ID A0A023WZX9_9ACTN Unreviewed; 777 AA.
AC A0A023WZX9;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=RradSPS_0504 {ECO:0000313|EMBL:AHY45787.1};
OS Rubrobacter radiotolerans.
OC Bacteria; Actinomycetota; Rubrobacteria; Rubrobacterales; Rubrobacteraceae;
OC Rubrobacter.
OX NCBI_TaxID=42256 {ECO:0000313|EMBL:AHY45787.1, ECO:0000313|Proteomes:UP000025229};
RN [1] {ECO:0000313|EMBL:AHY45787.1, ECO:0000313|Proteomes:UP000025229}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RSPS-4 {ECO:0000313|EMBL:AHY45787.1,
RC ECO:0000313|Proteomes:UP000025229};
RA Egas C.C., Barroso C.C., Froufe H.J.C., Pacheco J.J., Albuquerque L.L.,
RA da Costa M.M.S.;
RT "Complete genome sequence of the Radio-Resistant Rubrobacter radiotolerans
RT RSPS-4.";
RL Submitted (MAR-2014) 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};
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DR EMBL; CP007514; AHY45787.1; -; Genomic_DNA.
DR RefSeq; WP_051589263.1; NZ_CP007514.1.
DR AlphaFoldDB; A0A023WZX9; -.
DR STRING; 42256.RradSPS_0504; -.
DR KEGG; rrd:RradSPS_0504; -.
DR PATRIC; fig|42256.3.peg.512; -.
DR eggNOG; COG0744; Bacteria.
DR HOGENOM; CLU_006354_6_1_11; -.
DR Proteomes; UP000025229; Chromosome.
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 NCBIfam; TIGR02074; PBP_1a_fam; 1.
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 Glycosyltransferase {ECO:0000313|EMBL:AHY45787.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:AHY45787.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000025229};
KW Transferase {ECO:0000313|EMBL:AHY45787.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..44
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 73..252
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 342..596
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 645..777
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 666..762
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 777 AA; 84238 MW; 24014B8D9611A9B1 CRC64;
MSRRRRRLHR QNRLWTWVRT TFLVVAGLGM LALVGVFSSF AYSYNAFADD LPDLSDYQST
ELAQTSIVYD ASGEVISELY GVQNRFVVDL EEVDPTLQDA VVAIEDHRFY QHRGLDFEAI
ARAAQRNVET LSIQEGGSTI TQQLIKNTYI PQEQRAVASF QRKIDEAALA WQYEKENSKD
EILEQYLNTV YFGANAYGAE AAARTYFNKS ASELELAESA LLAGIINLPG AYDPFNDPES
AQARRNVVLD SMLRYGFINE EEHAQATASE IELSRGRVEA RDDNEYFLDA VRREIAREYG
DEAVYEGGLN IYTTLDPRLQ AEASRAVDSV VDPSVGDPSA SLVSIEPQTG AVRAMVGGSD
FEQVKFNLAT QSKRQPGSSF KAFVLAEAID QGISPESVFE SRDLRIPLPA GSEEPFYEVS
NYGFIERGPI TVEEATAQSD NTVFVQLAQE VGMENVVDMA NRLGITSTVE PYLSSAIGGL
GEGVSPLEMA SAYSTFANSG THMEPYLVER VTRGEGENET VLQEHELSGR EVLSRDEAAV
VTETLRGVVE RGTASAFHDL DSEIGRPSAG KTGTTEYFAD AWYVGYIPQL ATSVWVGYPG
ERTPMVNIRG YEEINGENFP LDIWSNYMQG AVQYYDVQQF DTPSSSLDLE VENGGNVRAS
AGGSSDDDGD DNNGGSTTAS SSGSSGGGSS AAAPSSGSSG GLSSSITTPG PSSAPTTPAP
SGGLSSGQPQ IYQVGPDGSF TPISPSDPNY QFYQQQATPL PQPRRSVKRG LVARRSA
//
