ID   BLAN_ENTCL              Reviewed;         292 AA.
AC   P52663;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Imipenem-hydrolyzing beta-lactamase;
DE            EC=3.5.2.6;
DE   AltName: Full=Carbapenemase;
DE   AltName: Full=NMC-A;
DE   Flags: Precursor;
GN   Name=nmcA;
OS   Enterobacter cloacae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Enterobacter; Enterobacter cloacae complex.
OX   NCBI_TaxID=550;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 28-34.
RC   STRAIN=NOR-1;
RX   PubMed=8052644; DOI=10.1073/pnas.91.16.7693;
RA   Naas T., Nordmann P.;
RT   "Analysis of a carbapenem-hydrolyzing class A beta-lactamase from
RT   Enterobacter cloacae and of its LysR-type regulatory protein.";
RL   Proc. Natl. Acad. Sci. U.S.A. 91:7693-7697(1994).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS).
RC   STRAIN=NOR-1;
RX   PubMed=10464248; DOI=10.1074/jbc.274.36.25260;
RA   Mourey L., Kotra L.P., Bellettini J., Bulychev A., O'Brien M., Miller M.J.,
RA   Mobashery S., Samama J.-P.;
RT   "Inhibition of the broad spectrum nonmetallocarbapenamase of class A (NMC-
RT   A) beta-lactamase from Enterobacter cloacae by monocyclic beta-lactams.";
RL   J. Biol. Chem. 274:25260-25265(1999).
CC   -!- FUNCTION: Hydrolyzes carbapenems such as imipenem, which are extended-
CC       spectrum beta-lactam antibiotics.
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; Z21956; CAA79967.1; -; Genomic_DNA.
DR   PIR; S35915; S35915.
DR   RefSeq; WP_050737109.1; NG_049342.1.
DR   PDB; 1BUE; X-ray; 1.64 A; A=28-292.
DR   PDB; 1BUL; X-ray; 1.89 A; A=28-292.
DR   PDBsum; 1BUE; -.
DR   PDBsum; 1BUL; -.
DR   AlphaFoldDB; P52663; -.
DR   SMR; P52663; -.
DR   BindingDB; P52663; -.
DR   ChEMBL; CHEMBL4314; -.
DR   ABCD; P52663; 1 sequenced antibody.
DR   SABIO-RK; P52663; -.
DR   EvolutionaryTrace; P52663; -.
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   3D-structure; Antibiotic resistance; Direct protein sequencing;
KW   Disulfide bond; Hydrolase; Signal.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000269|PubMed:8052644"
FT   CHAIN           28..292
FT                   /note="Imipenem-hydrolyzing beta-lactamase"
FT                   /id="PRO_0000017000"
FT   ACT_SITE        71
FT                   /note="Acyl-ester intermediate"
FT   BINDING         236..238
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   DISULFID        70..240
FT   HELIX           32..42
FT                   /evidence="ECO:0007829|PDB:1BUE"
FT   STRAND          44..52
FT                   /evidence="ECO:0007829|PDB:1BUE"
FT   TURN            53..55
FT                   /evidence="ECO:0007829|PDB:1BUE"
FT   STRAND          58..62
FT                   /evidence="ECO:0007829|PDB:1BUE"
FT   HELIX           70..73
FT                   /evidence="ECO:0007829|PDB:1BUE"
FT   HELIX           74..86
FT                   /evidence="ECO:0007829|PDB:1BUE"
FT   HELIX           108..112
FT                   /evidence="ECO:0007829|PDB:1BUE"
FT   TURN            113..116
FT                   /evidence="ECO:0007829|PDB:1BUE"
FT   HELIX           120..129
FT                   /evidence="ECO:0007829|PDB:1BUE"
FT   HELIX           133..142
FT                   /evidence="ECO:0007829|PDB:1BUE"
FT   HELIX           146..156
FT                   /evidence="ECO:0007829|PDB:1BUE"
FT   HELIX           170..172
FT                   /evidence="ECO:0007829|PDB:1BUE"
FT   HELIX           185..197
FT                   /evidence="ECO:0007829|PDB:1BUE"
FT   STRAND          198..201
FT                   /evidence="ECO:0007829|PDB:1BUE"
FT   HELIX           203..214
FT                   /evidence="ECO:0007829|PDB:1BUE"
FT   TURN            220..222
FT                   /evidence="ECO:0007829|PDB:1BUE"
FT   HELIX           223..226
FT                   /evidence="ECO:0007829|PDB:1BUE"
FT   STRAND          231..239
FT                   /evidence="ECO:0007829|PDB:1BUE"
FT   STRAND          246..253
FT                   /evidence="ECO:0007829|PDB:1BUE"
FT   STRAND          260..267
FT                   /evidence="ECO:0007829|PDB:1BUE"
FT   HELIX           277..289
FT                   /evidence="ECO:0007829|PDB:1BUE"
SQ   SEQUENCE   292 AA;  32075 MW;  4D33FD8669998F1B CRC64;
     MSLNVKQSRI AILFSSCLIS ISFFSQANTK GIDEIKNLET DFNGRIGVYA LDTGSGKSFS
     YRANERFPLC SSFKGFLAAA VLKGSQDNRL NLNQIVNYNT RSLEFHSPIT TKYKDNGMSL
     GDMAAAALQY SDNGATNIIL ERYIGGPEGM TKFMRSIGDE DFRLDRWELD LNTAIPGDER
     DTSTPAAVAK SLKTLALGNI LSEHEKETYQ TWLKGNTTGA ARIRASVPSD WVVGDKTGSC
     GAYGTANDYA VVWPKNRAPL IISVYTTKNE KEAKHEDKVI AEASRIAIDN LK