ID A9ZLW9_HELPX Unreviewed; 659 AA.
AC A9ZLW9;
DT 26-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=Penicillin binding protein {ECO:0000313|EMBL:BAF96851.1};
GN Name=pbp1 {ECO:0000313|EMBL:BAF96851.1};
OS Helicobacter pylori (Campylobacter pylori).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=210 {ECO:0000313|EMBL:BAF96851.1};
RN [1] {ECO:0000313|EMBL:BAF96851.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HPA1012 {ECO:0000313|EMBL:BAF96851.1};
RA Shirai M.;
RT "H. pylori pbp1 gene.";
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
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; AB128025; BAF96851.1; -; Genomic_DNA.
DR AlphaFoldDB; A9ZLW9; -.
DR CAZy; GT51; Glycosyltransferase Family 51.
DR UniPathway; UPA00219; -.
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: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 Membrane {ECO:0000256|SAM:Phobius};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 54..229
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 331..603
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 659 AA; 74125 MW; EEF0DA67A9A6B0C7 CRC64;
MLKKIFYGFI VLFLIIVGLL AILIAQVWVS TNKDIAKIRD YRPSVASQIL DRKGRLIANI
YDKEFRFYAR FEEIPPRFIE SLLAVEDTLF FEHGGINLDA IMRAMIKNAK SGRYTEGGST
LTQQLVKNMV LTREKTLTRK LKEAIISIRI EKVLSKEEIL ERYLNQTFFG HGYYGVKTAS
LGYFKKPLDK LTLKEITMLV ALPRAPSFYD PTKNLKFSLS RANDILRRLY SLGWISSNEL
KGALNEVPII YNQTSTQNIA PYVVDEVLKQ LDQLDGLKTQ GYTIKLTIDL DYQRLALESL
RFGHQKILEK IAKEEPKTNA SNEDEDNLNA SMIVTDTSTG KILALVGGID YKKSAFNRAT
QAKRQFGSAI KPFLYQIAFD NGYSTTSKIP DTARNFEDGN YSKNSEQNHA WHPSNYSRKF
LGLVTLQEAL SHSLNLATIN LSDQLGFEKI YQSLSDMGFK NLPKDLSIVL GSFAISPIEA
AEKYSLFSNY GTMLKPMLIE SITDQQNDVK TFTPIETKKI TSKEQAFLTL SVLMNAVENG
TGSLARIKGL EIAGKTGTSN NDIDAWFIGF TPTLQSVIWF GRDDNTPIGK GASGGVVSAP
VYSYFMRNIL AIEPSLKRKF DVPKGLRKEI VDKIPYYSTP NSITPTPQKT DDGEEPLLF
//
