ID E2E8M6_LISMN Unreviewed; 289 AA.
AC E2E8M6;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
DE Flags: Fragment;
GN Name=pbpA {ECO:0000313|EMBL:ADN88663.1};
OS Listeria monocytogenes.
OC Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=1639 {ECO:0000313|EMBL:ADN88663.1};
RN [1] {ECO:0000313|EMBL:ADN88663.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FSL C1-406 {ECO:0000313|EMBL:ADN88663.1}, FSL E1-039
RC {ECO:0000313|EMBL:ADN88693.1}, FSL S4-440
RC {ECO:0000313|EMBL:ADN88701.1}, and FSL S4-643
RC {ECO:0000313|EMBL:ADN88692.1};
RX PubMed=20656873; DOI=10.1128/AEM.00447-10;
RA den Bakker H.C., Bundrant B.N., Fortes E.D., Orsi R.H., Wiedmann M.;
RT "A population genetics-based and phylogenetic approach to understanding the
RT evolution of virulence in the genus Listeria.";
RL Appl. Environ. Microbiol. 76:6085-6100(2010).
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; GU475751; ADN88663.1; -; Genomic_DNA.
DR EMBL; GU475780; ADN88692.1; -; Genomic_DNA.
DR EMBL; GU475781; ADN88693.1; -; Genomic_DNA.
DR EMBL; GU475789; ADN88701.1; -; Genomic_DNA.
DR AlphaFoldDB; E2E8M6; -.
DR CAZy; GT51; Glycosyltransferase Family 51.
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; 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 PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF29; PENICILLIN-BINDING PROTEIN 1A; 1.
DR Pfam; PF00912; Transgly; 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:ARBA00022670};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670}.
FT DOMAIN 1..113
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ADN88663.1"
FT NON_TER 289
FT /evidence="ECO:0000313|EMBL:ADN88663.1"
SQ SEQUENCE 289 AA; 33144 MW; 0B0AF29E0D7EC495 CRC64;
ASTLSQQIIK MSYLDYTNKT LARKAQEAWL ALQLEEKYSK NDILEIYVNK VYMSDRVHGM
QTASEHYFGK NLKDLTLAQT ALLAGMPQSP NNYNPYEHPE AAKKRRDQVL TNMYTHDKIT
KEEMTEAQKT SITTGLRSKK DREDKIYKYD SYVTQVLSEI PKEYDVYRDG LTIHTALDRD
AQEYTEKMLN TNEIVNFTDD EMQAGIVLQD TKTGRVQAIG GGRKQKVTRG YNYATQVKRS
VGSTMKPIAD YGPAFEYLDW STAHILEDEP YTYSGGTPIN NWDFAYKGP
//
