ID A0A1Q3VPX0_9PROT Unreviewed; 788 AA.
AC A0A1Q3VPX0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=BGO63_14625 {ECO:0000313|EMBL:OJW48583.1};
OS Candidatus Accumulibacter sp. 66-26.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Candidatus Accumulibacter.
OX NCBI_TaxID=1895689 {ECO:0000313|EMBL:OJW48583.1, ECO:0000313|Proteomes:UP000186203};
RN [1] {ECO:0000313|EMBL:OJW48583.1, ECO:0000313|Proteomes:UP000186203}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=66-26 {ECO:0000313|EMBL:OJW48583.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
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 -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the transpeptidase
CC family. {ECO:0000256|ARBA:ARBA00007090}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the
CC glycosyltransferase 51 family. {ECO:0000256|ARBA:ARBA00007739}.
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:OJW48583.1}.
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DR EMBL; MKUH01000023; OJW48583.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q3VPX0; -.
DR STRING; 1895689.BGO63_14625; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000186203; Unassembled WGS sequence.
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:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0008360; P:regulation of cell shape; 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; IPR011815; PBP_1c.
DR InterPro; IPR009647; PBP_C.
DR InterPro; IPR036950; PBP_transglycosylase.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR NCBIfam; TIGR02073; PBP_1c; 1.
DR PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF15; PENICILLIN-BINDING PROTEIN 1C; 1.
DR Pfam; PF06832; BiPBP_C; 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 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW Protease {ECO:0000256|ARBA:ARBA00022670}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..788
FT /note="peptidoglycan glycosyltransferase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013292882"
FT DOMAIN 58..225
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 321..486
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT DOMAIN 694..772
FT /note="Penicillin-binding C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06832"
FT REGION 632..653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 788 AA; 83724 MW; 294218A8C04FA3E0 CRC64;
MSFRSLRRPL LAVCLALCAG AAGALPAFSE VRSSWRESDA WLLARDGRPV HALRLDLRVR
RLPWTRIEDV SPALLRALLA SEDRRFYEHA GVDWGAAAAS AWRNLWNTRT RGASTLSMQL
VGLLDEYGDE QAARRGRRNV AQKLSQAAGA LWLERRWKKD EILEAYLNLA GFRGELVGVA
AMSRGLFGKW PDGLDEREAA LAAALLRAPG ASPQSVAARA CGVLQATARM QREREQDAAA
DCAGLDGLAR LALSGGLRAE AGGGWLGAEQ SPGLAPHLAR KLLAQPGERL RSTLDADLQR
FSTAALQRHL REIARQNAED GALLVLDNAS GEVLAWVGSS GALSDAPEVD GASALRQAGS
TLKPFLYAQA FERRDLTAAS LIDDSPLALT TGDGLYVPQN YAPQYRGWVS ARMALAGSLN
VPAVRTLVRV GPDAFRDRLH AFGFLSLREP GEHYGYSLAL GSADVSLLML ANAYRTLANG
GLWSPLRAVV GGAGGAAAGS AGKLPTGVSD EAPGAAPRVP CSAAGCAGVF SGRARRAAPA
APVFVAADIL ADRAARAGTF GLESWLATPY WSAVKTGTSK DMRDNWCIGF SRRYTVAVWV
GNAAGEAMRD VSGVSGAAPV WREVMDWLQR GDDSAGAGRR GVVRSEPPPA PPGVQRLAVR
FAPADKVREP PREEWFLAGT GMRVVQLAEA QALARIAYPG QGTVVALDPD IPPARQRIAL
QLSGPPGAGW QWRLDGAPLG GAAREVLWRP RPGSHRLALH GADGREIEAV SFEVRALRGR
GAAGRAPR
//
