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P14559

- BLAC_STRAL

UniProt

P14559 - BLAC_STRAL

Protein

Beta-lactamase

Gene
N/A
Organism
Streptomyces albus G
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 80 (01 Oct 2014)
      Sequence version 1 (01 Jan 1990)
      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 sitei89 – 891Acyl-ester intermediate1 PublicationPROSITE-ProRule annotation

    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
    OrganismiStreptomyces albus G
    Taxonomic identifieri1962 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3939Tat-type signalAdd
    BLAST
    Chaini40 – 314275Beta-lactamasePRO_0000017012Add
    BLAST

    Post-translational modificationi

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

    Structurei

    Secondary structure

    1
    314
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi48 – 6013
    Beta strandi62 – 709
    Turni71 – 733
    Beta strandi76 – 805
    Helixi88 – 914
    Helixi92 – 10211
    Beta strandi105 – 1073
    Turni108 – 1114
    Helixi118 – 1247
    Turni129 – 1324
    Helixi134 – 1396
    Helixi144 – 15310
    Helixi157 – 16711
    Helixi171 – 1799
    Helixi193 – 1953
    Helixi208 – 21912
    Beta strandi221 – 2244
    Helixi226 – 23712
    Turni243 – 2453
    Helixi246 – 2494
    Beta strandi254 – 2629
    Beta strandi268 – 2758
    Beta strandi282 – 2898
    Helixi299 – 31214

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BSGX-ray1.85A47-314[»]
    ProteinModelPortaliP14559.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP14559.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni259 – 2613Substrate bindingBy similarity

    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.
    IPR006311. TAT_signal.
    [Graphical view]
    PfamiPF00144. Beta-lactamase. 1 hit.
    [Graphical view]
    PRINTSiPR00118. BLACTAMASEA.
    SUPFAMiSSF56601. SSF56601. 1 hit.
    PROSITEiPS00146. BETA_LACTAMASE_A. 1 hit.
    PS51318. TAT. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P14559-1 [UniParc]FASTAAdd to Basket

    « Hide

    MHPSTSRPSR RTLLTATAGA ALAAATLVPG TAHASSGGRG HGSGSVSDAE    50
    RRLAGLERAS GARLGVYAYD TGSGRTVAYR ADELFPMCSV FKTLSSAAVL 100
    RDLDRNGEFL SRRILYTQDD VEQADGAGPE TGKPQNLANA QLTVEELCEV 150
    SITASDNCAA NLMLRELGGP AAVTRFVRSL GDRVTRLDRW EPELNSAEPG 200
    RVTDTTSPRA ITRTYGRLVL GDALNPRDRR LLTSWLLANT TSGDRFRAGL 250
    PDDWTLGDKT GAGRYGTNND AGVTWPPGRA PIVLTVLTAK TEQDAARDDG 300
    LVADAARVLA ETLG 314
    Length:314
    Mass (Da):33,265
    Last modified:January 1, 1990 - v1
    Checksum:i5A17D7D19C84E511
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M28303 Genomic DNA. Translation: AAA26775.1.
    PIRiS00057. PNSM1U.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M28303 Genomic DNA. Translation: AAA26775.1 .
    PIRi S00057. PNSM1U.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BSG X-ray 1.85 A 47-314 [» ]
    ProteinModelPortali P14559.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P14559.

    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.
    IPR006311. TAT_signal.
    [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.
    PS51318. TAT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.

    Entry informationi

    Entry nameiBLAC_STRAL
    AccessioniPrimary (citable) accession number: P14559
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: January 1, 1990
    Last modified: October 1, 2014
    This is version 80 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