ID A5JGA0_HELPX Unreviewed; 320 AA.
AC A5JGA0;
DT 26-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2007, sequence version 1.
DT 24-JAN-2024, entry version 42.
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 Name=hcpE {ECO:0000313|EMBL:ABQ45716.1};
OS Helicobacter pylori (Campylobacter pylori).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=210 {ECO:0000313|EMBL:ABQ45716.1};
RN [1] {ECO:0000313|EMBL:ABQ45716.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=K42 {ECO:0000313|EMBL:ABQ45716.1};
RA Perez C., Ogura M., Berg D., Kalia A.;
RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABQ45716.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=K42 {ECO:0000313|EMBL:ABQ45716.1};
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; EF372796; ABQ45716.1; -; Genomic_DNA.
DR AlphaFoldDB; A5JGA0; -.
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; 8.
DR SMART; SM00671; SEL1; 7.
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 TPR repeat {ECO:0000256|ARBA:ARBA00022803}.
FT NON_TER 320
FT /evidence="ECO:0000313|EMBL:ABQ45716.1"
SQ SEQUENCE 320 AA; 35285 MW; 501425CBA360995B CRC64;
MSVKILKILV CGLFFLNAHL WGKQDNSFLG VAERAYKSGN YSKAASYFKK ACNDGVSEGC
TQLGIIYENG QGTRIDYKKA LEYYQSACQA DDREGCFGLG GLYDEGLGTT QNYQEAIDAY
AKACVLKHPE SCYNLGIIYD RKIKGNAAQA VTYYQKSCNF DMAKGCYVLG VAYEKGFLEV
QQSNHKAVIY YLKACRLDDG QACRALGSLF ENGDAGLDED FEVAFDYLQK ACALNNSGGC
ASLGSMYMLG RYVKKDPQKA FNFFKQACDM GSAVSCSRMG FMYSQGDAVP KDLRKALDNY
ERGCDMGDEV GCFALAGMYY
//
