ID M3LZI7_HELPX Unreviewed; 114 AA.
AC M3LZI7;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=HMPREF1399_00667 {ECO:0000313|EMBL:EMG93677.1};
OS Helicobacter pylori GAM118Bi.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1159027 {ECO:0000313|EMBL:EMG93677.1, ECO:0000313|Proteomes:UP000011879};
RN [1] {ECO:0000313|EMBL:EMG93677.1, ECO:0000313|Proteomes:UP000011879}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GAM118Bi {ECO:0000313|EMBL:EMG93677.1,
RC ECO:0000313|Proteomes:UP000011879};
RA Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., Courtney L.,
RA Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., Miner T., Farmer C.,
RA Delehaunty K., Cordes M., Minx P., Tomlinson C., Chen J., Wollam A.,
RA Pepin K.H., Bhonagiri V., Zhang X., Suruliraj S., Antonio M., Secka O.,
RA Thomas J., Warren W., Mitreva M., Mardis E.R., Wilson R.K.;
RL Submitted (NOV-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:EMG93677.1}.
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DR EMBL; APDD01000048; EMG93677.1; -; Genomic_DNA.
DR AlphaFoldDB; M3LZI7; -.
DR HOGENOM; CLU_000288_36_12_7; -.
DR Proteomes; UP000011879; 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; 3.
DR SMART; SM00671; SEL1; 3.
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 TPR repeat {ECO:0000256|ARBA:ARBA00022803}.
FT NON_TER 114
FT /evidence="ECO:0000313|EMBL:EMG93677.1"
SQ SEQUENCE 114 AA; 12606 MW; 56266A39BDE5CF62 CRC64;
MAEPNAKELV DLGRNSYSKQ DFTQAKKYFE KACELKDGVG CFNLGVLYDN GHRVGKDLKK
VARLYFKACE LNDGSGCFNA GNIYRRGDGV AKNFKEALAR YSKACELENG GGCF
//
