P22391 (BLO1_KLEOX) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Beta-lactamase OXY-1
EC=3.5.2.6

Alternative name(s):
Penicillinase

Gene names

Name:

bla

Organism

Klebsiella oxytoca

Taxonomic identifier

571 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	291 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 broad-spectrum beta-lactam antibiotics. Active against cephalosporins.
Catalytic activity	A beta-lactam + H2O = a substituted beta-amino acid.
Miscellaneous	In strain KH66 OXY-1 is known as OXY-1a.
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
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

Chain

25 – 291

267

Beta-lactamase OXY-1

PRO_0000016997

Regions

Region

237 – 239

3

Substrate binding By similarity

Sites

Active site

73

1

Acyl-ester intermediate By similarity

Natural variations

Natural variant

262

1

L → P in strain: KH66.

Natural variant

278

1

E → K in strain: KH66.

Secondary structure

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291

Helix Strand Turn

Details...

Helix

32 – 44

13

Beta strand

46 – 54

9

Turn

55 – 57

3

Beta strand

60 – 64

5

Helix

72 – 75

4

Helix

76 – 89

14

Beta strand

91 – 93

3

Helix

102 – 104

3

Helix

112 – 114

3

Turn

116 – 118

3

Helix

122 – 131

10

Helix

135 – 145

11

Helix

148 – 157

10

Helix

171 – 173

3

Helix

186 – 197

12

Beta strand

199 – 202

4

Helix

204 – 215

12

Turn

221 – 223

3

Helix

224 – 227

4

Beta strand

232 – 241

10

Turn

242 – 244

3

Beta strand

245 – 253

9

Beta strand

255 – 257

3

Beta strand

260 – 267

8

Helix

277 – 288

12

Sequences

	Sequence		Length	Mass (Da)
	P22391 [UniParc]. Last modified August 1, 1991. Version 1. Checksum: 9908F5AA97EDDC8A	FASTA	291	31,044
	10 20 30 40 50 60 MLKSSWRKTA LMAAAAVPLL LASGSLWASA DAIQQKLADL EKRSGGRLGV ALINTADDSQ 70 80 90 100 110 120 TLYRGDERFA MCSTGKVMAA AAVLKQSESN PEVVNKRLEI KKSDLVVWSP ITEKHLQSGM 130 140 150 160 170 180 TLAELSAAAL QYSDNTAMNK MISYLGGPEK VTAFAQSIGD VTFRLDRTEP ALNSAIPGDK 190 200 210 220 230 240 RDTTTPLAMA ESLRKLTLGN ALGEQQRAQL VTWLKGNTTG GQSIRAGLPA SWAVGDKTGA 250 260 270 280 290 GDYGTTNDIA VIWPENHAPL VLVTYFTQPQ QDAKSRKEVL AAAAKIVTEG L

References

[1]	"Chromosomal beta-lactamase of Klebsiella oxytoca, a new class A enzyme that hydrolyzes broad-spectrum beta-lactam antibiotics." Arakawa Y., Ohta M., Kido N., Mori M., Ito H., Komatsu T., Fujii Y., Kato N. Antimicrob. Agents Chemother. 33:63-70(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: E23004.
[2]	"Klebsiella oxytoca: resistance to aztreonam by overproduction of the chromosomally encoded beta-lactamase." Fournier B., Arlet G., Lagrange P.H., Philippon A. FEMS Microbiol. Lett. 116:31-36(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: SL781 and SL7811.
[3]	"Genetic characterization of resistance to extended-spectrum beta-lactams in Klebsiella oxytoca isolates recovered from patients with septicemia at hospitals in the Stockholm area." Wu S.W., Dornbusch K., Kronvall G. Antimicrob. Agents Chemother. 43:1294-1297(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: KH66.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M27459 Genomic DNA. Translation: AAA25084.1.
Z30177 Genomic DNA. Translation: CAA82916.1.
Z30178 Genomic DNA. Translation: CAA82917.1.
Y17715 Genomic DNA. Translation: CAB42615.1.

PIR

S42075.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3BYD	X-ray	1.93	A	25-291	[»]

ProteinModelPortal

P22391.

SMR

P22391. Positions 31-291.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

Gene3D

3.40.710.10. 1 hit.

InterPro

IPR001466. Beta-lactam-related.
IPR012338. Beta-lactam/transpept-like.
IPR000871. Beta-lactam_class-A/D.
IPR023650. Beta-lactam_class-A_AS.
[Graphical view]

Pfam

PF00144. Beta-lactamase. 1 hit.
[Graphical view]

PRINTS

PR00118. BLACTAMASEA.

SUPFAM

SSF56601. PBP_transp_fold. 1 hit.

PROSITE

PS00146. BETA_LACTAMASE_A. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P22391.

Entry information

Entry name

BLO1_KLEOX

Accession

Primary (citable) accession number: P22391
Secondary accession number(s): Q9S6S0

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	August 1, 1991
Last modified:	April 3, 2013
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program