BLKPC_KLEPN
ID BLKPC_KLEPN Reviewed; 293 AA.
AC Q9F663;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 2.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Carbapenem-hydrolyzing beta-lactamase KPC;
DE EC=3.5.2.6;
DE AltName: Full=Carbapenem-hydrolyzing beta-lactamase KPC-1;
DE Flags: Precursor;
GN Name=bla; Synonyms=kpc, kpc1;
OS Klebsiella pneumoniae.
OG Plasmid nonconjugative 50kb.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=573;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBSTRATES, AND ACTIVITY REGULATION.
RC STRAIN=1534;
RX PubMed=11257029; DOI=10.1128/aac.45.4.1151-1161.2001;
RA Yigit H., Queenan A.M., Anderson G.J., Domenech-Sanchez A., Biddle J.W.,
RA Steward C.D., Alberti S., Bush K., Tenover F.C.;
RT "Novel carbapenem-hydrolyzing beta-lactamase, KPC-1, from a carbapenem-
RT resistant strain of Klebsiella pneumoniae.";
RL Antimicrob. Agents Chemother. 45:1151-1161(2001).
RN [2]
RP SEQUENCE REVISION TO 174.
RA Yigit H., Queenan A.M., Anderson G.J., Domenech-Sanchez A., Biddle J.W.,
RA Steward C.D., Alberti S., Bush K., Tenover F.C.;
RT "Novel carbapenem-hydrolyzing beta-lactamase, KPC-1, from a carbapenem-
RT resistant strain of Klebsiella pneumoniae.";
RL Antimicrob. Agents Chemother. 52:809-809(2008).
CC -!- FUNCTION: Hydrolyzes carbapenems, penicillins, cephalosporins and
CC monobactams 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:11257029}.
CC -!- MISCELLANEOUS: Initially two different KPC beta-lactamases were
CC identified from two different Klebsiella (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; AF297554; AAG13410.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; WP_004199234.1; NZ_WVUE01000041.1.
DR RefSeq; YP_002286834.1; NC_011382.1.
DR RefSeq; YP_002286844.1; NC_011383.1.
DR RefSeq; YP_002286855.1; NC_011383.1.
DR RefSeq; YP_003754012.1; NC_014312.1.
DR RefSeq; YP_006958635.1; NC_019152.1.
DR RefSeq; YP_006959213.1; NC_019161.1.
DR RefSeq; YP_006959400.1; NC_019165.1.
DR RefSeq; YP_006971133.1; NC_019384.1.
DR RefSeq; YP_007366474.1; NC_020132.1.
DR RefSeq; YP_007688776.1; NC_020893.1.
DR RefSeq; YP_008003445.1; NC_021238.1.
DR RefSeq; YP_008998912.1; NC_023331.1.
DR RefSeq; YP_009022511.1; NC_023903.1.
DR RefSeq; YP_009022618.1; NC_023904.1.
DR RefSeq; YP_009022725.1; NC_023905.1.
DR RefSeq; YP_009022831.1; NC_023906.1.
DR RefSeq; YP_009070099.1; NC_025166.1.
DR RefSeq; YP_009071849.1; NC_025187.1.
DR RefSeq; YP_009328785.1; NC_032103.1.
DR PDB; 2OV5; X-ray; 1.85 A; A/B/C=30-290.
DR PDB; 3E2K; X-ray; 2.10 A; A/B=30-293.
DR PDB; 3E2L; X-ray; 1.87 A; A/B=30-293.
DR PDB; 3RXW; X-ray; 1.26 A; A=26-289.
DR PDB; 3RXX; X-ray; 1.62 A; A=26-289.
DR PDB; 4ZBE; X-ray; 1.80 A; A=26-289.
DR PDB; 5EEC; X-ray; 1.87 A; A/B=25-293.
DR PDB; 5UJ3; X-ray; 1.45 A; A=25-293.
DR PDB; 5UJ4; X-ray; 1.40 A; A=25-293.
DR PDB; 5UL8; X-ray; 1.15 A; A=25-293.
DR PDB; 6B1F; X-ray; 1.44 A; A/B=22-289.
DR PDB; 6B1H; X-ray; 1.80 A; A/B=22-289.
DR PDB; 6B1J; X-ray; 1.60 A; A/B=22-289.
DR PDB; 6B1W; X-ray; 1.73 A; A/B=22-289.
