ID   BLA2_STEMA              Reviewed;         303 AA.
AC   P96465;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Beta-lactamase L2;
DE            EC=3.5.2.6;
DE   AltName: Full=Penicillinase;
DE   Flags: Precursor;
OS   Stenotrophomonas maltophilia (Pseudomonas maltophilia) (Xanthomonas
OS   maltophilia).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=40324;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=IID 1275;
RX   PubMed=9210666; DOI=10.1128/aac.41.7.1460;
RA   Walsh T.R., Macgowan A.P., Bennett P.M.;
RT   "Sequence analysis and enzyme kinetics of the L2 serine beta-lactamase from
RT   Stenotrophomonas maltophilia.";
RL   Antimicrob. Agents Chemother. 41:1460-1464(1997).
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   -!- PTM: Predicted to be exported by the Tat system. The position of the
CC       signal peptide cleavage has not been experimentally proven.
CC   -!- SIMILARITY: Belongs to the class-A beta-lactamase family.
CC       {ECO:0000305}.
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DR   EMBL; Y08562; CAA69869.1; -; Genomic_DNA.
DR   AlphaFoldDB; P96465; -.
DR   SMR; P96465; -.
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; -; 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   InterPro; IPR006311; TAT_signal.
DR   PANTHER; PTHR35333; PTHR35333; 1.
DR   Pfam; PF13354; Beta-lactamase2; 1.
DR   PRINTS; PR00118; BLACTAMASEA.
DR   SUPFAM; SSF56601; SSF56601; 1.
DR   PROSITE; PS00146; BETA_LACTAMASE_A; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
KW   Antibiotic resistance; Hydrolase; Signal.
FT   SIGNAL          1..35
FT                   /note="Tat-type signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT   CHAIN           36..303
FT                   /note="Beta-lactamase L2"
FT                   /id="PRO_0000017021"
FT   ACT_SITE        83
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10101"
FT   BINDING         247..249
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   303 AA;  32208 MW;  C278DAF4C824FD3C CRC64;
     MLARRRFLQF SGAAVASSLA LPLLARAAGK TAASAPTDAA LTAATDFAAL EKAVRGRFGV
     TLLDTASGRR IGHRQDERFP MCSTFKSVLA ATVLSQAERQ PALLDTRVPV RDADLLSHAP
     VTRRHAGKDM TVRDLCRATI ITSDNTAANL LFGVVGGPPA VTAFLRSIGD AVSRTDRLEP
     ELNSFAKGDP RDTTTPAAMA ATLQRVVLGE VLQLASRQQL ADWLIDNETG DACLRAGLGK
     LWRVRDKTGS NGEDARNDIA VLWPVAGGAP WVLTAYLQAG AISYEQRATV LAQVGRIADR
     LIG