ID G8PDT6_PEDCP Unreviewed; 712 AA.
AC G8PDT6;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN OrderedLocusNames=PECL_1159 {ECO:0000313|EMBL:AEV95421.1};
OS Pediococcus claussenii (strain ATCC BAA-344 / DSM 14800 / JCM 18046 / KCTC
OS 3811 / P06).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Pediococcus.
OX NCBI_TaxID=701521 {ECO:0000313|EMBL:AEV95421.1, ECO:0000313|Proteomes:UP000005444};
RN [1] {ECO:0000313|Proteomes:UP000005444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-344 / DSM 14800 / JCM 18046 / KCTC 3811 / P06
RC {ECO:0000313|Proteomes:UP000005444};
RA Pittet V., Abegunde T., Marfleet T., Haakensen M., Morrow K.,
RA Jayaprakash T., Schroeder K., Trost B., Byrns S., Bergsveinson J.,
RA Kusalik A., Ziola B.;
RT "Genome and plasmid sequences for the beer-spoilage organism Pediococcus
RT claussenii ATCC BAA-344T.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEV95421.1, ECO:0000313|Proteomes:UP000005444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-344 / DSM 14800 / JCM 18046 / KCTC 3811 / P06
RC {ECO:0000313|Proteomes:UP000005444};
RX PubMed=22328764; DOI=10.1128/JB.06759-11;
RA Pittet V., Abegunde T., Marfleet T., Haakensen M., Morrow K.,
RA Jayaprakash T., Schroeder K., Trost B., Byrns S., Bergsveinson J.,
RA Kusalik A., Ziola B.;
RT "Complete Genome Sequence of the Beer Spoilage Organism Pediococcus
RT claussenii ATCC BAA-344T.";
RL J. Bacteriol. 194:1271-1272(2012).
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; CP003137; AEV95421.1; -; Genomic_DNA.
DR AlphaFoldDB; G8PDT6; -.
DR STRING; 701521.PECL_1159; -.
DR KEGG; pce:PECL_1159; -.
DR PATRIC; fig|701521.8.peg.1101; -.
DR eggNOG; COG0744; Bacteria.
DR HOGENOM; CLU_006354_2_2_9; -.
DR Proteomes; UP000005444; Chromosome.
DR GO; GO:0016020; C:membrane; 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:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 6.20.370.110; -; 1.
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:SF32; PENICILLIN-BINDING PROTEIN 2A; 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 Reference proteome {ECO:0000313|Proteomes:UP000005444};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 38..59
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 90..263
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 361..608
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 712 AA; 78087 MW; 88FAB94B45B06A11 CRC64;
MLSMKNQNGF MAKIIAWLKP IFKVINRFIK KYWHRYQITR WIIVFFLGIF FAMSAYLTFE
AKTANVGDLK AALSKSTVIY DDDNSKAGSL YSQKGTWVDL DKISPNVQNA VISTEDRNFY
KEHGFSIKGI GRAAVLFAMN KLLGRDYISG GGSTLTQQLV KNAFLSQQQT FSRKARELFL
SVEVENVYSK QDILAMYLNN AYFGNGVWGV QDAAKRYFGV SASELSVPQS AVIAGMLTNP
SGFNPVDHPT NAKDRRNVVL GLMEENGKIS ASQEKTYQQE PVLTANTYHY EDTYKYPYYF
DSVISEAINR YGLTEADIMN RGYKIYTYLD QSKQTGMEQT FDNAANFPSN ATDGTMVQAS
SVAVDPKNGG VEAVVGGRGK HVFRGFNRAT QIKRQPGSTL KPIAVYAPAI EDGYSYDSNL
QDKLTSYGSN NYRPANYNDQ YSGKLPMYQA LEQSKNAPAV WLLNKIGVNK GYDSVEKFGL
HPESGDKNLA MALGGLTKGV SPLQLAGAYT AFANDGNLAQ TGFIRKIVDA SGNVIVNNQP
STKKIISTKV SKEMTSMMLG VYNDSAGTGY GAEPAGYTIA GKTGSTEADG TGSADATKDK
WMVGYTPDIV VATWEGFDDT NKAHHLENIT GVGMNGLFRS EMGAILPSTK GTKFDTQMAS
TLAQNSGSPS NLWDDIQNGT SSIQDSISQG TNTVRDKAEE WFNDAKNFIT GH
//
