ID   HCPD_HELPY              Reviewed;         306 AA.
AC   O24968;
DT   15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 113.
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=HP_0160;
OS   Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85962;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700392 / 26695;
RX   PubMed=9252185; DOI=10.1038/41483;
RA   Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA   Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA   Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA   Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA   McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA   Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA   Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA   Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT   "The complete genome sequence of the gastric pathogen Helicobacter
RT   pylori.";
RL   Nature 388:539-547(1997).
RN   [2]
RP   PENICILLIN-BINDING.
RX   PubMed=10438788; DOI=10.1128/jb.181.16.5107-5110.1999;
RA   Krishnamurthy P., Parlow M.H., Schneider J., Burroughs S., Wickland C.,
RA   Vakil N.B., Dunn B.E., Phadnis S.H.;
RT   "Identification of a novel penicillin-binding protein from Helicobacter
RT   pylori.";
RL   J. Bacteriol. 181:5107-5110(1999).
CC   -!- FUNCTION: May hydrolyze 6-aminopenicillinic acid and 7-
CC       aminocephalosporanic acid (ACA) derivatives (By similarity). Binds to
CC       penicillin. {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; AE000511; AAD07230.1; -; Genomic_DNA.
DR   PIR; H64539; H64539.
DR   RefSeq; NP_206959.1; NC_000915.1.
DR   RefSeq; WP_000597856.1; NC_018939.1.
DR   AlphaFoldDB; O24968; -.
DR   SMR; O24968; -.
DR   STRING; 85962.C694_00800; -.
DR   PaxDb; O24968; -.
DR   EnsemblBacteria; AAD07230; AAD07230; HP_0160.
DR   KEGG; hpy:HP_0160; -.
DR   PATRIC; fig|85962.47.peg.173; -.
DR   eggNOG; COG0790; Bacteria.
DR   OMA; YYRRGCH; -.
DR   PhylomeDB; O24968; -.
DR   Proteomes; UP000000429; 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; 2.
DR   Pfam; PF08238; Sel1; 7.
DR   SMART; SM00671; SEL1; 7.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   1: Evidence at protein level;
KW   Antibiotic resistance; Disulfide bond; Hydrolase; Reference proteome;
KW   Repeat; Secreted; Signal; TPR repeat.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           26..306
FT                   /note="Putative beta-lactamase HcpD"
FT                   /id="PRO_0000013198"
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   306 AA;  34097 MW;  D3BDE25CA3009B87 CRC64;
     MIKSWTKKWF LILFLMASCS SYLVATTGEK YFKMATQAFK RGDYHKAVAF YKRSCNLRVG
     VGCTSLGSMY EDGDGVDQNI TKAVFYYRRG CNLRNHLACA SLGSMYEDGD GVQKNLPKAI
     YYYRRGCHLK GGVSCGSLGF MYFNGTGVKQ NYAKALFLSK YACSLNYGIS CNFVGYMYRN
     AKGVQKDLKK ALANFKRGCH LKDGASCVSL GYMYEVGMDV KQNGEQALNL YKKGCYLKRG
     SGCHNVAVMY YTGKGVPKDL DKAISYYKKG CTLGFSGSCK VLEEVIGKKS DDLQDDAQND
     TQDDMQ