ID   A5JG64_HELPX            Unreviewed;       250 AA.
AC   A5JG64;
DT   26-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2007, sequence version 1.
DT   13-SEP-2023, entry version 44.
DE   RecName: Full=Beta-lactamase {ECO:0000256|ARBA:ARBA00012865, ECO:0000256|RuleBase:RU366075};
DE            EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865, ECO:0000256|RuleBase:RU366075};
GN   Name=hcpA {ECO:0000313|EMBL:ABQ45680.1};
OS   Helicobacter pylori (Campylobacter pylori).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=210 {ECO:0000313|EMBL:ABQ45680.1};
RN   [1] {ECO:0000313|EMBL:ABQ45680.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=K8 {ECO:0000313|EMBL:ABQ45680.1};
RA   Perez C., Ogura M., Berg D., Kalia A.;
RL   Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ABQ45680.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=K8 {ECO:0000313|EMBL:ABQ45680.1};
RA   Ogura M., Dailide G., Dailidiene D., Secka O., Ito Y., Lee H.-K., Tan S.,
RA   Berg D., Kalia A.;
RT   "Geographic subdivision facilitates local adaptations in H. pylori
RT   populations.";
RL   Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Hydrolyzes 6-aminopenicillinic acid and 7-
CC       aminocephalosporanic acid (ACA) derivatives.
CC       {ECO:0000256|RuleBase:RU366075}.
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:0000256|ARBA:ARBA00001526,
CC         ECO:0000256|RuleBase:RU366075};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613,
CC       ECO:0000256|RuleBase:RU366075}.
CC   -!- SIMILARITY: Belongs to the hcp beta-lactamase family.
CC       {ECO:0000256|ARBA:ARBA00008486, ECO:0000256|RuleBase:RU366075}.
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DR   EMBL; EF372760; ABQ45680.1; -; Genomic_DNA.
DR   AlphaFoldDB; A5JG64; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008800; F:beta-lactamase activity; IEA:UniProtKB-UniRule.
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; 6.
DR   SMART; SM00671; SEL1; 5.
DR   SMART; SM00028; TPR; 2.
DR   SUPFAM; SSF81901; HCP-like; 1.
PE   3: Inferred from homology;
KW   Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU366075};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|RuleBase:RU366075};
KW   TPR repeat {ECO:0000256|ARBA:ARBA00022803}.
SQ   SEQUENCE   250 AA;  27493 MW;  D3E6A03E8DC289B9 CRC64;
     MLGSVKKTLF GVLCLGALCL RELMAEPNAK EFVNLGIEST KKQDFTQAKT HFEKACELKD
     GFGCVFLGAF YEEGKGVGKD LKKAIQFYTK GCELNDGYGC RLLGNLYYNG QGVSKDAKKA
     SQYYSKSCEL NHAEGCMVLG SLYHHGLGTP KDSRKALDLY EKACDLKDSP GCINAGYMYG
     VAKNFKEAIV RYSKACELKD GRGCYNLGVM QYNAQGTAKD EKQAVENFKK GCKSSVKEAC
     DALKELKIEL
//