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P14559 (BLAC_STRAL) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 79. 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

EC=3.5.2.6
Alternative name(s):
Penicillinase
OrganismStreptomyces albus G
Taxonomic identifier1962 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Protein attributes

Sequence length314 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Post-translational modification

Predicted to be exported by the Tat system. The position of the signal peptide cleavage has been experimentally proven.

Sequence similarities

Belongs to the class-A beta-lactamase family.

Ontologies

Keywords
   Biological processAntibiotic resistance
   DomainSignal
   Molecular functionHydrolase
   Technical term3D-structure
Direct protein sequencing
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 – 3939Tat-type signal
Chain40 – 314275Beta-lactamase
PRO_0000017012

Regions

Region259 – 2613Substrate binding By similarity

Sites

Active site891Acyl-ester intermediate Ref.2

Secondary structure

............................................. 314
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P14559 [UniParc].

Last modified January 1, 1990. Version 1.
Checksum: 5A17D7D19C84E511

FASTA31433,265
        10         20         30         40         50         60 
MHPSTSRPSR RTLLTATAGA ALAAATLVPG TAHASSGGRG HGSGSVSDAE RRLAGLERAS 

        70         80         90        100        110        120 
GARLGVYAYD TGSGRTVAYR ADELFPMCSV FKTLSSAAVL RDLDRNGEFL SRRILYTQDD 

       130        140        150        160        170        180 
VEQADGAGPE TGKPQNLANA QLTVEELCEV SITASDNCAA NLMLRELGGP AAVTRFVRSL 

       190        200        210        220        230        240 
GDRVTRLDRW EPELNSAEPG RVTDTTSPRA ITRTYGRLVL GDALNPRDRR LLTSWLLANT 

       250        260        270        280        290        300 
TSGDRFRAGL PDDWTLGDKT GAGRYGTNND AGVTWPPGRA PIVLTVLTAK TEQDAARDDG 

       310 
LVADAARVLA ETLG 

« Hide

References

[1]"Nucleotide sequence of the gene encoding the Streptomyces albus G beta-lactamase precursor."
Dehottay P., Dusart J., de Meester F., Joris B., van Beeumen J., Erpicum T., Frere J.-M., Ghuysen J.-M.
Eur. J. Biochem. 166:345-350(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
[2]"The active sites of the beta-lactamases of Streptomyces cacaoi and Streptomyces albus G."
de Meester F., Joris B., Lenzini M.V., Dehottay P., Erpicium T., Dusart J., Klein D., Ghuysen J.-M., Frere J.-M., van Beeumen J.
Biochem. J. 244:427-432(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 81-92, ACTIVE SITE SER-89.
[3]Fonze E., Charlier P., Dideberg O.
Submitted (JUL-1998) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 47-314.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M28303 Genomic DNA. Translation: AAA26775.1.
PIRPNSM1U. S00057.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BSGX-ray1.85A47-314[»]
ProteinModelPortalP14559.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.40.710.10. 1 hit.
InterProIPR001466. Beta-lactam-related.
IPR012338. Beta-lactam/transpept-like.
IPR000871. Beta-lactam_class-A/D.
IPR023650. Beta-lactam_class-A_AS.
IPR006311. TAT_signal.
[Graphical view]
PfamPF00144. Beta-lactamase. 1 hit.
[Graphical view]
PRINTSPR00118. BLACTAMASEA.
SUPFAMSSF56601. SSF56601. 1 hit.
PROSITEPS00146. BETA_LACTAMASE_A. 1 hit.
PS51318. TAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP14559.

Entry information

Entry nameBLAC_STRAL
AccessionPrimary (citable) accession number: P14559
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: October 16, 2013
This is version 79 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