ID A5JGE6_HELPX Unreviewed; 267 AA.
AC A5JGE6;
DT 26-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2007, sequence version 1.
DT 24-JAN-2024, entry version 46.
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};
DE Flags: Fragment;
GN ORFNames=hp0628 {ECO:0000313|EMBL:ABQ45762.1};
OS Helicobacter pylori (Campylobacter pylori).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=210 {ECO:0000313|EMBL:ABQ45762.1};
RN [1] {ECO:0000313|EMBL:ABQ45762.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JF55 {ECO:0000313|EMBL:ABQ45762.1};
RA Perez C., Ogura M., Berg D., Kalia A.;
RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABQ45762.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JF55 {ECO:0000313|EMBL:ABQ45762.1};
RA Ogura M., Dailide G., Dailidiene D., Secka O., Ito Y., Lee H.-K., Tan S.,
RA Berg D., Kalia A.;
RT "Geographic subdivision facilitates local adaptations in H. pylori
RT populations.";
RL Submitted (MAY-2007) 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}.
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DR EMBL; EF372843; ABQ45762.1; -; Genomic_DNA.
DR AlphaFoldDB; A5JGE6; -.
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};
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..19
FT /evidence="ECO:0000256|RuleBase:RU366075"
FT CHAIN 20..267
FT /note="Beta-lactamase"
FT /evidence="ECO:0000256|RuleBase:RU366075"
FT /id="PRO_5036515751"
FT REGION 22..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..62
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 267
FT /evidence="ECO:0000313|EMBL:ABQ45762.1"
SQ SEQUENCE 267 AA; 28421 MW; B2D7E5531CB40FD5 CRC64;
MLKKSLLLLV FLVLQLSGAE ENNQAPKNTP PELNPANAKG APNPNTQITP KNDNSNLLDK
LGSPENAQTE LSAGIDLAKK GDYQGAFKLF SQSCDNGNAA GCFALGAMYA NGVGIQTNRL
KAARYYEMGC SGGDATACAN LAQMYENKKN ADTNDKENAL QLYAVACQGG DMLACNNLGW
MFANGSGVPK DYYKAMGYYK FSCDNGNDMG CYNLGLMSNV NNIYGIDKAK LSQVDLNYLA
CNAGDMMGCA NLGWIYANGD LGAPLNN
//