ID   BLKPC_KLEOX             Reviewed;         293 AA.
AC   Q848S6;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Carbapenem-hydrolyzing beta-lactamase KPC;
DE            EC=3.5.2.6;
DE   AltName: Full=Carbapenem-hydrolyzing beta-lactamase KPC-2;
DE   Flags: Precursor;
GN   Name=bla; Synonyms=kpc, kpc2;
OS   Klebsiella oxytoca.
OG   Plasmid conjugative 70kb.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=571;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBSTRATES, AND ACTIVITY REGULATION.
RC   STRAIN=3127;
RX   PubMed=14638498; DOI=10.1128/aac.47.12.3881-3889.2003;
RA   Yigit H., Queenan A.M., Rasheed J.K., Biddle J.W., Domenech-Sanchez A.,
RA   Alberti S., Bush K., Tenover F.C.;
RT   "Carbapenem-resistant strain of Klebsiella oxytoca harboring carbapenem-
RT   hydrolyzing beta-lactamase KPC-2.";
RL   Antimicrob. Agents Chemother. 47:3881-3889(2003).
CC   -!- FUNCTION: Hydrolyzes carbapenems, penicillins, cephalosporins and
CC       aztreonam with varying efficiency.
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   -!- ACTIVITY REGULATION: Not inhibited by EDTA, inhibited by clavulanic
CC       acid and tazobactam. {ECO:0000269|PubMed:14638498}.
CC   -!- MISCELLANEOUS: Initially two different KPC beta-lactamases were
CC       identified from two different bacteria (KPC-1 and KPC-2); they were
CC       later shown to be identical.
CC   -!- SIMILARITY: Belongs to the class-A beta-lactamase family.
CC       {ECO:0000305}.
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DR   EMBL; AY210886; AAO53443.1; -; Genomic_DNA.
DR   RefSeq; WP_004199234.1; NZ_PQKQ01000039.1.
DR   PDB; 5MGI; X-ray; 1.50 A; A=26-289.
DR   PDBsum; 5MGI; -.
DR   AlphaFoldDB; Q848S6; -.
DR   SMR; Q848S6; -.
DR   ChEMBL; CHEMBL3562180; -.
DR   GeneID; 67375509; -.
DR   OrthoDB; 991474at2; -.
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; Hydrolase; Plasmid; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..293
FT                   /note="Carbapenem-hydrolyzing beta-lactamase KPC"
FT                   /id="PRO_0000349144"
FT   ACT_SITE        69
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        167
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         233..235
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   TURN            28..30
FT                   /evidence="ECO:0007829|PDB:5MGI"
FT   HELIX           31..40
FT                   /evidence="ECO:0007829|PDB:5MGI"
FT   STRAND          42..50
FT                   /evidence="ECO:0007829|PDB:5MGI"
FT   TURN            51..53
FT                   /evidence="ECO:0007829|PDB:5MGI"
FT   STRAND          56..60
FT                   /evidence="ECO:0007829|PDB:5MGI"
FT   HELIX           68..70
FT                   /evidence="ECO:0007829|PDB:5MGI"
FT   HELIX           71..83
FT                   /evidence="ECO:0007829|PDB:5MGI"
FT   HELIX           98..100
FT                   /evidence="ECO:0007829|PDB:5MGI"
FT   HELIX           106..110
FT                   /evidence="ECO:0007829|PDB:5MGI"
FT   TURN            111..114
FT                   /evidence="ECO:0007829|PDB:5MGI"
FT   HELIX           118..127
FT                   /evidence="ECO:0007829|PDB:5MGI"
FT   HELIX           131..140
FT                   /evidence="ECO:0007829|PDB:5MGI"
FT   HELIX           143..153
FT                   /evidence="ECO:0007829|PDB:5MGI"
FT   HELIX           167..169
FT                   /evidence="ECO:0007829|PDB:5MGI"
FT   HELIX           182..193
FT                   /evidence="ECO:0007829|PDB:5MGI"
FT   STRAND          195..198
FT                   /evidence="ECO:0007829|PDB:5MGI"
FT   HELIX           200..211
FT                   /evidence="ECO:0007829|PDB:5MGI"
FT   TURN            217..219
FT                   /evidence="ECO:0007829|PDB:5MGI"
FT   HELIX           220..223
FT                   /evidence="ECO:0007829|PDB:5MGI"
FT   STRAND          228..236
FT                   /evidence="ECO:0007829|PDB:5MGI"
FT   HELIX           239..241
FT                   /evidence="ECO:0007829|PDB:5MGI"
FT   STRAND          243..250
FT                   /evidence="ECO:0007829|PDB:5MGI"
FT   STRAND          257..264
FT                   /evidence="ECO:0007829|PDB:5MGI"
FT   HELIX           274..287
FT                   /evidence="ECO:0007829|PDB:5MGI"
SQ   SEQUENCE   293 AA;  31115 MW;  13EB2FC28005EE5F CRC64;
     MSLYRRLVLL SCLSWPLAGF SATALTNLVA EPFAKLEQDF GGSIGVYAMD TGSGATVSYR
     AEERFPLCSS FKGFLAAAVL ARSQQQAGLL DTPIRYGKNA LVPWSPISEK YLTTGMTVAE
     LSAAAVQYSD NAAANLLLKE LGGPAGLTAF MRSIGDTTFR LDRWELELNS AIPGDARDTS
     SPRAVTESLQ KLTLGSALAA PQRQQFVDWL KGNTTGNHRI RAAVPADWAV GDKTGTCGVY
     GTANDYAVVW PTGRAPIVLA VYTRAPNKDD KHSEAVIAAA ARLALEGLGV NGQ