ID   BLA1_AERHY              Reviewed;         304 AA.
AC   Q44056;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 2.
DT   27-MAR-2024, entry version 79.
DE   RecName: Full=Beta-lactamase AER-1;
DE            EC=3.5.2.6;
DE   AltName: Full=Penicillinase;
DE   Flags: Precursor;
GN   Name=aer1;
OS   Aeromonas hydrophila.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=644;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=VL7711; TRANSPOSON=Omega7711;
RX   PubMed=9687391; DOI=10.1128/aac.42.8.1966;
RA   Sanschagrin F., Bejaoui N., Levesque R.C.;
RT   "Structure of CARB-4 and AER-1 carbenicillin-hydrolyzing beta-lactamases.";
RL   Antimicrob. Agents Chemother. 42:1966-1972(1998).
CC   -!- FUNCTION: Hydrolyzes carbenicillin. Methicillin and oxacillin are
CC       weakly hydrolyzed.
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; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU10101};
CC   -!- SIMILARITY: Belongs to the class-A beta-lactamase family.
CC       {ECO:0000305}.
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DR   EMBL; U14748; AAC09015.1; -; Genomic_DNA.
DR   RefSeq; WP_063857819.1; NG_048688.1.
DR   AlphaFoldDB; Q44056; -.
DR   SMR; Q44056; -.
DR   KEGG; ag:AAC09015; -.
DR   GO; GO:0008800; F:beta-lactamase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030655; P:beta-lactam antibiotic catabolic process; IEA:InterPro.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR045155; Beta-lactam_cat.
DR   InterPro; IPR000871; Beta-lactam_class-A.
DR   InterPro; IPR023650; Beta-lactam_class-A_AS.
DR   PANTHER; PTHR35333; BETA-LACTAMASE; 1.
DR   PANTHER; PTHR35333:SF3; BETA-LACTAMASE2 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF13354; Beta-lactamase2; 1.
DR   PRINTS; PR00118; BLACTAMASEA.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR   PROSITE; PS00146; BETA_LACTAMASE_A; 1.
PE   3: Inferred from homology;
KW   Antibiotic resistance; Disulfide bond; Hydrolase; Signal;
KW   Transposable element.
FT   SIGNAL          1..37
FT                   /evidence="ECO:0000255"
FT   CHAIN           38..304
FT                   /note="Beta-lactamase AER-1"
FT                   /id="PRO_0000017048"
FT   REGION          173..195
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        173..187
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        83
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10101"
FT   BINDING         248..250
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   DISULFID        90..137
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   304 AA;  32428 MW;  66AD56ED45D02A41 CRC64;
     MYVLSVEKPT LRNKFAAGIG VVLVCVVASF IPTPVFALDT TKLIQAVQSE ESALHARVGM
     TVFDSNTGTT WNYRGDERFP LNSTHKTFSC AALLAKVDGK SLSLGQSVSI SKEMLVTYSP
     ITEKSLSPET VTFGKICQAA VSYSDNTAAN VVFDAIGGAT GFNAYMRSIG DEETQLDRKE
     PELNEGTPGD VRDTTTPNAM VNSLRKILLG DALSASSRSQ LTQWMLDDQV AGALLRASLP
     SDWKIADKTG AGGYGSRSIV AVIWPPSKQP LVVGIYITQT KASMQASNQA IARIGVVLKD
     TVAP
//