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P0A1V8 (BLO2_SALTM) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 41. 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-2

EC=3.5.2.6
Alternative name(s):
Penicillinase
Gene names
Name:bla
Synonyms:oxa2
Encoded onPlasmid IncN R46 Ref.1 Ref.2 Ref.3
Plasmid pBP11 Ref.4
OrganismSalmonella typhimurium
Taxonomic identifier90371 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length275 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This is an oxacillin-hydrolyzing beta-lactamase.

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
   Technical term3D-structure
Direct protein sequencing
Plasmid
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 – 2121 Ref.3
Chain22 – 275254Beta-lactamase OXA-2
PRO_0000017026

Regions

Region210 – 2123Substrate binding By similarity

Sites

Active site721Acyl-ester intermediate By similarity

Amino acid modifications

Modified residue751N6-carboxylysine

Secondary structure

........................................ 275
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A1V8 [UniParc].

Last modified August 13, 1987. Version 1.
Checksum: D3678DFCB78DE8B6

FASTA27531,686
        10         20         30         40         50         60 
MAIRIFAILF SIFSLATFAH AQEGTLERSD WRKFFSEFQA KGTIVVADER QADRAMLVFD 

        70         80         90        100        110        120 
PVRSKKRYSP ASTFKIPHTL FALDAGAVRD EFQIFRWDGV NRGFAGHNQD QDLRSAMRNS 

       130        140        150        160        170        180 
TVWVYELFAK EIGDDKARRY LKKIDYGNAD PSTSNGDYWI EGSLAISAQE QIAFLRKLYR 

       190        200        210        220        230        240 
NELPFRVEHQ RLVKDLMIVE AGRNWILRAK TGWEGRMGWW VGWVEWPTGS VFFALNIDTP 

       250        260        270 
NRMDDLFKRE AIVRAILRSI EALPPNPAVN SDAAR 

« Hide

References

[1]"Sequence of the OXA2 beta-lactamase: comparison with other penicillin-reactive enzymes."
Dale J.W., Godwin D., Mossakowska D., Stephenson P., Wall S.
FEBS Lett. 191:39-44(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Type 1A.
[2]"Oxacillin-hydrolysing beta-lactamases. A comparative analysis at nucleotide and amino acid sequence levels."
Mossakowska D., Ali N.A., Dale J.W.
Eur. J. Biochem. 180:309-318(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Improved purification and characterization of the OXA-2 beta-lactamase."
Holland S., Dale J.W.
Biochem. J. 224:1009-1013(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 22-32.
[4]"Nucleotide sequence of an OXA-2 beta-lactamase gene from the R-plasmid R1767 derived plasmid pBP11 and comparison to closely related resistance determinants found in R46 and Tn2603."
Nuecken E.J., Henschke R.B., Schmidt F.R.J.
J. Gen. Microbiol. 135:761-765(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"Substrate-induced inactivation of the OXA2 beta-lactamase."
Ledent P., Frere J.M.
Biochem. J. 295:871-878(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 22-275, CARBAMYLATION AT LYS-75.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M25261 Genomic DNA. Translation: AAA98357.1.
X03037 Genomic DNA. Translation: CAA26839.1.
X07260 Genomic DNA. Translation: CAA30246.1.
PIRPNEBT. A91350.
RefSeqNP_511223.1. NC_003292.1.
NP_511225.1. NC_003292.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1K38X-ray1.50A/B22-275[»]
ProteinModelPortalP0A1V8.
SMRP0A1V8. Positions 25-265.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP0A1V8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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

EvolutionaryTraceP0A1V8.

Entry information

Entry nameBLO2_SALTM
AccessionPrimary (citable) accession number: P0A1V8
Secondary accession number(s): P05191, Q57015
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: November 13, 2013
This is version 41 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