HCPA_HELPY
ID HCPA_HELPY Reviewed; 250 AA.
AC O25001; O32634; O85223;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 132.
DE RecName: Full=Beta-lactamase HcpA;
DE EC=3.5.2.6 {ECO:0000269|PubMed:10748053};
DE AltName: Full=Cysteine-rich 28 kDa protein;
DE Flags: Precursor;
GN Name=hcpA; OrderedLocusNames=HP_0211;
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 [GENOMIC DNA].
RC STRAIN=ATCC 49503 / 60190;
RX PubMed=9317022; DOI=10.1128/iai.65.10.4158-4164.1997;
RA Karita M., Etterbeek M.L., Forsyth M.H., Tummuru M.K.R., Blaser M.J.;
RT "Characterization of Helicobacter pylori dapE and construction of a
RT conditionally lethal dapE mutant.";
RL Infect. Immun. 65:4158-4164(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 49503 / 60190;
RX PubMed=9596777; DOI=10.1128/iai.66.6.2984-2986.1998;
RA Cao P., McClain M.S., Forsyth M.H., Cover T.L.;
RT "Extracellular release of antigenic proteins by Helicobacter pylori.";
RL Infect. Immun. 66:2984-2986(1998).
RN [3]
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 [4]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, MASS SPECTROMETRY, DISULFIDE BONDS, AND SUBUNIT.
RX PubMed=10748053; DOI=10.1074/jbc.m001869200;
RA Mittl P.R.E., Luethy L., Hunziker P., Gruetter M.G.;
RT "The cysteine-rich protein A from Helicobacter pylori is a beta-
RT lactamase.";
RL J. Biol. Chem. 275:17693-17699(2000).
RN [5]
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).
CC -!- FUNCTION: Slowly hydrolyzes 6-aminopenicillinic acid and 7-
CC aminocephalosporanic acid (ACA) derivatives. May be involved in the
CC synthesis of the cell wall peptidoglycan.
CC {ECO:0000269|PubMed:10748053}.
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:10748053};
CC -!- ACTIVITY REGULATION: Inhibited by cloxacillin and oxacillin but not by
CC ACA derivatives or metal chelators. {ECO:0000269|PubMed:10748053}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=145 uM for ampicillin {ECO:0000269|PubMed:10748053};
CC KM=48 uM for benzylpenicillin {ECO:0000269|PubMed:10748053};
CC KM=155 uM for amoxicillin {ECO:0000269|PubMed:10748053};
CC KM=406 uM for cephaloridine {ECO:0000269|PubMed:10748053};
CC KM=47 uM for nitrocefine {ECO:0000269|PubMed:10748053};
CC Note=kcat is 1.06 min(-1) with ampicillin as substrate. kcat is 0.74
CC min(-1) with benzylpenicillin as substrate. kcat is 0.55 min(-1) with
CC amoxicillin as substrate. kcat is 0.30 min(-1) with cephaloridine as
CC substrate. kcat is 0.28 min(-1) with nitrocefine as substrate.
CC {ECO:0000269|PubMed:10748053};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:10748053}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9596777}.
CC -!- MASS SPECTROMETRY: Mass=25613; Mass_error=1.6; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:10748053};
CC -!- MISCELLANEOUS: Antibodies against HcpA 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; AF008565; AAB63298.1; -; Genomic_DNA.
DR EMBL; AF053708; AAC24210.1; -; Genomic_DNA.
DR EMBL; AE000511; AAD07279.1; -; Genomic_DNA.
DR PIR; C64546; C64546.
DR RefSeq; NP_207009.1; NC_000915.1.
DR RefSeq; WP_000901420.1; NC_018939.1.
DR AlphaFoldDB; O25001; -.
DR SMR; O25001; -.
DR STRING; 85962.C694_01060; -.
DR PaxDb; O25001; -.
DR EnsemblBacteria; AAD07279; AAD07279; HP_0211.
DR KEGG; hpy:HP_0211; -.
DR PATRIC; fig|85962.47.peg.228; -.
DR eggNOG; COG0790; Bacteria.
DR OMA; THFEKAC; -.
DR PhylomeDB; O25001; -.
DR Proteomes; UP000000429; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; -; 1.
DR InterPro; IPR006597; Sel1-like.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF08238; Sel1; 4.
DR Pfam; PF13181; TPR_8; 1.
DR SMART; SM00671; SEL1; 6.
DR SMART; SM00028; TPR; 3.
PE 1: Evidence at protein level;
KW Antibiotic resistance; Disulfide bond; Hydrolase; Reference proteome;
KW Repeat; Secreted; Signal; TPR repeat.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..250
FT /note="Beta-lactamase HcpA"
FT /id="PRO_0000013194"
FT REPEAT 29..62
FT /note="TPR 1"
FT REPEAT 67..98
FT /note="TPR 2"
FT REPEAT 100..133
FT /note="TPR 3"
FT REPEAT 134..169
FT /note="TPR 4"
FT REPEAT 170..202
FT /note="TPR 5"
FT DISULFID 56..64
FT /evidence="ECO:0000269|PubMed:10748053"
FT DISULFID 92..100
FT /evidence="ECO:0000269|PubMed:10748053"
FT DISULFID 128..136
FT /evidence="ECO:0000269|PubMed:10748053"
FT DISULFID 164..172
FT /evidence="ECO:0000269|PubMed:10748053"
FT DISULFID 196..204
FT /evidence="ECO:0000269|PubMed:10748053"
FT DISULFID 232..240
FT /evidence="ECO:0000255"
FT VARIANT 4
FT /note="N -> S (in strain: ATCC 49503)"
FT VARIANT 9
FT /note="L -> F (in strain: ATCC 49503)"
FT VARIANT 11
FT /note="G -> W (in strain: ATCC 49503)"
FT VARIANT 17
FT /note="T -> A (in strain: ATCC 49503)"
FT VARIANT 91
FT /note="G -> S (in strain: ATCC 49503)"
FT VARIANT 194
FT /note="K -> Q (in strain: ATCC 49503)"
FT VARIANT 199
FT /note="K -> N (in strain: ATCC 49503)"
FT VARIANT 235
FT /note="S -> G (in strain: ATCC 49503)"
SQ SEQUENCE 250 AA; 27366 MW; A375FF12EB795355 CRC64;
MLGNVKKTLF GVLCLGTLCL RGLMAEPDAK ELVNLGIESA KKQDFAQAKT HFEKACELKN
GFGCVFLGAF YEEGKGVGKD LKKAIQFYTK GCELNDGYGC NLLGNLYYNG QGVSKDAKKA
SQYYSKACDL NHAEGCMVLG SLHHYGVGTP KDLRKALDLY EKACDLKDSP GCINAGYIYS
VTKNFKEAIV RYSKACELKD GRGCYNLGVM QYNAQGTAKD EKQAVENFKK GCKSSVKEAC
DALKELKIEL
