HCPC_HELPJ
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 25-MAY-2022, entry version 120.
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; 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. {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}.
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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 STRING; 85963.jhp_1024; -.
DR EnsemblBacteria; AAD06595; AAD06595; jhp_1024.
DR GeneID; 66522285; -.
DR KEGG; hpj:jhp_1024; -.
DR PATRIC; fig|85963.30.peg.1567; -.
DR eggNOG; COG0790; Bacteria.
DR OMA; WYTRLEN; -.
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 InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR13891; PTHR13891; 2.
DR Pfam; PF08238; Sel1; 7.
DR SMART; SM00671; SEL1; 7.
DR SMART; SM00028; TPR; 4.
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
