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 27-MAR-2024, entry version 118. 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; Pseudomonadota; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 7LR9; X-ray; 1.47 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 PDB; 7TI2; X-ray; 1.75 A; A=25-293. DR PDB; 7U8S; X-ray; 1.60 A; A=26-290. DR PDB; 7U9B; X-ray; 1.95 A; A=25-291. DR PDB; 7UA7; X-ray; 2.25 A; A=25-292. DR PDB; 7UTB; X-ray; 1.38 A; A=24-289. DR PDB; 7VQN; X-ray; 2.34 A; A/B/C/D=25-289. DR PDB; 8AKI; X-ray; 1.40 A; A=25-293. DR PDB; 8AKJ; X-ray; 1.35 A; A=25-293. DR PDB; 8AKK; X-ray; 1.36 A; A=25-293. DR PDB; 8AKL; X-ray; 1.35 A; A=25-293. DR PDB; 8AKM; X-ray; 1.25 A; A=25-293. DR PDB; 8G2R; X-ray; 1.28 A; A=24-289. DR PDB; 8G2T; X-ray; 1.26 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; 7LR9; -. DR PDBsum; 7TB7; -. DR PDBsum; 7TBX; -. DR PDBsum; 7TC1; -. DR PDBsum; 7TI2; -. DR PDBsum; 7U8S; -. DR PDBsum; 7U9B; -. DR PDBsum; 7UA7; -. DR PDBsum; 7UTB; -. DR PDBsum; 7VQN; -. DR PDBsum; 8AKI; -. DR PDBsum; 8AKJ; -. DR PDBsum; 8AKK; -. DR PDBsum; 8AKL; -. DR PDBsum; 8AKM; -. DR PDBsum; 8G2R; -. DR PDBsum; 8G2T; -. DR AlphaFoldDB; Q9F663; -. DR SMR; Q9F663; -. DR BindingDB; Q9F663; -. DR ChEMBL; CHEMBL6132; -. DR DrugBank; DB09060; Avibactam. DR DrugBank; DB12107; Vaborbactam. DR DrugCentral; Q9F663; -. 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; DD-peptidase/beta-lactamase superfamily; 1. DR InterPro; IPR012338; Beta-lactam/transpept-like. DR InterPro; IPR045155; Beta-lactam_cat. DR InterPro; IPR000871; Beta-lactam_class-A. DR PANTHER; PTHR35333; BETA-LACTAMASE; 1. DR PANTHER; PTHR35333:SF3; BETA-LACTAMASE2 DOMAIN-CONTAINING PROTEIN; 1. DR Pfam; PF13354; Beta-lactamase2; 1. DR PRINTS; PR00118; BLACTAMASEA. DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 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 HELIX 239..241 FT /evidence="ECO:0007829|PDB:7TB7" FT STRAND 243..250 FT /evidence="ECO:0007829|PDB:6TD0" FT STRAND 252..254 FT /evidence="ECO:0007829|PDB:7U8S" 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 //