ID I9RVA7_HELPX Unreviewed; 355 AA.
AC I9RVA7;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 33.
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=HPHPH16_0546 {ECO:0000313|EMBL:EJB50376.1};
OS Helicobacter pylori Hp H-16.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=992038 {ECO:0000313|EMBL:EJB50376.1, ECO:0000313|Proteomes:UP000005509};
RN [1] {ECO:0000313|EMBL:EJB50376.1, ECO:0000313|Proteomes:UP000005509}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hp H-16 {ECO:0000313|EMBL:EJB50376.1,
RC ECO:0000313|Proteomes:UP000005509};
RX PubMed=23661595; DOI=10.1111/2049-632X.12045;
RA Blanchard T.G., Czinn S.J., Correa P., Nakazawa T., Keelan M.,
RA Morningstar L., Santana-Cruz I., Maroo A., McCracken C., Shefchek K.,
RA Daugherty S., Song Y., Fraser C.M., Fricke W.F.;
RT "Genome sequences of 65 Helicobacter pylori strains isolated from
RT asymptomatic individuals and patients with gastric cancer, peptic ulcer
RT disease, or gastritis.";
RL Pathog. Dis. 68:39-43(2013).
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}.
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:EJB50376.1}.
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DR EMBL; AKOF01000001; EJB50376.1; -; Genomic_DNA.
DR RefSeq; WP_001022034.1; NZ_AKOF01000001.1.
DR AlphaFoldDB; I9RVA7; -.
DR PATRIC; fig|992038.3.peg.529; -.
DR Proteomes; UP000005509; 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; 2.
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; 8.
DR Pfam; PF13181; TPR_8; 1.
DR SMART; SM00671; SEL1; 8.
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|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 355 AA; 39635 MW; 436B540F33C9FE63 CRC64;
MNIKILKILV GGLFFWGLNA HLWGKQDNSF LGIGERAYKS GNYSKAMSYF KKTCNDNVSE
GCTQLGIIYE NGQGTRIDYK KALEYYKTAC QADDREGCFG LGRLYDEGLG TTQNYQEAID
AYAKACVLKH PESCYNLGII YDRKIKGNAA QAVTYYQKSC NFDMAKGCYV LGTAYEKGFL
EVKQSNHKAV IYYLKACRLN EGQACRALGS LFENGDAGLD EDFEVAFDYL QKACALNNSG
GCASLGSMYM LGRYVKKDPQ KAFNYFKQAC DMGSAVSCSR MGFMYSQGDT VPKDLRKALD
NYERGCDMGD EVGCFALAGM YYNMKDKENA IMIYDKGCKL GMKQACENLT KLRGY
//