ID J0SUB4_HELPX Unreviewed; 183 AA.
AC J0SUB4;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 36.
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 ORFNames=HPHPP28B_0347 {ECO:0000313|EMBL:EJC39273.1};
OS Helicobacter pylori Hp P-28b.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=992114 {ECO:0000313|EMBL:EJC39273.1, ECO:0000313|Proteomes:UP000003138};
RN [1] {ECO:0000313|EMBL:EJC39273.1, ECO:0000313|Proteomes:UP000003138}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hp P-28b {ECO:0000313|EMBL:EJC39273.1,
RC ECO:0000313|Proteomes:UP000003138};
RA Blanchard T.G., Czinn S.J., McCracken C., Abolude K., Maroo A.,
RA Santana-Cruz I., Tallon L.J., Ficke F.W.F.;
RT "Genome sequence of Helicobacter pylori Hp P-28b.";
RL Submitted (MAY-2012) 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|RuleBase:RU366075}.
CC -!- SIMILARITY: Belongs to the hcp beta-lactamase family.
CC {ECO:0000256|ARBA:ARBA00008486, ECO:0000256|RuleBase:RU366075}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EJC39273.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AKQM01000003; EJC39273.1; -; Genomic_DNA.
DR AlphaFoldDB; J0SUB4; -.
DR PATRIC; fig|992114.3.peg.336; -.
DR Proteomes; UP000003138; Unassembled WGS sequence.
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 PANTHER; PTHR13891:SF1; CYTOCHROME C OXIDASE ASSEMBLY FACTOR 7; 1.
DR PANTHER; PTHR13891; UNCHARACTERIZED; 1.
DR Pfam; PF08238; Sel1; 5.
DR SMART; SM00671; SEL1; 4.
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|RuleBase:RU366075, ECO:0000313|EMBL:EJC39273.1};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|RuleBase:RU366075};
KW TPR repeat {ECO:0000256|ARBA:ARBA00022803}.
SQ SEQUENCE 183 AA; 19754 MW; F38487BCC4A5F6FC CRC64;
MVIILLWSRR RKNLIKAAQY ASKACDLNNG SGCGVLGFLY GSGKGVEKNL IKAAYFYSKA
CDLNNGGGCG NLGVLYQKGE VVEKDLTKAA YLYSKACELK DGLGCKDLGT LYYSGKGVEK
DLIKAAYFYS KACELKESFG CGALAVLYIN GQGVEKNLTK ADQYISKACK LGDQEACEAL
KEK
//