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P00809 (BLAC_BACCE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Beta-lactamase 1
EC=3.5.2.6
Alternative name(s):
Beta-lactamase I
Penicillinase
Gene names
Name:blaY
OrganismBacillus cereus
Taxonomic identifier1396 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

Protein attributes

Sequence length306 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

This protein is a beta-lactamase with a substrate specificity for penicillins.

Catalytic activity

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

Sequence similarities

Belongs to the class-A beta-lactamase family.

Sequence caution

The sequence CAA26021.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAA29819.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processAntibiotic resistance
   DomainSignal
   Molecular functionHydrolase
   Technical term3D-structure
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: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727
Chain28 – 306279Beta-lactamase 1
PRO_0000016970

Regions

Region253 – 2553Substrate binding By similarity

Sites

Active site911Acyl-ester intermediate By similarity
Active site1871Proton acceptor By similarity

Experimental info

Sequence conflict2731S → R in CAA29819. Ref.2
Sequence conflict278 – 2803VLI → IAIL in CAA29819. Ref.2
Sequence conflict291 – 2922ND → DN in CAA29819. Ref.2
Sequence conflict305 – 3062GS → ALR in CAA29819. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P00809 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: F00F4DB9DB6D41AA

FASTA30633,322
        10         20         30         40         50         60 
MILKNKRMLK IGICVGILGL SITSLEAFTG ESLQVEAKEK TGQVKHKNQA THKEFSQLEK 

        70         80         90        100        110        120 
KFDARLGVYA IDTGTNQTIS YRPNERFAFA STYKALAAGV LLQQNSIDSL NEVITYTKED 

       130        140        150        160        170        180 
LVDYSPVTEK HVDTGMKLGE IAEAAVRSSD NTAGNILFNK IGGPKGYEKA LRHMGDRITM 

       190        200        210        220        230        240 
SNRFETELNE AIPGDIRDTS TAKAIATNLK AFTVGNALPA EKRKILTEWM KGNATGDKLI 

       250        260        270        280        290        300 
RAGIPTDWVV GDKSGAGSYG TRNDIAVVWP PNSAPIIVLI SSKDEKEAIY NDQLIAEATK 


VIVKGS

« Hide

References

[1]"Molecular cloning and nucleotide sequence of the type I beta-lactamase gene from Bacillus cereus."
Sloma A., Gross M.
Nucleic Acids Res. 11:4997-5004(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 569/H / NCTC 9945.
[2]"Beta-lactamase I from Bacillus cereus. Structure and site-directed mutagenesis."
Madgwick P.J., Waley S.G.
Biochem. J. 248:657-662(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 569/H/9.
[3]"Bacillus cereus 569/H beta-lactamase I: cloning in Escherichia coli and signal sequence determination."
Mezes P.S.F., Yang Y.Q., Hussain M., Lampen J.O.
FEBS Lett. 161:195-200(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 3-75.
Strain: 569/H / NCTC 9945.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X01990 Genomic DNA. Translation: CAA26021.1. Different initiation.
X01602 Genomic DNA. Translation: CAA25753.1.
X06599 Genomic DNA. Translation: CAA29819.1. Different initiation.
PIRPNBSU. A01004.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2CN9model-A80-104[»]
A258-270[»]
ProteinModelPortalP00809.
SMRP00809. Positions 54-305.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKP00809.

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.
[Graphical view]
PfamPF00144. Beta-lactamase. 1 hit.
[Graphical view]
PRINTSPR00118. BLACTAMASEA.
SUPFAMSSF56601. PBP_transp_fold. 1 hit.
PROSITEPS00146. BETA_LACTAMASE_A. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChEMBLCHEMBL5732.

Entry information

Entry nameBLAC_BACCE
AccessionPrimary (citable) accession number: P00809
Secondary accession number(s): P70876
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: April 3, 2013
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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