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 27-MAR-2024, entry version 122. 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; Campylobacterota; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 KEGG; hpj:jhp_0148; -. DR eggNOG; COG0790; Bacteria. 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; Tetratricopeptide repeat domain; 1. DR InterPro; IPR040239; HcpB-like. DR InterPro; IPR006597; Sel1-like. DR InterPro; IPR011990; TPR-like_helical_dom_sf. DR PANTHER; PTHR13891:SF1; CYTOCHROME C OXIDASE ASSEMBLY FACTOR 7; 1. DR PANTHER; PTHR13891; UNCHARACTERIZED; 1. DR Pfam; PF08238; Sel1; 7. DR SMART; SM00671; SEL1; 7. DR SUPFAM; SSF81901; HCP-like; 1. 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 //