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P00808 (BLAC_BACLI) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 117. 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

Cleaved into the following 2 chains:

  1. Large exopenicillinase
  2. Small exopenicillinase
Gene names
Name:penP
Synonyms:blaP
OrganismBacillus licheniformis
Taxonomic identifier1402 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length307 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.

Subcellular location

Cell membrane; Lipid-anchor Probable.

Induction

By the bacillus licheniformis protein BlaR1.

Post-translational modification

Large exopenicillinase is the primary secretion product; it can be converted to small exopenicillinase.

Sequence similarities

Belongs to the class-A beta-lactamase family.

Ontologies

Keywords
   Biological processAntibiotic resistance
   Cellular componentCell membrane
Membrane
   DomainSignal
   Molecular functionHydrolase
   PTMLipoprotein
Palmitate
   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

   Cellular_componentplasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   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 – 2626
Chain27 – 307281Large exopenicillinase
PRO_0000016973
Chain43 – 307265Small exopenicillinase
PRO_0000016974

Regions

Region248 – 2503Substrate binding

Sites

Active site861Acyl-ester intermediate
Active site1821Proton acceptor

Amino acid modifications

Lipidation271N-palmitoyl cysteine
Lipidation271S-diacylglycerol cysteine

Secondary structure

................................................... 307
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00808 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 7E25B1E72129A6DA

FASTA30733,996
        10         20         30         40         50         60 
MKLWFSTLKL KKAAAVLLFS CVALAGCANN QTNASQPAEK NEKTEMKDDF AKLEEQFDAK 

        70         80         90        100        110        120 
LGIFALDTGT NRTVAYRPDE RFAFASTIKA LTVGVLLQQK SIEDLNQRIT YTRDDLVNYN 

       130        140        150        160        170        180 
PITEKHVDTG MTLKELADAS LRYSDNAAQN LILKQIGGPE SLKKELRKIG DEVTNPERFE 

       190        200        210        220        230        240 
PELNEVNPGE TQDTSTARAL VTSLRAFALE DKLPSEKREL LIDWMKRNTT GDALIRAGVP 

       250        260        270        280        290        300 
DGWEVADKTG AASYGTRNDI AIIWPPKGDP VVLAVLSSRD KKDAKYDDKL IAEATKVVMK 


ALNMNGK 

« Hide

References

[1]"Penicillinase from Bacillus licheniformis: nucleotide sequence of the gene and implications for the biosynthesis of a secretory protein in a Gram-positive bacterium."
Neugebauer K., Sprengel R., Schaller H.
Nucleic Acids Res. 9:2577-2588(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 25972 / 749/C / DSM 8782 / NCIMB 11109 / IMET 10723.
[2]"The promoter-proximal region of the Bacillus licheniformis penicillinase gene: nucleotide sequence and predicted leader peptide sequence."
Kroyer J., Chang S.
Gene 15:343-347(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-72.
Strain: ATCC 25972 / 749/C / DSM 8782 / NCIMB 11109 / IMET 10723.
[3]"The amino acid sequence of penicillinase from Bacillus licheniformis."
Meadway R.J.
Biochem. J. 115:12P-13P(1969) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 43-307.
[4]"Regulation of the penicillinase genes of Bacillus licheniformis: interaction of the pen repressor with its operators."
Wittman V., Wong H.C.
J. Bacteriol. 170:3206-3212(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-15.
Strain: ATCC 25972 / 749/C / DSM 8782 / NCIMB 11109 / IMET 10723.
[5]"Large exopenicillinase, initial extracellular form detected in cultures of Bacillus licheniformis."
Izui K., Nielsen J.B.K., Caulfield M.P., Lampen J.O.
Biochemistry 19:1882-1886(1980) [PubMed] [Europe PMC] [Abstract]
Cited for: CONFIRMATION OF THE AMINO ENDS OF THE LARGE AND SMALL EXOPENICILLINASE.
[6]"Beta-lactamase of Bacillus licheniformis 749/C at 2-A resolution."
Moews P.C., Knox J.R., Dideberg O., Charlier P., Frere J.-M.
Proteins 7:156-171(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[7]"Beta-lactamase of Bacillus licheniformis 749/C. Refinement at 2-A resolution and analysis of hydration."
Knox J.R., Moews P.C.
J. Mol. Biol. 220:435-455(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[8]"Crystal structures of the Bacillus licheniformis BS3 class A beta-lactamase and of the acyl-enzyme adduct formed with cefoxitin."
Fonze E., Vanhove M., Dive G., Sauvage E., Frere J.-M., Charlier P.
Biochemistry 41:1877-1885(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
V00093 Genomic DNA. Translation: CAA23431.1.
M21337 Genomic DNA. Translation: AAA22649.2.
PIRPNBSL. A93727.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1I2SX-ray1.70A/B26-307[»]
1I2WX-ray1.70A/B26-307[»]
1MBLX-ray2.00A/B48-303[»]
1W7FX-ray1.80A/B1-307[»]
2BLMX-ray2.00A/B43-307[»]
2WK0X-ray1.65A/B43-307[»]
2Y91X-ray2.00A/B43-307[»]
3B3XX-ray2.50A/B43-307[»]
3LY3X-ray1.80A47-305[»]
3LY4X-ray1.80A47-303[»]
3M2JX-ray1.80A/B47-303[»]
3M2KX-ray3.50A/B47-303[»]
3SH7X-ray2.50A/B43-307[»]
3SH8X-ray2.00A/B43-307[»]
3SH9X-ray1.90A/B43-307[»]
3SOIX-ray1.73A/B46-303[»]
4BLMX-ray2.00A/B43-307[»]
ProteinModelPortalP00808.
SMRP00808. Positions 48-303.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBP00808.
ChEMBLCHEMBL5633.
DrugBankDB01331. Cefoxitin.

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.
[Graphical view]
PfamPF00144. Beta-lactamase. 1 hit.
[Graphical view]
PRINTSPR00118. BLACTAMASEA.
SUPFAMSSF56601. SSF56601. 1 hit.
PROSITEPS00146. BETA_LACTAMASE_A. 1 hit.
PS51257. PROKAR_LIPOPROTEIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP00808.

Entry information

Entry nameBLAC_BACLI
AccessionPrimary (citable) accession number: P00808
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: October 16, 2013
This is version 117 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