ID A0A0S1SL12_9BACT Unreviewed; 794 AA.
AC A0A0S1SL12; A0A0S1SH67; A0A0S1SKI3; A0A0S1SQ41; A0A0S1SU71;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=PeribacterD1_0344 {ECO:0000313|EMBL:ALM13042.1};
OS Candidatus Peribacter riflensis.
OC Bacteria; Candidatus Peregrinibacteria; Candidatus Peribacteria;
OC Candidatus Peribacterales; Candidatus Peribacteraceae; Peribacter.
OX NCBI_TaxID=1735162 {ECO:0000313|EMBL:ALM13042.1, ECO:0000313|Proteomes:UP000069135};
RN [1] {ECO:0000313|Proteomes:UP000069135}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Anantharaman K., Brown C.T., Burstein D., Castelle C.J., Probst A.J.,
RA Thomas B.C., Williams K.H., Banfield J.F.;
RT "Analysis of five complete genome sequences for members of the class
RT Peribacteria in the recently recognized Peregrinibacteria bacterial
RT phylum.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ALM13042.1, ECO:0000313|Proteomes:UP000069135}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIFOXYD1_FULL_PER-ii_59_16 {ECO:0000313|EMBL:ALM13042.1};
RX PubMed=26844018;
RA Anantharaman K., Brown C.T., Burstein D., Castelle C.J., Probst A.J.,
RA Thomas B.C., Williams K.H., Banfield J.F.;
RT "Analysis of five complete genome sequences for members of the class
RT Peribacteria in the recently recognized Peregrinibacteria bacterial
RT phylum.";
RL PeerJ 4:E1607-E1607(2016).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP013065; ALM13042.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S1SL12; -.
DR STRING; 1735162.PeribacterB2_0344; -.
DR KEGG; prf:PeribacterA2_0344; -.
DR PATRIC; fig|1735161.3.peg.343; -.
DR Proteomes; UP000069135; Chromosome.
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:0009252; P:peptidoglycan biosynthetic process; IEA:InterPro.
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; 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:SF33; PEPTIDOGLYCAN GLYCOSYLTRANSFERASE; 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 4: Predicted;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670}.
FT DOMAIN 57..231
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 313..580
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT DOMAIN 706..779
FT /note="Penicillin-binding C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06832"
FT REGION 675..705
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 691..705
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 794 AA; 87413 MW; 36B19582C0C73510 CRC64;
MRGNKITRIC MLPRSRHLLW LFPLLALAGA ILLPLPERFL DRKSTSVLLL ERSGQELYEV
RKPTHGSQQW IGLNAIPKPC ISALLAIEDH NFYTHPGVSI KGIARALWQN LSAGRIVSGG
STITQQLARI TLNTRERTLS SKVLEALFAL KLEQTLTKDD ILERYLNTAY FGHRAYGLSA
ATRTFFGKSV HELSTAECTL LAGLPQSPSA LDPFINFTAA RERQGRVLTA MRDQGALTEA
QIEQIESEPI ALTADQTAIR APHFVMWLLN ERPEDLQSPT VTTTLDLTLQ TAVERIIERK
LEELKEKNVT SAAVVVLDAK NGDILAMVGS ADYFDEEHDG AVNSVLAARQ SGSALKPFTY
ALALARGDTA ATTVADTAVQ FLTREGTPYT PRNYDYLEHG LVRYREALAN SYNIAAVRVA
ERVGIDSLLS FLRSAGLSTL TKTPEHYGLA LTLGDAEVRL LELAQAFAIF PRGGETLPIR
TLLSDPTQNG AHILDPKVAW LITDILSDAS ARLSEFGEGG PLTFDFPVAA KTGTTRNSRD
NWTVGFTPDR IVGVWVGNAD NSPMRETSGV TGAGPIFHDV VLAATKNLPM SDFAQPEGLK
QVTICRLSGK LPTELCPHTI EEWFIAGTEP KEPDDLYRLF EIDRRNGLLS NKYCDQEFVD
KKGLAVFPKD TEKWGREQGW PLPPTRVSPL CGDESPTSDS SAPGSASWIE IISPQPNESY
LLDPLIPDAQ EQVIFEAHAS PAIRTMDWYV DGKKIGAAQA PDFRIKWQPQ PGRHQLTAQS
GEERAMLTFE VLAR
//
