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HCPC_HELPY
ID   HCPC_HELPY              Reviewed;         290 AA.
AC   O25728;
DT   15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 129.
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=HP_1098;
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   ANTIGENICITY.
RX   PubMed=11921447;
RX   DOI=10.1002/1615-9861(200203)2:3<313::aid-prot313>3.0.co;2-7;
RA   Haas G., Karaali G., Ebermayer K., Metzger W.G., Lamer S., Zimny-Arndt U.,
RA   Diescher S., Goebel U.B., Vogt K., Roznowski A.B., Wiedenmann B.J.,
RA   Meyer T.F., Aebischer T., Jungblut P.R.;
RT   "Immunoproteomics of Helicobacter pylori infection and relation to gastric
RT   disease.";
RL   Proteomics 2:313-324(2002).
RN   [3]
RP   ANTIGENICITY.
RX   PubMed=12853383; DOI=10.1128/cdli.10.4.542-545.2003;
RA   Mittl P.R.E., Luethy L., Reinhardt C., Joller H.;
RT   "Detection of high titers of antibody against Helicobacter cysteine-rich
RT   proteins A, B, C, and E in Helicobacter pylori-infected individuals.";
RL   Clin. Diagn. Lab. Immunol. 10:542-545(2003).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 24-290, AND DISULFIDE BONDS.
RX   PubMed=15223324; DOI=10.1016/j.jmb.2004.04.055;
RA   Luethy L., Grutter M.G., Mittl P.R.E.;
RT   "The crystal structure of Helicobacter cysteine-rich protein C at 2.0 A
RT   resolution: similar peptide-binding sites in TPR and SEL1-like repeat
RT   proteins.";
RL   J. Mol. Biol. 340:829-841(2004).
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   -!- MISCELLANEOUS: Antibodies against HcpC are present in sera from human
CC       patients infected by Helicobacter pylori.
CC   -!- SIMILARITY: Belongs to the hcp beta-lactamase family. {ECO:0000305}.
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DR   EMBL; AE000511; AAD08141.1; -; Genomic_DNA.
DR   PIR; B64657; B64657.
DR   RefSeq; NP_207889.1; NC_000915.1.
DR   RefSeq; WP_000892717.1; NC_018939.1.
DR   PDB; 1OUV; X-ray; 2.00 A; A=24-290.
DR   PDBsum; 1OUV; -.
DR   AlphaFoldDB; O25728; -.
DR   SMR; O25728; -.
DR   DIP; DIP-3502N; -.
DR   IntAct; O25728; 1.
DR   MINT; O25728; -.
DR   STRING; 85962.C694_05665; -.
DR   PaxDb; O25728; -.
DR   EnsemblBacteria; AAD08141; AAD08141; HP_1098.
DR   KEGG; hpy:HP_1098; -.
DR   PATRIC; fig|85962.47.peg.1178; -.
DR   eggNOG; COG0790; Bacteria.
DR   OMA; WYTRLEN; -.
DR   PhylomeDB; O25728; -.
DR   EvolutionaryTrace; O25728; -.
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   InterPro; IPR019734; TPR_repeat.
DR   PANTHER; PTHR13891; PTHR13891; 2.
DR   Pfam; PF08238; Sel1; 7.
DR   SMART; SM00671; SEL1; 7.
DR   SMART; SM00028; TPR; 3.
DR   PROSITE; PS50005; TPR; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Antibiotic resistance; Disulfide bond; Hydrolase;
KW   Reference proteome; Repeat; Secreted; Signal; TPR repeat.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..290
FT                   /note="Putative beta-lactamase HcpC"
FT                   /id="PRO_0000013196"
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:0000269|PubMed:15223324"
FT   DISULFID        92..100
FT                   /evidence="ECO:0000269|PubMed:15223324"
FT   DISULFID        128..136
FT                   /evidence="ECO:0000269|PubMed:15223324"
FT   DISULFID        164..172
FT                   /evidence="ECO:0000269|PubMed:15223324"
FT   DISULFID        200..208
FT                   /evidence="ECO:0000269|PubMed:15223324"
FT   DISULFID        236..244
FT                   /evidence="ECO:0000269|PubMed:15223324"
FT   DISULFID        272..280
FT                   /evidence="ECO:0000269|PubMed:15223324"
FT   HELIX           29..41
FT                   /evidence="ECO:0007829|PDB:1OUV"
FT   HELIX           45..57
FT                   /evidence="ECO:0007829|PDB:1OUV"
FT   HELIX           61..73
FT                   /evidence="ECO:0007829|PDB:1OUV"
FT   STRAND          75..77
FT                   /evidence="ECO:0007829|PDB:1OUV"
FT   HELIX           81..93
FT                   /evidence="ECO:0007829|PDB:1OUV"
FT   HELIX           97..109
FT                   /evidence="ECO:0007829|PDB:1OUV"
FT   STRAND          111..113
FT                   /evidence="ECO:0007829|PDB:1OUV"
FT   HELIX           117..129
FT                   /evidence="ECO:0007829|PDB:1OUV"
FT   HELIX           133..145
FT                   /evidence="ECO:0007829|PDB:1OUV"
FT   STRAND          147..149
FT                   /evidence="ECO:0007829|PDB:1OUV"
FT   HELIX           153..165
FT                   /evidence="ECO:0007829|PDB:1OUV"
FT   HELIX           169..181
FT                   /evidence="ECO:0007829|PDB:1OUV"
FT   STRAND          183..185
FT                   /evidence="ECO:0007829|PDB:1OUV"
FT   HELIX           189..201
FT                   /evidence="ECO:0007829|PDB:1OUV"
FT   HELIX           205..217
FT                   /evidence="ECO:0007829|PDB:1OUV"
FT   HELIX           225..237
FT                   /evidence="ECO:0007829|PDB:1OUV"
FT   HELIX           241..252
FT                   /evidence="ECO:0007829|PDB:1OUV"
FT   STRAND          255..258
FT                   /evidence="ECO:0007829|PDB:1OUV"
FT   HELIX           264..274
FT                   /evidence="ECO:0007829|PDB:1OUV"
FT   HELIX           277..284
FT                   /evidence="ECO:0007829|PDB:1OUV"
SQ   SEQUENCE   290 AA;  31594 MW;  0F0CFD779A6F108E CRC64;
     MLENVKKSFF RVLCLGALCL GGLMAEQDPK ELVGLGAKSY KEKDFTQAKK YFEKACDLKE
     NSGCFNLGVL YYQGQGVEKN LKKAASFYAK ACDLNYSNGC HLLGNLYYSG QGVSQNTNKA
     LQYYSKACDL KYAEGCASLG GIYHDGKVVT RDFKKAVEYF TKACDLNDGD GCTILGSLYD
     AGRGTPKDLK KALASYDKAC DLKDSPGCFN AGNMYHHGEG ATKNFKEALA RYSKACELEN
     GGGCFNLGAM QYNGEGVTRN EKQAIENFKK GCKLGAKGAC DILKQLKIKV
 
 
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