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P14489 (BLO10_PSEAI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 22, 2014. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Beta-lactamase OXA-10

EC=3.5.2.6
Alternative name(s):
Beta-lactamase PSE-2
Gene names
Name:bla
Synonyms:oxa10, pse2
Encoded onPlasmid pMON234
OrganismPseudomonas aeruginosa
Taxonomic identifier287 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length266 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Hydrolyzes both carbenicillin and oxacillin.

Catalytic activity

A beta-lactam + H2O = a substituted beta-amino acid.

Sequence similarities

Belongs to the class-D beta-lactamase family.

Ontologies

Keywords
   Biological processAntibiotic resistance
   DomainSignal
   Molecular functionHydrolase
   PTMDisulfide bond
   Technical term3D-structure
Plasmid
Transposable element
Gene Ontology (GO)
   Biological_processantibiotic catabolic process

Inferred from electronic annotation. Source: InterPro

response to antibiotic

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionbeta-lactamase activity

Inferred from electronic annotation. Source: UniProtKB-EC

penicillin binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020
Chain21 – 266246Beta-lactamase OXA-10
PRO_0000017030

Regions

Region205 – 2073Substrate binding By similarity

Sites

Active site671Acyl-ester intermediate

Amino acid modifications

Modified residue701N6-carboxylysine
Disulfide bond44 ↔ 51

Secondary structure

................................................ 266
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P14489 [UniParc].

Last modified January 1, 1990. Version 1.
Checksum: 9ABFF429D028F240

FASTA26629,507
        10         20         30         40         50         60 
MKTFAAYVII ACLSSTALAG SITENTSWNK EFSAEAVNGV FVLCKSSSKS CATNDLARAS 

        70         80         90        100        110        120 
KEYLPASTFK IPNAIIGLET GVIKNEHQVF KWDGKPRAMK QWERDLTLRG AIQVSAVPVF 

       130        140        150        160        170        180 
QQIAREVGEV RMQKYLKKFS YGNQNISGGI DKFWLEGQLR ISAVNQVEFL ESLYLNKLSA 

       190        200        210        220        230        240 
SKENQLIVKE ALVTEAAPEY LVHSKTGFSG VGTESNPGVA WWVGWVEKET EVYFFAFNMD 

       250        260 
IDNESKLPLR KSIPTKIMES EGIIGG 

« Hide

References

[1]"Sequence of PSE-2 beta-lactamase."
Huovinen P., Huovinen S., Jacoby G.A.
Antimicrob. Agents Chemother. 32:134-136(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Transposon: Tn1404.
[2]"Insights into class D beta-lactamases are revealed by the crystal structure of the OXA10 enzyme from Pseudomonas aeruginosa."
Maveyraud L., Golemi D., Kotra L.P., Tranier S., Vakulenko S., Mobashery S., Samama J.-P.
Structure 8:1289-1298(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.66 ANGSTROMS) OF 21-266, CARBAMYLATION AT LYS-70.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U37105 Genomic DNA. Translation: AAB60534.1.
J03427 Genomic DNA. Translation: AAA25648.1.
PIRS06462.
RefSeqYP_008532606.1. NC_022344.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1E3UX-ray1.66A/B/C/D21-266[»]
1E4DX-ray1.80A/B/C/D21-266[»]
1EWZX-ray2.40A/B/C/D21-266[»]
1FOFX-ray2.00A/B20-265[»]
1K4EX-ray2.00A/B20-266[»]
1K4FX-ray1.60A/B20-266[»]
1K54X-ray1.70A/B/C/D21-266[»]
1K55X-ray1.39A/B/C/D21-266[»]
1K56X-ray1.70A/B/C/D21-266[»]
1K57X-ray1.90A/B/C/D21-266[»]
1K6RX-ray2.30A/B20-266[»]
1K6SX-ray2.03A/B20-266[»]
2HP5X-ray2.70A/B/C/D20-266[»]
2HP6X-ray2.20A/B20-266[»]
2HP9X-ray2.50A/B20-266[»]
2HPBX-ray2.05A/B20-266[»]
2RL3X-ray1.90A/B20-266[»]
2WGIX-ray2.85A/B20-266[»]
2WGVX-ray1.80A/B20-266[»]
2WGWX-ray1.80A/B20-266[»]
2WKHX-ray1.79A/B20-266[»]
2WKIX-ray2.10A/B20-266[»]
2X01X-ray1.90A/B20-266[»]
2X02X-ray1.35A/B20-266[»]
3LCEX-ray2.00A/B/C/D21-266[»]
ProteinModelPortalP14489.
SMRP14489. Positions 21-266.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBP14489.
ChEMBLCHEMBL5482.
DrugBankDB00760. Meropenem.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID16834474.

Family and domain databases

Gene3D3.40.710.10. 1 hit.
InterProIPR012338. Beta-lactam/transpept-like.
IPR002137. Beta-lactam_class-D_AS.
IPR001460. PCN-bd_Tpept.
[Graphical view]
PfamPF00905. Transpeptidase. 1 hit.
[Graphical view]
SUPFAMSSF56601. SSF56601. 1 hit.
PROSITEPS00337. BETA_LACTAMASE_D. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP14489.

Entry information

Entry nameBLO10_PSEAI
AccessionPrimary (citable) accession number: P14489
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: January 22, 2014
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references