DR PDB; 6B1X; X-ray; 1.45 A; A/B=22-289.
DR PDB; 6B1Y; X-ray; 1.80 A; A/B=22-289.
DR PDB; 6D15; X-ray; 1.30 A; A=25-293.
DR PDB; 6D16; X-ray; 1.40 A; A=25-293.
DR PDB; 6D17; X-ray; 1.45 A; A=25-293.
DR PDB; 6D18; X-ray; 1.35 A; A=25-293.
DR PDB; 6D19; X-ray; 1.45 A; A=25-293.
DR PDB; 6J8Q; X-ray; 1.79 A; A/B/C/D=26-289.
DR PDB; 6JN3; X-ray; 2.22 A; A/B/C/D=26-289.
DR PDB; 6JN4; X-ray; 1.90 A; A/B/C/D=26-289.
DR PDB; 6JN5; X-ray; 1.97 A; A/B/C/D=26-289.
DR PDB; 6M7I; X-ray; 1.70 A; A=25-293.
DR PDB; 6MEY; X-ray; 1.42 A; A=25-293.
DR PDB; 6MLL; X-ray; 1.86 A; A=25-293.
DR PDB; 6MNP; X-ray; 2.20 A; A=25-293.
DR PDB; 6QW9; X-ray; 1.04 A; A=25-293.
DR PDB; 6QWA; X-ray; 1.06 A; A=25-293.
DR PDB; 6QWB; X-ray; 1.04 A; A=25-293.
DR PDB; 6QWC; X-ray; 1.30 A; A=25-293.
DR PDB; 6QWD; X-ray; 1.20 A; A=25-293.
DR PDB; 6QWE; X-ray; 1.40 A; A=25-293.
DR PDB; 6TD0; X-ray; 0.99 A; A=25-293.
DR PDB; 6TD1; X-ray; 1.20 A; A=25-293.
DR PDB; 6V1J; X-ray; 1.30 A; A=25-293.
DR PDB; 6V7I; X-ray; 1.25 A; A=25-293.
DR PDB; 6XD5; X-ray; 1.20 A; A=1-293.
DR PDB; 6XD7; X-ray; 1.65 A; A=1-293.
DR PDB; 6XJ8; X-ray; 2.05 A; A=1-293.
DR PDB; 6Z21; X-ray; 1.30 A; A=25-293.
DR PDB; 6Z22; X-ray; 1.40 A; A=25-293.
DR PDB; 6Z23; X-ray; 1.31 A; A=25-293.
DR PDB; 6Z24; X-ray; 1.25 A; A=25-293.
DR PDB; 6Z25; X-ray; 1.24 A; A=25-293.
DR PDB; 7A61; X-ray; 1.25 A; A=25-293.
DR PDB; 7E9A; X-ray; 2.25 A; A/B/C/D=26-289.
DR PDB; 7LJK; X-ray; 1.81 A; A/B=26-289.
DR PDB; 7LK8; X-ray; 1.43 A; A/B=30-289.
DR PDB; 7LLB; X-ray; 1.67 A; A/B=26-289.
DR PDB; 7LLH; X-ray; 2.10 A; A/B=29-288.
DR PDB; 7LNL; X-ray; 1.82 A; A/B=22-289.
DR PDB; 7TB7; X-ray; 0.99 A; A=24-289.
DR PDB; 7TBX; X-ray; 3.16 A; A/B=23-289.
DR PDB; 7TC1; X-ray; 1.16 A; A=24-289.
DR PDBsum; 2OV5; -.
DR PDBsum; 3E2K; -.
DR PDBsum; 3E2L; -.
DR PDBsum; 3RXW; -.
DR PDBsum; 3RXX; -.
DR PDBsum; 4ZBE; -.
DR PDBsum; 5EEC; -.
DR PDBsum; 5UJ3; -.
DR PDBsum; 5UJ4; -.
DR PDBsum; 5UL8; -.
DR PDBsum; 6B1F; -.
DR PDBsum; 6B1H; -.
DR PDBsum; 6B1J; -.
DR PDBsum; 6B1W; -.
DR PDBsum; 6B1X; -.
DR PDBsum; 6B1Y; -.
DR PDBsum; 6D15; -.
DR PDBsum; 6D16; -.
DR PDBsum; 6D17; -.
DR PDBsum; 6D18; -.
