ID B1PZ94_9GAMM Unreviewed; 382 AA.
AC B1PZ94;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=Beta-lactamase {ECO:0000256|ARBA:ARBA00018879, ECO:0000256|RuleBase:RU361140};
DE EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865, ECO:0000256|RuleBase:RU361140};
GN Name=blaMOX-3 {ECO:0000313|EMBL:ACA30419.1};
OS Aeromonas sp. HCUZ 2422275.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Aeromonas.
OX NCBI_TaxID=505724 {ECO:0000313|EMBL:ACA30419.1};
RN [1] {ECO:0000313|EMBL:ACA30419.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HCUZ 2422275 {ECO:0000313|EMBL:ACA30419.1};
RA Miro E., Castillo F.J., Seral C., Arias A., Mirelis B., Navarro F.;
RT "MOX-3, A New AmpC type in Aeromonas sp.";
RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
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|RuleBase:RU361140};
CC -!- SIMILARITY: Belongs to the class-C beta-lactamase family.
CC {ECO:0000256|ARBA:ARBA00007840, ECO:0000256|RuleBase:RU361140}.
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DR EMBL; EU515248; ACA30419.1; -; Genomic_DNA.
DR RefSeq; WP_063860846.1; NG_049316.1.
DR AlphaFoldDB; B1PZ94; -.
DR MEROPS; S12.006; -.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR GO; GO:0008800; F:beta-lactamase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0017001; P:antibiotic catabolic process; IEA:InterPro.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR InterPro; IPR001466; Beta-lactam-related.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR001586; Beta-lactam_class-C_AS.
DR PANTHER; PTHR46825:SF8; BETA-LACTAMASE-RELATED; 1.
DR PANTHER; PTHR46825; D-ALANYL-D-ALANINE-CARBOXYPEPTIDASE/ENDOPEPTIDASE AMPH; 1.
DR Pfam; PF00144; Beta-lactamase; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR PROSITE; PS00336; BETA_LACTAMASE_C; 1.
PE 3: Inferred from homology;
KW Antibiotic resistance {ECO:0000256|RuleBase:RU361140};
KW Hydrolase {ECO:0000256|RuleBase:RU361140};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..382
FT /note="Beta-lactamase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002769957"
FT DOMAIN 36..378
FT /note="Beta-lactamase-related"
FT /evidence="ECO:0000259|Pfam:PF00144"
SQ SEQUENCE 382 AA; 41094 MW; 6631127425C8EF1E CRC64;
MQQRQSILWG AVATLMWAGL AHAGETSPVD PLRPVVDASI QPLLKEHRIP GMAVAVLKDG
KAHYFNYGVA DRERAVGVSE QTLFEIGSVS KPLTATLGAY AVVKGAMQLD DKASRHAPWL
KGSAFDSITM GELATYSAGG LPLQFPEEVD SLEKMQAYYR QWTPAYSPGS HRQYSNPSIG
LFGHLAASSL KQPFAQLMEQ TLLPGLGLHH TYVNVPKQAM ASYAYGYSKE DKPIRVSPGM
LADEAYGIKT SSADLLRFVK ANISGVDDKA LQQAISLTHK GHYSVGGMTQ GLGWERYAYP
VSEQTLLAGN SAKVILEANP TAAPRESGSQ MLFNKTGSTS GFGAYVAFVP AKGIGIVMLA
NRNYPIPARV KAAHAILTQL AR
//
