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Q47066 (BLT1_ECOLX) Reviewed, UniProtKB/Swiss-Prot

Last modified December 11, 2013. Version 77. 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 Toho-1

EC=3.5.2.6
Gene names
Name:bla
Encoded onPlasmid
OrganismEscherichia coli
Taxonomic identifier562 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length291 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Has strong cefotaxime-hydrolyzing activity.

Catalytic activity

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

Subunit structure

Monomer.

Sequence similarities

Belongs to the class-A beta-lactamase family.

Ontologies

Keywords
   Biological processAntibiotic resistance
   DomainSignal
   Molecular functionHydrolase
   Technical term3D-structure
Plasmid
Gene Ontology (GO)
   Biological_processbeta-lactam antibiotic 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

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2929
Chain30 – 291262Beta-lactamase Toho-1
PRO_0000016994

Regions

Region237 – 2393Substrate binding

Sites

Active site731Acyl-ester intermediate

Secondary structure

.............................................. 291
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q47066 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 83FC0CD9CD41E7C0

FASTA29131,447
        10         20         30         40         50         60 
MMTQSIRRSM LTVMATLPLL FSSATLHAQA NSVQQQLEAL EKSSGGRLGV ALINTADNSQ 

        70         80         90        100        110        120 
ILYRADERFA MCSTSKVMAA AAVLKQSESD KHLLNQRVEI KKSDLVNYNP IAEKHVNGTM 

       130        140        150        160        170        180 
TLAELGAAAL QYSDNTAMNK LIAHLGGPDK VTAFARSLGD ETFRLDRTEP TLNTAIPGDP 

       190        200        210        220        230        240 
RDTTTPLAMA QTLKNLTLGK ALAETQRAQL VTWLKGNTTG SASIRAGLPK SWVVGDKTGS 

       250        260        270        280        290 
GDYGTTNDIA VIWPENHAPL VLVTYFTQPE QKAERRRDIL AAAAKIVTHG F 

« Hide

References

[1]"Cloning and sequence of the gene encoding a cefotaxime-hydrolyzing class A beta-lactamase isolated from Escherichia coli."
Ishii Y., Ohno A., Taguchi H., Imajo S., Ishiguro M., Matsuzawa H.
Antimicrob. Agents Chemother. 39:2269-2275(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: TUH12191.
[2]"Crystal structure of the E166A mutant of extended-spectrum beta-lactamase Toho-1 at 1.8 A resolution."
Ibuka A., Taguchi A., Ishiguro M., Fushinobu S., Ishii Y., Kamitori S., Okuyama K., Yamaguchi K., Konno M., Matsuzawa H.
J. Mol. Biol. 285:2079-2087(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANT ALA-169.
Strain: TUH12191.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D37830 Genomic DNA. Translation: BAA07082.1.
PIRJP0074.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BZAX-ray1.80A30-291[»]
1IYOX-ray1.80A30-291[»]
1IYPX-ray2.00A30-291[»]
1IYQX-ray2.10A30-291[»]
1IYSX-ray1.65A31-291[»]
1WE4X-ray1.70A31-291[»]
2WYXneutron diffraction2.10A33-288[»]
2XQZneutron diffraction2.10A32-291[»]
2XR0X-ray2.20A32-291[»]
2ZQ7X-ray0.94A30-291[»]
2ZQ8X-ray1.03A30-291[»]
2ZQ9X-ray1.07A30-291[»]
2ZQAX-ray0.95A30-291[»]
2ZQCX-ray1.07A30-291[»]
2ZQDX-ray1.19A30-291[»]
4BD0X-ray1.21A31-291[»]
4BD1neutron diffraction2.00A31-291[»]
ProteinModelPortalQ47066.
SMRQ47066. Positions 31-291.
ModBaseSearch...
MobiDBSearch...

Chemistry

ChEMBLCHEMBL1697675.

Proteomic databases

PRIDEQ47066.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKQ47066.

Family and domain databases

Gene3D3.40.710.10. 1 hit.
InterProIPR012338. Beta-lactam/transpept-like.
IPR000871. Beta-lactam_class-A/D.
IPR023650. Beta-lactam_class-A_AS.
[Graphical view]
PRINTSPR00118. BLACTAMASEA.
SUPFAMSSF56601. SSF56601. 1 hit.
PROSITEPS00146. BETA_LACTAMASE_A. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ47066.

Entry information

Entry nameBLT1_ECOLX
AccessionPrimary (citable) accession number: Q47066
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1996
Last modified: December 11, 2013
This is version 77 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