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Q47066

- BLT1_ECOLX

UniProt

Q47066 - BLT1_ECOLX

Protein

Beta-lactamase Toho-1

Gene

bla

Organism
Escherichia coli
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 79 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Has strong cefotaxime-hydrolyzing activity.

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei73 – 731Acyl-ester intermediate

    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

    Enzyme and pathway databases

    SABIO-RKQ47066.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Beta-lactamase Toho-1 (EC:3.5.2.6)
    Gene namesi
    Name:bla
    Encoded oniPlasmid0 Publication
    OrganismiEscherichia coli
    Taxonomic identifieri562 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2929Add
    BLAST
    Chaini30 – 291262Beta-lactamase Toho-1PRO_0000016994Add
    BLAST

    Proteomic databases

    PRIDEiQ47066.

    Interactioni

    Subunit structurei

    Monomer.

    Structurei

    Secondary structure

    1
    291
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi33 – 4311
    Beta strandi46 – 549
    Turni55 – 573
    Beta strandi60 – 645
    Helixi72 – 754
    Helixi76 – 8712
    Helixi93 – 953
    Beta strandi97 – 993
    Helixi102 – 1043
    Helixi112 – 1154
    Beta strandi118 – 1214
    Helixi122 – 13110
    Helixi135 – 14511
    Helixi148 – 15710
    Helixi171 – 1733
    Helixi186 – 19813
    Beta strandi199 – 2024
    Helixi204 – 21512
    Turni221 – 2233
    Helixi224 – 2274
    Beta strandi232 – 24110
    Turni242 – 2443
    Beta strandi245 – 2539
    Beta strandi255 – 2573
    Beta strandi260 – 2678
    Helixi277 – 28812

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BZAX-ray1.80A30-290[»]
    1IYOX-ray1.80A30-291[»]
    1IYPX-ray2.00A30-291[»]
    1IYQX-ray2.10A30-291[»]
    1IYSX-ray1.65A31-291[»]
    1WE4X-ray1.70A30-291[»]
    2WYXneutron diffraction2.10A33-288[»]
    2XQZneutron diffraction2.10A32-291[»]
    2XR0X-ray2.20A32-291[»]
    2ZQ7X-ray0.94A30-291[»]
    2ZQ8X-ray1.03A30-291[»]
    2ZQ9X-ray1.07A30-291[»]
    2ZQAX-ray0.95A30-291[»]
    2ZQCX-ray1.07A30-291[»]
    2ZQDX-ray1.19A30-291[»]
    4BD0X-ray1.21A31-291[»]
    4BD1neutron diffraction2.00A31-291[»]
    ProteinModelPortaliQ47066.
    SMRiQ47066. Positions 31-291.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ47066.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni237 – 2393Substrate 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.
    InterProiIPR012338. Beta-lactam/transpept-like.
    IPR000871. Beta-lactam_class-A/D.
    IPR023650. Beta-lactam_class-A_AS.
    [Graphical view]
    PRINTSiPR00118. BLACTAMASEA.
    SUPFAMiSSF56601. SSF56601. 1 hit.
    PROSITEiPS00146. BETA_LACTAMASE_A. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q47066-1 [UniParc]FASTAAdd to Basket

    « Hide

    MMTQSIRRSM LTVMATLPLL FSSATLHAQA NSVQQQLEAL EKSSGGRLGV    50
    ALINTADNSQ ILYRADERFA MCSTSKVMAA AAVLKQSESD KHLLNQRVEI 100
    KKSDLVNYNP IAEKHVNGTM TLAELGAAAL QYSDNTAMNK LIAHLGGPDK 150
    VTAFARSLGD ETFRLDRTEP TLNTAIPGDP RDTTTPLAMA QTLKNLTLGK 200
    ALAETQRAQL VTWLKGNTTG SASIRAGLPK SWVVGDKTGS GDYGTTNDIA 250
    VIWPENHAPL VLVTYFTQPE QKAERRRDIL AAAAKIVTHG F 291
    Length:291
    Mass (Da):31,447
    Last modified:November 1, 1996 - v1
    Checksum:i83FC0CD9CD41E7C0
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D37830 Genomic DNA. Translation: BAA07082.1.
    PIRiJP0074.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D37830 Genomic DNA. Translation: BAA07082.1 .
    PIRi JP0074.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BZA X-ray 1.80 A 30-290 [» ]
    1IYO X-ray 1.80 A 30-291 [» ]
    1IYP X-ray 2.00 A 30-291 [» ]
    1IYQ X-ray 2.10 A 30-291 [» ]
    1IYS X-ray 1.65 A 31-291 [» ]
    1WE4 X-ray 1.70 A 30-291 [» ]
    2WYX neutron diffraction 2.10 A 33-288 [» ]
    2XQZ neutron diffraction 2.10 A 32-291 [» ]
    2XR0 X-ray 2.20 A 32-291 [» ]
    2ZQ7 X-ray 0.94 A 30-291 [» ]
    2ZQ8 X-ray 1.03 A 30-291 [» ]
    2ZQ9 X-ray 1.07 A 30-291 [» ]
    2ZQA X-ray 0.95 A 30-291 [» ]
    2ZQC X-ray 1.07 A 30-291 [» ]
    2ZQD X-ray 1.19 A 30-291 [» ]
    4BD0 X-ray 1.21 A 31-291 [» ]
    4BD1 neutron diffraction 2.00 A 31-291 [» ]
    ProteinModelPortali Q47066.
    SMRi Q47066. Positions 31-291.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    ChEMBLi CHEMBL1697675.

    Proteomic databases

    PRIDEi Q47066.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    SABIO-RK Q47066.

    Miscellaneous databases

    EvolutionaryTracei Q47066.

    Family and domain databases

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

    Publicationsi

    1. "Cloning and sequence of the gene encoding a cefotaxime-hydrolyzing class A beta-lactamase isolated from Escherichia coli."
      Ishii Y., Ohno A., Taguchi H., Imajo S., Ishiguro M., Matsuzawa H.
      Antimicrob. Agents Chemother. 39:2269-2275(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: TUH12191.
    2. "Crystal structure of the E166A mutant of extended-spectrum beta-lactamase Toho-1 at 1.8 A resolution."
      Ibuka A., Taguchi A., Ishiguro M., Fushinobu S., Ishii Y., Kamitori S., Okuyama K., Yamaguchi K., Konno M., Matsuzawa H.
      J. Mol. Biol. 285:2079-2087(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANT ALA-169.
      Strain: TUH12191.

    Entry informationi

    Entry nameiBLT1_ECOLX
    AccessioniPrimary (citable) accession number: Q47066
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 79 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, Plasmid

    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