HCPD_HELPJ
ID HCPD_HELPJ Reviewed; 305 AA.
AC Q9ZMS0;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 116.
DE RecName: Full=Putative beta-lactamase HcpD;
DE EC=3.5.2.6;
DE AltName: Full=Cysteine-rich protein D;
DE AltName: Full=Penicillin-binding protein 4;
DE Short=PBP 4;
DE Flags: Precursor;
GN Name=hcpD; OrderedLocusNames=jhp_0148;
OS Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J99 / ATCC 700824;
RX PubMed=9923682; DOI=10.1038/16495;
RA Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J.,
RA Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D.,
RA Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.;
RT "Genomic sequence comparison of two unrelated isolates of the human gastric
RT pathogen Helicobacter pylori.";
RL Nature 397:176-180(1999).
CC -!- FUNCTION: May hydrolyze 6-aminopenicillinic acid and 7-
CC aminocephalosporanic acid (ACA) derivatives. Binds to penicillin (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-lactam + H2O = a substituted beta-amino acid;
CC Xref=Rhea:RHEA:20401, ChEBI:CHEBI:15377, ChEBI:CHEBI:35627,
CC ChEBI:CHEBI:140347; EC=3.5.2.6;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the hcp beta-lactamase family. {ECO:0000305}.
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DR EMBL; AE001439; AAD05729.1; -; Genomic_DNA.
DR PIR; F71968; F71968.
DR RefSeq; WP_000597796.1; NC_000921.1.
DR AlphaFoldDB; Q9ZMS0; -.
DR SMR; Q9ZMS0; -.
DR STRING; 85963.jhp_0148; -.
DR EnsemblBacteria; AAD05729; AAD05729; jhp_0148.
DR KEGG; hpj:jhp_0148; -.
DR eggNOG; COG0790; Bacteria.
DR OMA; YYRRGCH; -.
DR Proteomes; UP000000804; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008800; F:beta-lactamase activity; IEA:UniProtKB-EC.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR040239; HcpB-like.
DR InterPro; IPR006597; Sel1-like.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR13891; PTHR13891; 3.
DR Pfam; PF08238; Sel1; 7.
DR SMART; SM00671; SEL1; 7.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Antibiotic resistance; Disulfide bond; Hydrolase; Repeat; Secreted; Signal;
KW TPR repeat.
FT SIGNAL 1..27
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 28..305
FT /note="Putative beta-lactamase HcpD"
FT /id="PRO_0000013199"
FT REPEAT 28..61
FT /note="TPR 1"
FT REPEAT 96..133
FT /note="TPR 2"
FT REPEAT 168..205
FT /note="TPR 3"
FT REPEAT 240..277
FT /note="TPR 4"
FT DISULFID 55..63
FT /evidence="ECO:0000255"
FT DISULFID 91..99
FT /evidence="ECO:0000255"
FT DISULFID 127..135
FT /evidence="ECO:0000255"
FT DISULFID 163..171
FT /evidence="ECO:0000255"
FT DISULFID 199..207
FT /evidence="ECO:0000255"
FT DISULFID 235..243
FT /evidence="ECO:0000255"
FT DISULFID 271..279
FT /evidence="ECO:0000255"
SQ SEQUENCE 305 AA; 33807 MW; 1B969C1EDAD5DEB2 CRC64;
MIKSWTKKWF LILFLMASCF GHLVATTGEK YFKMANQALK RGDYHRAVAF YKRSCNLRMG
VGCTSLGSMY EYGDGVDQNI SKAVFYYRRG CNLRNHLACA SLGSMYEDGD GVQKDFPKAI
YYYRRGCHLK GGVSCGSLGF MYFNGTGVKQ NYAKALSFSK YACSLNYGIS CNFVGYMYKS
AKGVEKDLKK ALANFKRGCH LKDGASCVSL GYLYEAGMDV KQNEEQALNL YKKGCSLKEG
SGCHNVAVMY YTGKGAPKDL EKATSYYKKG CALGFSGSCK VLEVIGKESD NLQDDAQNDT
QDSVQ