ID HCPC_HELPJ Reviewed; 290 AA. AC Q9ZKB5; DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 27-MAR-2024, entry version 127. DE RecName: Full=Putative beta-lactamase HcpC; DE EC=3.5.2.6; DE AltName: Full=Cysteine-rich protein C; DE Flags: Precursor; GN Name=hcpC; OrderedLocusNames=jhp_1024; 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. {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:0000305}. 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; AAD06595.1; -; Genomic_DNA. DR PIR; C71859; C71859. DR RefSeq; WP_000892769.1; NZ_CP011330.1. DR AlphaFoldDB; Q9ZKB5; -. DR SMR; Q9ZKB5; -. DR GeneID; 66522285; -. DR KEGG; hpj:jhp_1024; -. DR PATRIC; fig|85963.30.peg.1567; -. 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 InterPro; IPR019734; TPR_repeat. 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 SMART; SM00028; TPR; 4. DR SUPFAM; SSF81901; HCP-like; 1. DR PROSITE; PS50005; TPR; 1. PE 3: Inferred from homology; KW Antibiotic resistance; Disulfide bond; Hydrolase; Repeat; Secreted; Signal; KW TPR repeat. FT SIGNAL 1..25 FT /evidence="ECO:0000255" FT CHAIN 26..290 FT /note="Putative beta-lactamase HcpC" FT /id="PRO_0000013197" FT REPEAT 29..62 FT /note="TPR 1" FT REPEAT 64..98 FT /note="TPR 2" FT REPEAT 100..133 FT /note="TPR 3" FT REPEAT 134..170 FT /note="TPR 4" FT REPEAT 172..205 FT /note="TPR 5" FT REPEAT 206..242 FT /note="TPR 6" FT REPEAT 244..278 FT /note="TPR 7" FT DISULFID 56..64 FT /evidence="ECO:0000255" FT DISULFID 92..100 FT /evidence="ECO:0000255" FT DISULFID 128..136 FT /evidence="ECO:0000255" FT DISULFID 164..172 FT /evidence="ECO:0000255" FT DISULFID 200..208 FT /evidence="ECO:0000255" FT DISULFID 236..244 FT /evidence="ECO:0000255" FT DISULFID 272..280 FT /evidence="ECO:0000255" SQ SEQUENCE 290 AA; 31527 MW; 0F5AC40DAEA2427D CRC64; MLENVKKSLF RVLCLGALCL GGLMAEQDPK ELVGLGAKSY KEQDFTQAKK YFEKACDLKE NSGCFNLGVL YYQGHGVEKN LKKAASFYSK ACDLNYSNGC HLLGNLYYSG QGVSQNTNKA LQYYSKACDL KYAEGCASLG GIYHDGKVVT RDFKKAVEYF TKACDLNDGD GCTILGSLYD AGRGTPKDLK KALASYDKAC DLKDSPGCFN AGNMYHHGEG AAKNFKEALA RYSKACELEN GGGCFNLGAM QYNGEGATRN EKQAIENFKK GCKLGAKGAC DILKQLKIKV //