ID V5NP48_HELPX Unreviewed; 306 AA.
AC V5NP48;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 24-JAN-2024, entry version 30.
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=U064_0500 {ECO:0000313|EMBL:AHA89432.1};
OS Helicobacter pylori BM012S.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1407463 {ECO:0000313|EMBL:AHA89432.1, ECO:0000313|Proteomes:UP000018543};
RN [1] {ECO:0000313|EMBL:AHA89432.1, ECO:0000313|Proteomes:UP000018543}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BM012S {ECO:0000313|EMBL:AHA89432.1,
RC ECO:0000313|Proteomes:UP000018543};
RX DOI=10.1371/journal.pone.0082187;
RA Linz B., Windsor H.M., Gajewski J.P., Hake C.M., Drautz D.I.,
RA Schuster S.C., Marshall B.J.;
RT "Helicobacter pylori genomic microevolution during naturally occurring
RT transmission between adults.";
RL PLoS ONE 8:E82187-E82187(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|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; CP006889; AHA89432.1; -; Genomic_DNA.
DR RefSeq; WP_023591824.1; NC_022911.1.
DR AlphaFoldDB; V5NP48; -.
DR KEGG; hez:U064_0500; -.
DR PATRIC; fig|1407463.3.peg.511; -.
DR HOGENOM; CLU_000288_36_2_7; -.
DR Proteomes; UP000018543; Chromosome.
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; 7.
DR SMART; SM00671; SEL1; 7.
DR SUPFAM; SSF81901; HCP-like; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|RuleBase:RU366075};
KW TPR repeat {ECO:0000256|ARBA:ARBA00022803}.
SQ SEQUENCE 306 AA; 33984 MW; E821E03A50788231 CRC64;
MIKSWTKKWF LILFLMASCF SYLVATTGEK YFKMAAQALK RGDYHKAVAF YKRSCNLRVG
VGCTSLGSMY EDGDGVDQNI PKAVFYYRRG CNLRNYLACA SLGSMYEDGD SVQKDLPKAL
YYYRRGCHLK GGVSCGSLGF MYFNGTGVKQ NYAKALSLSK YACSLNYGIS CNFAGYMYRN
AKGVQKDLKK ALANFKRGCH LKDGASCVNL GYMYEVGMDV KQNGEQALNL YKKGCFLKEG
SGCHNVAVMY YTGKGAPKDL DKAISYYKKG CTLGFSGSCK VLEEVIGKKS DDLQDDAQND
TQDDTQ
//