DR PDBsum; 6D19; -.
DR PDBsum; 6J8Q; -.
DR PDBsum; 6JN3; -.
DR PDBsum; 6JN4; -.
DR PDBsum; 6JN5; -.
DR PDBsum; 6M7I; -.
DR PDBsum; 6MEY; -.
DR PDBsum; 6MLL; -.
DR PDBsum; 6MNP; -.
DR PDBsum; 6QW9; -.
DR PDBsum; 6QWA; -.
DR PDBsum; 6QWB; -.
DR PDBsum; 6QWC; -.
DR PDBsum; 6QWD; -.
DR PDBsum; 6QWE; -.
DR PDBsum; 6TD0; -.
DR PDBsum; 6TD1; -.
DR PDBsum; 6V1J; -.
DR PDBsum; 6V7I; -.
DR PDBsum; 6XD5; -.
DR PDBsum; 6XD7; -.
DR PDBsum; 6XJ8; -.
DR PDBsum; 6Z21; -.
DR PDBsum; 6Z22; -.
DR PDBsum; 6Z23; -.
DR PDBsum; 6Z24; -.
DR PDBsum; 6Z25; -.
DR PDBsum; 7A61; -.
DR PDBsum; 7E9A; -.
DR PDBsum; 7LJK; -.
DR PDBsum; 7LK8; -.
DR PDBsum; 7LLB; -.
DR PDBsum; 7LLH; -.
DR PDBsum; 7LNL; -.
DR PDBsum; 7TB7; -.
DR PDBsum; 7TBX; -.
DR PDBsum; 7TC1; -.
DR AlphaFoldDB; Q9F663; -.
DR SMR; Q9F663; -.
DR BindingDB; Q9F663; -.
DR ChEMBL; CHEMBL6132; -.
DR DrugBank; DB09060; Avibactam.
DR DrugBank; DB12107; Vaborbactam.
DR DrugCentral; Q9F663; -.
DR GeneID; 67375509; -.
DR KEGG; ag:AAG13410; -.
DR EvolutionaryTrace; Q9F663; -.
DR PRO; PR:Q9F663; -.
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_0000349143"
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 STRAND 26..29
FT /evidence="ECO:0007829|PDB:6TD0"
FT HELIX 33..40
FT /evidence="ECO:0007829|PDB:6TD0"
FT STRAND 42..50
FT /evidence="ECO:0007829|PDB:6TD0"
FT TURN 51..53
FT /evidence="ECO:0007829|PDB:6TD0"
FT STRAND 56..60
FT /evidence="ECO:0007829|PDB:6TD0"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:6TD0"
FT HELIX 71..83
FT /evidence="ECO:0007829|PDB:6TD0"
FT TURN 87..91
FT /evidence="ECO:0007829|PDB:6QWD"
FT HELIX 98..100
FT /evidence="ECO:0007829|PDB:6TD0"
FT HELIX 108..111
FT /evidence="ECO:0007829|PDB:6TD0"
FT TURN 112..114
FT /evidence="ECO:0007829|PDB:6TD0"
FT HELIX 118..127
FT /evidence="ECO:0007829|PDB:6TD0"
FT HELIX 131..141
FT /evidence="ECO:0007829|PDB:6TD0"
FT HELIX 144..153
FT /evidence="ECO:0007829|PDB:6TD0"
FT HELIX 167..169
FT /evidence="ECO:0007829|PDB:6TD0"
FT HELIX 182..193
FT /evidence="ECO:0007829|PDB:6TD0"
FT STRAND 195..198
FT /evidence="ECO:0007829|PDB:6TD0"
FT HELIX 200..211
FT /evidence="ECO:0007829|PDB:6TD0"
FT TURN 217..219
FT /evidence="ECO:0007829|PDB:6TD0"
FT HELIX 220..223
FT /evidence="ECO:0007829|PDB:6TD0"
FT STRAND 228..236
FT /evidence="ECO:0007829|PDB:6TD0"
FT TURN 238..241
FT /evidence="ECO:0007829|PDB:6Z24"
FT STRAND 243..250
FT /evidence="ECO:0007829|PDB:6TD0"
FT STRAND 257..264
FT /evidence="ECO:0007829|PDB:6TD0"
FT HELIX 274..287
FT /evidence="ECO:0007829|PDB:6TD0"
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
