ID HCPB_HELPY Reviewed; 138 AA.
AC O25103;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 27-MAR-2024, entry version 120.
DE RecName: Full=Beta-lactamase HcpB;
DE EC=3.5.2.6 {ECO:0000269|PubMed:11777911};
DE AltName: Full=Cysteine-rich protein B;
GN Name=hcpB; OrderedLocusNames=HP_0336;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Campylobacterota; 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=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 [3]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND DISULFIDE BONDS.
RX PubMed=11777911; DOI=10.1074/jbc.m108993200;
RA Luethy L., Gruetter M.G., Mittl P.R.E.;
RT "The crystal structure of Helicobacter pylori cysteine-rich protein B
RT reveals a novel fold for a penicillin-binding protein.";
RL J. Biol. Chem. 277:10187-10193(2002).
CC -!- FUNCTION: Hydrolyzes 6-aminopenicillinic acid and 7-
CC aminocephalosporanic acid (ACA) derivatives.
CC {ECO:0000269|PubMed:11777911}.
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 Evidence={ECO:0000269|PubMed:11777911};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=174 uM for ampicillin {ECO:0000269|PubMed:11777911};
CC KM=126 uM for benzylpenicillin {ECO:0000269|PubMed:11777911};
CC KM=47 uM for amoxicillin {ECO:0000269|PubMed:11777911};
CC KM=53 uM for nitrocefine {ECO:0000269|PubMed:11777911};
CC Note=kcat is 0.76 min(-1) with ampicillin as substrate. kcat is 0.68
CC min(-1) with benzylpenicillin as substrate. kcat is 0.45 min(-1) with
CC amoxicillin as substrate. kcat is 0.45 min(-1) with nitrocefine as
CC substrate. {ECO:0000269|PubMed:11777911};
CC -!- MISCELLANEOUS: Antibodies against HcpB 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; AAD07408.1; -; Genomic_DNA.
DR PIR; H64561; H64561.
DR RefSeq; WP_001862988.1; NC_018939.1.
DR PDB; 1KLX; X-ray; 1.95 A; A=1-138.
DR PDBsum; 1KLX; -.
DR AlphaFoldDB; O25103; -.
DR SMR; O25103; -.
DR DIP; DIP-3342N; -.
DR IntAct; O25103; 50.
DR MINT; O25103; -.
DR STRING; 85962.HP_0336; -.
DR EnsemblBacteria; AAD07408; AAD07408; HP_0336.
DR KEGG; hpy:HP_0336; -.
DR InParanoid; O25103; -.
DR PhylomeDB; O25103; -.
DR EvolutionaryTrace; O25103; -.
DR Proteomes; UP000000429; Chromosome.
DR GO; GO:0008800; F:beta-lactamase activity; IDA:CACAO.
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; 4.
DR SMART; SM00671; SEL1; 3.
DR SUPFAM; SSF81901; HCP-like; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic resistance; Disulfide bond; Hydrolase;
KW Reference proteome; Repeat; TPR repeat.
FT CHAIN 1..138
FT /note="Beta-lactamase HcpB"
FT /id="PRO_0000221379"
FT REPEAT 1..28
FT /note="TPR 1"
FT REPEAT 57..94
FT /note="TPR 2"
FT REPEAT 97..130
FT /note="TPR 3"
FT DISULFID 22..30
FT /evidence="ECO:0000269|PubMed:11777911"
FT DISULFID 52..60
FT /evidence="ECO:0000269|PubMed:11777911"
FT DISULFID 88..96
FT /evidence="ECO:0000269|PubMed:11777911"
FT DISULFID 124..132
FT /evidence="ECO:0000269|PubMed:11777911"
FT HELIX 7..23
FT /evidence="ECO:0007829|PDB:1KLX"
FT HELIX 29..34
FT /evidence="ECO:0007829|PDB:1KLX"
FT HELIX 41..53
FT /evidence="ECO:0007829|PDB:1KLX"
FT HELIX 57..69
FT /evidence="ECO:0007829|PDB:1KLX"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:1KLX"
FT HELIX 77..89
FT /evidence="ECO:0007829|PDB:1KLX"
FT HELIX 93..105
FT /evidence="ECO:0007829|PDB:1KLX"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:1KLX"
FT HELIX 113..125
FT /evidence="ECO:0007829|PDB:1KLX"
FT HELIX 129..134
FT /evidence="ECO:0007829|PDB:1KLX"
SQ SEQUENCE 138 AA; 15346 MW; 4149505C1BE623B1 CRC64;
MVGGGTVKKD LKKAIQYYVK ACELNEMFGC LSLVSNSQIN KQKLFQYLSK ACELNSGNGC
RFLGDFYENG KYVKKDLRKA AQYYSKACGL NDQDGCLILG YKQYAGKGVV KNEKQAVKTF
EKACRLGSED ACGILNNY
//
