSERAA HVLERMREDG YISSELEKET LEKVKKYKFN ENSSQILAPH
     FVFWVKVEGG GLKITTTLDL KLQQETQKIV TEEIDKAESK GISNGAAIVV DPINGQVLAM
     VGSRGYFSDK TDGKYNVVTA GLRQPGSAIK PVTYLVAIKK GWTAASMIMD VPVTFPGVGG
     QKDYSPNNYN GKFNGPMSLR NALGNSINTI AVKMLANVGI KNMLQQAYDM GMTTLEPTAE
     NLSRFGLAVT LGGAEVRMSE LAAGYSSFAN GGKRVDLVGV LKVEDGDGKV LEEYKEVAGK
     QVMTPQEAFI INNILSDNSA RELTFGAVNS LVISNYQVAV KTGTTNDKRD NWAIGWTPNL
     LTAVWVGNND NSEMKSVASG VSGATPIWQR IMKFEIPKRQ KQDFSIPDRI VNMQVDALSG
     YAAHDGFPSR SDYFIDGTQP RITDPIHMKL KVCKGVSGLA TPEDVARGNY DEKEFIKLSE
     NDPISKDGKN RWQEGIDNWI LQQPDKDKYY PPSGYCRDDG MLDVGFESPS NQSTVGNEVQ
     VKITTSSLVK VTEVKLWVDG EEKKTWGEKP YETTINLADG PHSLKVKATD REGNTNEKEI
     KIGVNVAWDW KPAPVVTNTP IPSPTRILSP TLIPSLIPTG IGLTL
//
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