ID A9ZLW4_HELPX Unreviewed; 662 AA.
AC A9ZLW4;
DT 26-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Penicillin binding protein {ECO:0000313|EMBL:BAF96846.1};
GN Name=pbp1 {ECO:0000313|EMBL:BAF96846.1};
OS Helicobacter pylori (Campylobacter pylori).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=210 {ECO:0000313|EMBL:BAF96846.1};
RN [1] {ECO:0000313|EMBL:BAF96846.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HPA1007 {ECO:0000313|EMBL:BAF96846.1};
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; AB128020; BAF96846.1; -; Genomic_DNA.
DR AlphaFoldDB; A9ZLW4; -.
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..594
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 662 AA; 74399 MW; D83B952FE0946479 CRC64;
MLKKIFYGFI VLFLIVVGLL AILIAQVWVS TNKDIAKIKD YRPSVASQIL DRKGRLIANI
YDKEFRFYAR FEEIPPRFIE SLLAVEDTLF FEHGGINLDA IMRAMIKNAK SGRYTEGGST
LTQQLVKNMV LTREKTLTRK LKEAIISIRI EKVLSKEEIL ERYLNQTFFG HGYYGVKTAS
LGYFKKPLDK LTLKEIAMLV ALPRAPSFYD PTKNLEFSLS RANDILRRLY SLGWISSNEF
KSALNEVPIV YNQTSTQNIA PYVVDEVLKQ LDQLDGLKTQ GYTIKLTIDL DYQRLALESL
RFGHQKILEK IAKEEPKTNA SNEDEDNLNA SMIVTDTSTG KILALVGGID YKKSTFNRAT
QAKRQFGSAI KPFVYQIAFD NGYSTTSKIP DTARNFENGN YSKNSEQNHA WHPRNYSRKF
LGLVTLQEAL SHSLNLATIN LSDQLGFEKI YQSLSDMGFK NLPKKDLSIV LGSLAISPIE
AAEKYSLFSN YGTMLKPMLI ESITDQQNDV KTFTPMETKK ITSKEQAFLT LSVLMNAVEN
GTGSLARIKG LEIAGKTGTS NNNTDAWFIG FTPTLQSVIW FGRDDNTPTG KGATGGGAVV
SAPVYSYFMR NILAIEPSLK RKFDVPKGLH KEIVDKIPYY STPNSITPTP QKTDDGEEPL
LF
//
