ID A0A0G0HBG3_9BACT Unreviewed; 855 AA.
AC A0A0G0HBG3;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=US19_C0014G0011 {ECO:0000313|EMBL:KKQ09439.1};
OS Candidatus Daviesbacteria bacterium GW2011_GWB1_36_5.
OC Bacteria; Candidatus Daviesbacteria.
OX NCBI_TaxID=1618426 {ECO:0000313|EMBL:KKQ09439.1, ECO:0000313|Proteomes:UP000034492};
RN [1] {ECO:0000313|EMBL:KKQ09439.1, ECO:0000313|Proteomes:UP000034492}
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:KKQ09439.1}.
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DR EMBL; LBSA01000014; KKQ09439.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0HBG3; -.
DR PATRIC; fig|1618426.3.peg.562; -.
DR Proteomes; UP000034492; 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 NCBIfam; TIGR02074; PBP_1a_fam; 1.
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 26..47
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 72..248
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 338..613
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 643..673
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 855 AA; 92826 MW; FD6DF551C72B96B3 CRC64;
MPLRRIRPSA DYSDIKKVKF LKRLSTLGLT GLFVGLVGLI ILIIFFFTQV PSPEDLQNRS
VAQSTKIYDR NGELLYDIFQ NQNRTPVKLS DVPEVVKKAT IAIEDKDFYK HQGFDVFGIV
RSFYKLIISR RIEGGGSTLT QQLVKNALLT SDQSIIRKIK ELILAIEVER TYTKDQILEM
YLNEIPYGGT AYGIEAASNL YFGKHASELS LAEASLLAGL PQRPSVYSPY GTHPELAKER
QEAVLRRMVE DGYIKKDDAD LAKNQPLTYR TAQNEVGFKA PHFVLYVKQK LIEQYGDKLV
EQGGLKVTTT LDYKLQEESQ KIVKDEIDKI SKYTVGNGAA VVLDPKTGQI LSMVGSKDYF
GKSTPEGCTE GKTCLFEPNV NVALGLRQPG SATKPITYSA GMIKGFTASQ VLVDVKTEFP
GGNKPSYIPV NYDGQFRGPV QVRYALGNSY NIPAVKMLAL VGVKNVMDLG YRMGLTTWEP
TEENVNNAGL SLTLGGREVK LLDLTSAFGV LANKGQRQEP ISILKVTDSK GKDLFEYKQT
SGTKVLDEGI AFIISNILSD NGARSAAFGS NSILNVPGKT VSVKTGTTDE KRDNWTVGYT
PSFVVGVWVG NNNNEVMNPA IASGVTGASP IWQKIMVVAL RGKQDEKPSQ PDGVTLTDVD
GLMGGKPKDG SPTRKEFFLK GSEPSNVSSA YQRLKTCKSN PHRQANDGED LEERDVILLK
EDDPTGANKW QAGIDNWVLT APDARFVGDA KGCSGIPGFA GGGGGGSSPI SIVNVSNGAN
VPRIFDVLAS TNSPNGVKRV VWSIDSVQKA SQTGEPFALH VEFPPGDGGS HTISAELEDN
NGAKFSTSIG VTVAL
//
