ID Q17W35_HELAH Unreviewed; 659 AA.
AC Q17W35;
DT 25-JUL-2006, integrated into UniProtKB/TrEMBL.
DT 25-JUL-2006, sequence version 1.
DT 27-MAR-2024, entry version 100.
DE SubName: Full=Penicillin-binding protein {ECO:0000313|EMBL:CAK00141.1};
GN Name=pbp {ECO:0000313|EMBL:CAK00141.1};
GN OrderedLocusNames=Hac_1411 {ECO:0000313|EMBL:CAK00141.1};
OS Helicobacter acinonychis (strain Sheeba).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=382638 {ECO:0000313|EMBL:CAK00141.1, ECO:0000313|Proteomes:UP000000775};
RN [1] {ECO:0000313|EMBL:CAK00141.1, ECO:0000313|Proteomes:UP000000775}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sheeba {ECO:0000313|EMBL:CAK00141.1,
RC ECO:0000313|Proteomes:UP000000775};
RX PubMed=16789826; DOI=10.1371/journal.pgen.0020120;
RA Eppinger M., Baar C., Linz B., Raddatz G., Lanz C., Keller H., Morelli G.,
RA Gressmann H., Achtman M., Schuster S.C.;
RT "Who ate whom? Adaptive Helicobacter genomic changes that accompanied a
RT host jump from early humans to large felines.";
RL PLoS Genet. 2:1097-1110(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; AM260522; CAK00141.1; -; Genomic_DNA.
DR RefSeq; WP_011578231.1; NC_008229.1.
DR AlphaFoldDB; Q17W35; -.
DR STRING; 382638.Hac_1411; -.
DR CAZy; GT51; Glycosyltransferase Family 51.
DR KEGG; hac:Hac_1411; -.
DR eggNOG; COG0744; Bacteria.
DR HOGENOM; CLU_006354_2_4_7; -.
DR OrthoDB; 9766909at2; -.
DR BioCyc; HACI382638:HAC_RS06005-MONOMER; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000000775; Chromosome.
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..604
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 659 AA; 74063 MW; C50140386BC3F2AB CRC64;
MLKKIFYGLG VLVLIVMGLL AILIAQVWVN TDKDIAKIKD YRPSVASQIL DRKGRLIANI
YDKEFRFYAR FEEIPPRFIE SLLAVEDTLF FEHGGINLDA IMRAMIKNAQ SGRYTEGGST
LTQQLVKNMV LTREKTLTRK LREAIISIRI EQVLSKEEIL ERYLNQTFFG HGYYGVKTAS
LGYFKKPLDK LTLKEIAMLV ALPRAPSFYD PTKNLEFSLS RANDILRRLY SLGWISPSEL
KSALNEVPIV YNQTSTQNIA PYVVDEVLKQ LDQLDGLKTQ GYIIKLTIDL DYQRLALESL
RFGHQRILEK IAKEGPKTDA PNESEDNLNA SMVVTDTSTG KILALVGGID YKKSAFNRAT
QAKRQFGSAI KPFVYQIAFD NGYSTTSKIP DTARNFENDN YSKNSKQNHA WHPSNYSRKF
LGLVTLQEAL SHSLNLATIN LSDQLGFEKV YQSLSDMGFK NLPKDLSIVL GSFAISPIEA
AEKYSLFSHY GVMLKPMLIE SITNQQNEVK TFTPMETKKI TSKEQAFLTL SALMNAVENG
TGGLARVKGL EIAGKTGTSN NNVDAWFIGF TPTLQSVIWF GRDDNTPIGK RATGGIVSAP
VYSYFMRNIL AIEPSLKRKF DVPKNMRKEV VDKIPYYSTP NSITPTPKKT DGGEEPLLF
//
