ID A0ASK3_HELPX Unreviewed; 568 AA.
AC A0ASK3;
DT 28-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2006, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Penicillin binding protein 1A {ECO:0000313|EMBL:AAW69863.1};
DE Flags: Fragment;
GN Name=pbp1A {ECO:0000313|EMBL:AAW69863.1};
OS Helicobacter pylori (Campylobacter pylori).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=210 {ECO:0000313|EMBL:AAW69863.1};
RN [1] {ECO:0000313|EMBL:AAW69863.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=60 {ECO:0000313|EMBL:AAW69863.1};
RX PubMed=16684266; DOI=10.1111/j.1523-5378.2006.00398.x;
RA Gerrits M.M., Godoy A.P., Kuipers E.J., Ribeiro M.L., Stoof J.,
RA Mendonca S., van Vliet A.H., Pedrazzoli J. Jr, Kusters J.G.;
RT "Multiple mutations in or adjacent to the conserved penicillin-binding
RT protein motifs of the penicillin-binding protein 1A confer amoxicillin
RT resistance to Helicobacter pylori.";
RL Helicobacter 11:181-187(2006).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also
CC transpeptidation of peptidyl-alanyl moieties that are N-acyl
CC substituents of D-alanine.; EC=3.4.16.4;
CC Evidence={ECO:0000256|ARBA:ARBA00034000};
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 -!- 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}.
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DR EMBL; AY743232; AAW69863.1; -; Genomic_DNA.
DR AlphaFoldDB; A0ASK3; -.
DR CAZy; GT51; Glycosyltransferase Family 51.
DR UniPathway; UPA00219; -.
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:UniProtKB-UniPathway.
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:SF27; PENICILLIN-BINDING PROTEIN 1A; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670}.
FT DOMAIN 21..196
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 299..548
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAW69863.1"
FT NON_TER 568
FT /evidence="ECO:0000313|EMBL:AAW69863.1"
SQ SEQUENCE 568 AA; 63608 MW; C0FFEB658B9F1DE1 CRC64;
DIAKIKDYRP SVASQILDRK GRLIANIYDK EFRFYARFEE IPPRFIESLL AVEDTLFFEH
GGINLDAVMR AMIKNAKSGR YTEGGSTLTQ QLVKNMVLTR EKTLTRKLKE AIISLRIEKV
LSKEEILERY LNQTFFGHGY YGVKTASLGY FKKPLDKLTL KEITMLVALP RAPSFYDPTK
NLEFSLSRAN DILRRLYSLG WISSNELKSA LNEVPIVYNQ TSTQNIAPYV VDEVLKQLDQ
LDGLKTQGYT IKLTIDLDYQ RLALESLRFG HQKILEKIAK EKPKTNASND EDEDNLNASM
IVTETSTGKI LALVGGIDYK KSAFNRATQA KRQFGSAIKP FVYQIAFDNG YSTTSKIPDT
ARNFENGNYS KNSVQNHAWH PSNYTRKFLG LVTLQEALSH SLNLATINLS DQLGFEKIYQ
SLSDMGFKNL PKDLTIVLGS FAISPIDAAE KYSLFSNYGT MLKPMLIESI TDQQNNIKVF
TPMETKKITS KEQAFLTLSA LMDAVENGTG SLARIKGLEI AGKTGTSNNN VDAWFIGFTP
TLQSVIWFGR DDNTPIGKGA TGGVVSAP
//
