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P13661

- BLO1_ECOLX

UniProt

P13661 - BLO1_ECOLX

Protein

Beta-lactamase OXA-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 92 (01 Oct 2014)
      Sequence version 2 (10 Feb 2009)
      Previous versions | rss
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    Functioni

    This is an oxacillin-hydrolyzing beta-lactamase.

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei71 – 711Acyl-ester intermediate

    GO - Molecular functioni

    1. beta-lactamase activity Source: UniProtKB-EC
    2. penicillin binding Source: InterPro

    GO - Biological processi

    1. 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-RKP13661.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Beta-lactamase OXA-1 (EC:3.5.2.6)
    Alternative name(s):
    Penicillinase
    Gene namesi
    Name:bla
    Synonyms:oxa1
    Encoded oniPlasmid RGN2380 Publication
    OrganismiEscherichia coli
    Taxonomic identifieri562 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 25251 PublicationAdd
    BLAST
    Chaini26 – 276251Beta-lactamase OXA-1PRO_0000017024Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei74 – 741N6-carboxylysine1 Publication

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Structurei

    Secondary structure

    1
    276
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi30 – 378
    Beta strandi40 – 489
    Turni49 – 513
    Beta strandi54 – 585
    Helixi60 – 634
    Helixi70 – 723
    Helixi73 – 8311
    Helixi103 – 1053
    Helixi111 – 1177
    Helixi120 – 13011
    Helixi132 – 14211
    Turni153 – 1553
    Helixi158 – 1614
    Beta strandi164 – 1674
    Helixi172 – 18312
    Beta strandi187 – 1893
    Helixi191 – 20111
    Beta strandi202 – 2054
    Beta strandi211 – 22010
    Beta strandi227 – 23610
    Beta strandi242 – 25110
    Helixi259 – 27315

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1M6KX-ray1.50A/B26-276[»]
    3ISGX-ray1.40A/B26-276[»]
    4MLLX-ray1.37A/B/C/D26-276[»]
    ProteinModelPortaliP13661.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP13661.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni238 – 2403Substrate bindingBy similarity

    Sequence similaritiesi

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

    Keywords - Domaini

    Signal

    Family and domain databases

    Gene3Di3.40.710.10. 1 hit.
    InterProiIPR012338. Beta-lactam/transpept-like.
    IPR002137. Beta-lactam_class-D_AS.
    IPR001460. PCN-bd_Tpept.
    [Graphical view]
    PfamiPF00905. Transpeptidase. 1 hit.
    [Graphical view]
    SUPFAMiSSF56601. SSF56601. 1 hit.
    PROSITEiPS00337. BETA_LACTAMASE_D. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P13661-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKNTIHINFA IFLIIANIIY SSASASTDIS TVASPLFEGT EGCFLLYDAS    50
    TNAEIAQFNK AKCATQMAPD STFKIALSLM AFDAEIIDQK TIFKWDKTPK 100
    GMEIWNSNHT PKTWMQFSVV WVSQEITQKI GLNKIKNYLK DFDYGNQDFS 150
    GDKERNNGLT EAWLESSLKI SPEEQIQFLR KIINHNLPVK NSAIENTIEN 200
    MYLQDLDNST KLYGKTGAGF TANRTLQNGW FEGFIISKSG HKYVFVSALT 250
    GNLGSNLTSS IKAKKNAITI LNTLNL 276
    Length:276
    Mass (Da):30,880
    Last modified:February 10, 2009 - v2
    Checksum:i5ADF7626422BA124
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J02967 Genomic DNA. Translation: AAA91586.2.
    PIRiA39880.
    RefSeqiNP_957554.1. NC_005327.1.
    YP_006953880.1. NC_019089.1.
    YP_008574821.1. NC_022374.1.

    Genome annotation databases

    GeneIDi13906817.
    17035637.
    2716479.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J02967 Genomic DNA. Translation: AAA91586.2 .
    PIRi A39880.
    RefSeqi NP_957554.1. NC_005327.1.
    YP_006953880.1. NC_019089.1.
    YP_008574821.1. NC_022374.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1M6K X-ray 1.50 A/B 26-276 [» ]
    3ISG X-ray 1.40 A/B 26-276 [» ]
    4MLL X-ray 1.37 A/B/C/D 26-276 [» ]
    ProteinModelPortali P13661.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    ChEMBLi CHEMBL4951.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 13906817.
    17035637.
    2716479.

    Enzyme and pathway databases

    SABIO-RK P13661.

    Miscellaneous databases

    EvolutionaryTracei P13661.

    Family and domain databases

    Gene3Di 3.40.710.10. 1 hit.
    InterProi IPR012338. Beta-lactam/transpept-like.
    IPR002137. Beta-lactam_class-D_AS.
    IPR001460. PCN-bd_Tpept.
    [Graphical view ]
    Pfami PF00905. Transpeptidase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56601. SSF56601. 1 hit.
    PROSITEi PS00337. BETA_LACTAMASE_D. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Precise insertion of antibiotic resistance determinants into Tn21-like transposons: nucleotide sequence of the OXA-1 beta-lactamase gene."
      Ouellette M., Bissonnette L., Roy P.H.
      Proc. Natl. Acad. Sci. U.S.A. 84:7378-7382(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Transposon: Tn2603.
    2. Ouellette M., Roy P.H.
      Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION TO 131.
    3. "Comparison of beta-lactamases of classes A and D: 1.5-A crystallographic structure of the class D OXA-1 oxacillinase."
      Sun T., Nukaga M., Mayama K., Braswell E.H., Knox J.R.
      Protein Sci. 12:82-91(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 26-276, PROTEIN SEQUENCE OF N-TERMINUS, CARBAMYLATION AT LYS-74, SUBUNIT.

    Entry informationi

    Entry nameiBLO1_ECOLX
    AccessioniPrimary (citable) accession number: P13661
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: February 10, 2009
    Last modified: October 1, 2014
    This is version 92 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing, Plasmid, Transposable element

    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