Q9F663 (BLKPC_KLEPN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Carbepenem-hydrolyzing beta-lactamase KPC
EC=3.5.2.6

Alternative name(s):
Carbepenem-hydrolyzing beta-lactamase KPC-1

Gene names

Name:	bla
Synonyms:	kpc, kpc1

Encoded on

Plasmid nonconjugative 50kb

Organism

Klebsiella pneumoniae

Taxonomic identifier

573 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Klebsiella

Protein attributes

Sequence length	293 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Hydrolyzes carbapenems, penicillins, cephalosporins and monobactams with varying efficiency.
Catalytic activity	A beta-lactam + H2O = a substituted beta-amino acid.
Enzyme regulation	Not inhibited by EDTA, inhibited by clavulanic acid and tazobactam. Ref.1
Miscellaneous	Initially two different KPC beta-lactamases were identified from two different Klebsiella (KPC-1 and KPC-2); they were later shown to be identical.
Sequence similarities	Belongs to the class-A beta-lactamase family.

Ontologies

Keywords
Biological process	Antibiotic resistance
Domain	Signal
Molecular function	Hydrolase
Technical term	3D-structure Plasmid
Gene Ontology (GO)
Biological_process	beta-lactam antibiotic catabolic process Inferred from electronic annotation. Source: InterPro response to antibiotic Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	beta-lactamase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 24

24

Potential

Chain

25 – 293

269

Carbepenem-hydrolyzing beta-lactamase KPC

PRO_0000349143

Regions

Region

233 – 235

3

Substrate binding By similarity

Sites

Active site

69

1

Acyl-ester intermediate By similarity

Active site

167

1

Proton acceptor By similarity

Secondary structure

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293

Helix Strand Turn

Details...

Turn

28 – 30

3

Helix

31 – 40

10

Beta strand

42 – 50

9

Turn

51 – 53

3

Beta strand

56 – 60

5

Helix

68 – 70

3

Helix

71 – 83

13

Turn

87 – 91

5

Helix

98 – 100

3

Helix

106 – 110

5

Turn

111 – 114

4

Helix

118 – 127

10

Helix

131 – 141

11

Helix

143 – 153

11

Helix

167 – 169

3

Helix

182 – 193

12

Beta strand

195 – 198

4

Helix

200 – 211

12

Turn

217 – 219

3

Helix

220 – 223

4

Beta strand

228 – 235

8

Helix

239 – 241

3

Beta strand

243 – 250

8

Beta strand

257 – 264

8

Helix

274 – 287

14

Sequences

	Sequence		Length	Mass (Da)
	Q9F663 [UniParc]. Last modified September 2, 2008. Version 2. Checksum: 13EB2FC28005EE5F	FASTA	293	31,115
	10 20 30 40 50 60 MSLYRRLVLL SCLSWPLAGF SATALTNLVA EPFAKLEQDF GGSIGVYAMD TGSGATVSYR 70 80 90 100 110 120 AEERFPLCSS FKGFLAAAVL ARSQQQAGLL DTPIRYGKNA LVPWSPISEK YLTTGMTVAE 130 140 150 160 170 180 LSAAAVQYSD NAAANLLLKE LGGPAGLTAF MRSIGDTTFR LDRWELELNS AIPGDARDTS 190 200 210 220 230 240 SPRAVTESLQ KLTLGSALAA PQRQQFVDWL KGNTTGNHRI RAAVPADWAV GDKTGTCGVY 250 260 270 280 290 GTANDYAVVW PTGRAPIVLA VYTRAPNKDD KHSEAVIAAA ARLALEGLGV NGQ

References

[1]	"Novel carbapenem-hydrolyzing beta-lactamase, KPC-1, from a carbapenem-resistant strain of Klebsiella pneumoniae." Yigit H., Queenan A.M., Anderson G.J., Domenech-Sanchez A., Biddle J.W., Steward C.D., Alberti S., Bush K., Tenover F.C. Antimicrob. Agents Chemother. 45:1151-1161(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBSTRATES, ENZYME REGULATION. Strain: 1534.
[2]	"Novel carbapenem-hydrolyzing beta-lactamase, KPC-1, from a carbapenem-resistant strain of Klebsiella pneumoniae." Yigit H., Queenan A.M., Anderson G.J., Domenech-Sanchez A., Biddle J.W., Steward C.D., Alberti S., Bush K., Tenover F.C. Antimicrob. Agents Chemother. 52:809-809(2008) Cited for: SEQUENCE REVISION TO 174.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF297554 Genomic DNA. Translation: AAG13410.1. Sequence problems.

RefSeq

YP_002286834.1. NC_011382.1.
YP_002286844.1. NC_011383.1.
YP_002286855.1. NC_011383.1.
YP_003754012.1. NC_014312.1.
YP_006958635.1. NC_019152.1.
YP_006959213.1. NC_019161.1.
YP_006959400.1. NC_019165.1.
YP_006971133.1. NC_019384.1.
YP_007366474.1. NC_020132.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2OV5	X-ray	1.85	A/B/C	30-290	[»]
3E2K	X-ray	2.10	A/B	30-293	[»]
3E2L	X-ray	1.87	A/B	30-293	[»]
3RXW	X-ray	1.26	A	26-289	[»]
3RXX	X-ray	1.62	A	26-289	[»]

ProteinModelPortal

Q9F663.

SMR

Q9F663. Positions 30-293.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

13914015.
13914300.
13914665.
13923837.
14458242.
6993854.
6993864.
6993875.
9389494.

Phylogenomic databases

ProtClustDB

CLSK2410415.

Family and domain databases

Gene3D

3.40.710.10. 1 hit.

InterPro

IPR012338. Beta-lactam/transpept-like.
IPR000871. Beta-lactam_class-A/D.
[Graphical view]

PRINTS

PR00118. BLACTAMASEA.

SUPFAM

SSF56601. PBP_transp_fold. 1 hit.

PROSITE

PS00146. BETA_LACTAMASE_A. False negative.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

Q9F663.

ChEMBL

CHEMBL6132.

EvolutionaryTrace

Q9F663.

Entry information

Entry name

BLKPC_KLEPN

Accession

Primary (citable) accession number: Q9F663

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 2, 2008
Last sequence update:	September 2, 2008
Last modified:	April 3, 2013
This is version 50 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program