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
//