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Database: UniProt
Entry: Q8KXZ7_HELPX
LinkDB: Q8KXZ7_HELPX
Original site: Q8KXZ7_HELPX 
ID   Q8KXZ7_HELPX            Unreviewed;       325 AA.
AC   Q8KXZ7;
DT   01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2002, sequence version 1.
DT   24-JAN-2024, entry version 62.
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};
OS   Helicobacter pylori (Campylobacter pylori).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=210 {ECO:0000313|EMBL:AAM66150.1};
RN   [1] {ECO:0000313|EMBL:AAM66150.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CR14 {ECO:0000313|EMBL:AAM66150.1};
RX   PubMed=12427957;
RA   Chanto G., Occhialini A., Gras N., Alm R.A., Megraud F., Marais A.;
RT   "Identification of strain-specific genes located outside the plasticity
RT   zone in nine clinical isolates of Helicobacter pylori.";
RL   Microbiology 148:3671-3680(2002).
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|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; AF326629; AAM66150.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8KXZ7; -.
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; 2.
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; 7.
DR   SMART; SM00671; SEL1; 6.
DR   SUPFAM; SSF81901; HCP-like; 2.
PE   3: Inferred from homology;
KW   Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Hydrolase {ECO:0000256|RuleBase:RU366075};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Secreted {ECO:0000256|RuleBase:RU366075};
KW   Signal {ECO:0000256|RuleBase:RU366075};
KW   TPR repeat {ECO:0000256|ARBA:ARBA00022803}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|RuleBase:RU366075"
FT   CHAIN           27..325
FT                   /note="Beta-lactamase"
FT                   /evidence="ECO:0000256|RuleBase:RU366075"
FT                   /id="PRO_5036515743"
SQ   SEQUENCE   325 AA;  36018 MW;  32FA8B85083F9619 CRC64;
     MLGSVKKAVF RVLCLGALCL CGGLMAEQDP KELILSGITI YTDKNFTRAK KYFEKACKSN
     DADGCAILRE AYSKAIAREN ARESIEKALE HTATAKACKS NDAEKCRDLA EFYFNVNDLK
     NALEYYSKSC KLNNVEGCML SATFYNDMIK GLKKDKKDLE YYSKACELNY GDGCAILGDI
     YHNGEGVAKD LKKAFQYYSK ACELNNGEGY SKLGGAYFFG EGVTQDLKKA FGYYSKACKL
     NEALTCTLVG EFYRDGEGVA KDLKKAFEYS AKACELNDAK GCYALAAFFN EAKGVARGEK
     QTTENLEKSC KLGLKETCDI FKEQK
//
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