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P00808

- BLAC_BACLI

UniProt

P00808 - BLAC_BACLI

Protein

Beta-lactamase

Gene

penP

Organism
Bacillus licheniformis
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 119 (01 Oct 2014)
      Sequence version 1 (21 Jul 1986)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei86 – 861Acyl-ester intermediate
    Active sitei182 – 1821Proton acceptor

    GO - Molecular functioni

    1. beta-lactamase activity Source: UniProtKB-EC

    GO - Biological processi

    1. beta-lactam antibiotic catabolic process Source: InterPro
    2. response to antibiotic Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Antibiotic resistance

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Beta-lactamase (EC:3.5.2.6)
    Alternative name(s):
    Penicillinase
    Cleaved into the following 2 chains:
    Gene namesi
    Name:penP
    Synonyms:blaP
    OrganismiBacillus licheniformis
    Taxonomic identifieri1402 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

    Subcellular locationi

    Cell membrane Curated; Lipid-anchor Curated

    GO - Cellular componenti

    1. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2626Add
    BLAST
    Chaini27 – 307281Large exopenicillinasePRO_0000016973Add
    BLAST
    Chaini43 – 307265Small exopenicillinasePRO_0000016974Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi27 – 271N-palmitoyl cysteinePROSITE-ProRule annotation
    Lipidationi27 – 271S-diacylglycerol cysteinePROSITE-ProRule annotation

    Post-translational modificationi

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

    Keywords - PTMi

    Lipoprotein, Palmitate

    Expressioni

    Inductioni

    By the bacillus licheniformis protein BlaR1.

    Interactioni

    Structurei

    Secondary structure

    1
    307
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi49 – 579
    Beta strandi60 – 678
    Turni68 – 703
    Beta strandi73 – 775
    Beta strandi81 – 833
    Helixi85 – 873
    Helixi88 – 9912
    Helixi103 – 1064
    Turni113 – 1153
    Helixi123 – 1253
    Turni127 – 1293
    Helixi133 – 14311
    Helixi146 – 15510
    Helixi158 – 16811
    Beta strandi178 – 1803
    Helixi182 – 1843
    Beta strandi194 – 1963
    Helixi197 – 20812
    Beta strandi210 – 2134
    Helixi215 – 22612
    Turni232 – 2343
    Helixi235 – 2384
    Beta strandi244 – 2529
    Turni253 – 2553
    Beta strandi256 – 2649
    Beta strandi266 – 2683
    Beta strandi271 – 2788
    Helixi289 – 30113

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliP00808.
    SMRiP00808. Positions 48-303.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00808.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni248 – 2503Substrate binding

    Sequence similaritiesi

    Belongs to the class-A beta-lactamase family.Curated

    Keywords - Domaini

    Signal

    Family and domain databases

    Gene3Di3.40.710.10. 1 hit.
    InterProiIPR001466. Beta-lactam-related.
    IPR012338. Beta-lactam/transpept-like.
    IPR000871. Beta-lactam_class-A/D.
    IPR023650. Beta-lactam_class-A_AS.
    [Graphical view]
    PfamiPF00144. Beta-lactamase. 1 hit.
    [Graphical view]
    PRINTSiPR00118. BLACTAMASEA.
    SUPFAMiSSF56601. SSF56601. 1 hit.
    PROSITEiPS00146. BETA_LACTAMASE_A. 1 hit.
    PS51257. PROKAR_LIPOPROTEIN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P00808-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKLWFSTLKL KKAAAVLLFS CVALAGCANN QTNASQPAEK NEKTEMKDDF    50
    AKLEEQFDAK LGIFALDTGT NRTVAYRPDE RFAFASTIKA LTVGVLLQQK 100
    SIEDLNQRIT YTRDDLVNYN PITEKHVDTG MTLKELADAS LRYSDNAAQN 150
    LILKQIGGPE SLKKELRKIG DEVTNPERFE PELNEVNPGE TQDTSTARAL 200
    VTSLRAFALE DKLPSEKREL LIDWMKRNTT GDALIRAGVP DGWEVADKTG 250
    AASYGTRNDI AIIWPPKGDP VVLAVLSSRD KKDAKYDDKL IAEATKVVMK 300
    ALNMNGK 307
    Length:307
    Mass (Da):33,996
    Last modified:July 21, 1986 - v1
    Checksum:i7E25B1E72129A6DA
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    V00093 Genomic DNA. Translation: CAA23431.1.
    M21337 Genomic DNA. Translation: AAA22649.2.
    PIRiA93727. PNBSL.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    V00093 Genomic DNA. Translation: CAA23431.1 .
    M21337 Genomic DNA. Translation: AAA22649.2 .
    PIRi A93727. PNBSL.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1I2S X-ray 1.70 A/B 26-307 [» ]
    1I2W X-ray 1.70 A/B 26-307 [» ]
    1MBL X-ray 2.00 A/B 48-303 [» ]
    1W7F X-ray 1.80 A/B 1-307 [» ]
    2BLM X-ray 2.00 A/B 43-307 [» ]
    2WK0 X-ray 1.65 A/B 43-307 [» ]
    2Y91 X-ray 2.00 A/B 43-307 [» ]
    3B3X X-ray 2.50 A/B 43-307 [» ]
    3LY3 X-ray 1.80 A 47-305 [» ]
    3LY4 X-ray 1.80 A 47-303 [» ]
    3M2J X-ray 1.80 A/B 47-303 [» ]
    3M2K X-ray 3.50 A/B 47-303 [» ]
    3SH7 X-ray 2.50 A/B 43-307 [» ]
    3SH8 X-ray 2.00 A/B 43-307 [» ]
    3SH9 X-ray 1.90 A/B 43-307 [» ]
    3SOI X-ray 1.73 A/B 46-303 [» ]
    4BLM X-ray 2.00 A/B 43-307 [» ]
    ProteinModelPortali P00808.
    SMRi P00808. Positions 48-303.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    BindingDBi P00808.
    ChEMBLi CHEMBL5633.
    DrugBanki DB01331. Cefoxitin.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P00808.

    Family and domain databases

    Gene3Di 3.40.710.10. 1 hit.
    InterProi IPR001466. Beta-lactam-related.
    IPR012338. Beta-lactam/transpept-like.
    IPR000871. Beta-lactam_class-A/D.
    IPR023650. Beta-lactam_class-A_AS.
    [Graphical view ]
    Pfami PF00144. Beta-lactamase. 1 hit.
    [Graphical view ]
    PRINTSi PR00118. BLACTAMASEA.
    SUPFAMi SSF56601. SSF56601. 1 hit.
    PROSITEi PS00146. BETA_LACTAMASE_A. 1 hit.
    PS51257. PROKAR_LIPOPROTEIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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).

    Entry informationi

    Entry nameiBLAC_BACLI
    AccessioniPrimary (citable) accession number: P00808
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 119 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3