ID   BLAN_SERMA              Reviewed;         294 AA.
AC   P52682;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Carbapenem-hydrolyzing beta-lactamase Sme-1;
DE            EC=3.5.2.6;
DE   Flags: Precursor;
GN   Name=smeA; Synonyms=bpl-1, bplA;
OS   Serratia marcescens.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 28-38.
RC   STRAIN=S6;
RX   PubMed=8092824; DOI=10.1128/aac.38.6.1262;
RA   Naas T., Vandel L., Sougakoff W., Livermore D.M., Nordmann P.;
RT   "Cloning and sequence analysis of the gene for a carbapenem-hydrolyzing
RT   class A beta-lactamase, Sme-1, from Serratia marcescens S6.";
RL   Antimicrob. Agents Chemother. 38:1262-1270(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-32.
RC   STRAIN=S6;
RX   PubMed=7793864; DOI=10.1128/aac.39.3.629;
RA   Naas T., Livermore D.M., Nordmann P.;
RT   "Characterization of an LysR family protein, SmeR from Serratia marcescens
RT   S6, its effect on expression of the carbapenem-hydrolyzing beta-lactamase
RT   Sme-1, and comparison of this regulator with other beta-lactamase
RT   regulators.";
RL   Antimicrob. Agents Chemother. 39:629-637(1995).
CC   -!- FUNCTION: Can hydrolyze carbapenem compounds.
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   -!- SIMILARITY: Belongs to the class-A beta-lactamase family.
CC       {ECO:0000305}.
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DR   EMBL; Z28968; CAA82281.1; -; Genomic_DNA.
DR   EMBL; Z30237; CAA82944.1; -; Genomic_DNA.
DR   PIR; S44080; S44080.
DR   RefSeq; WP_063864724.1; NG_050134.1.
DR   AlphaFoldDB; P52682; -.
DR   SMR; P52682; -.
DR   KEGG; ag:CAA82281; -.
DR   SABIO-RK; P52682; -.
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   PANTHER; PTHR35333; PTHR35333; 1.
DR   Pfam; PF13354; Beta-lactamase2; 1.
DR   PRINTS; PR00118; BLACTAMASEA.
DR   SUPFAM; SSF56601; SSF56601; 1.
PE   1: Evidence at protein level;
KW   Antibiotic resistance; Direct protein sequencing; Hydrolase; Signal.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000269|PubMed:8092824"
FT   CHAIN           28..294
FT                   /note="Carbapenem-hydrolyzing beta-lactamase Sme-1"
FT                   /id="PRO_0000017001"
FT   ACT_SITE        73
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        172
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         238..240
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   294 AA;  32197 MW;  C33AAD6AA2293094 CRC64;
     MSNKVNFKTA SFLFSVCLAL SAFNAHANKS DAAAKQIKKL EEDFDGRIGV FAIDTGSGNT
     FGYRSDERFP LCSSFKGFLA AAVLERVQQK KLDINQKVKY ESRDLEYHSP ITTKYKGSGM
     TLGDMASAAL QYSDNGATNI IMERFLGGPE GMTKFMRSIG DNEFRLDRWE LELNTAIPGD
     KRDTSTPKAV ANSLNKLALG NVLNAKVKAI YQNWLKGNTT GDARIRASVP ADWVVGDKTG
     SCGAIGTAND YAVIWPKNRA PLIVSIYTTR KSKDDKHSDK TIAEASRIAI QAID