Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9S169

- BLA24_ECOLX

UniProt

Q9S169 - BLA24_ECOLX

Protein

Beta-lactamase SHV-24

Gene

bla

Organism
Escherichia coli
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 54 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Hydrolyzes ampicillin. Can also hydrolyze cephaloridine, aztreonam and ceftazidime with a low catalytic rate.1 Publication

    Catalytic activityi

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

    Kineticsi

    1. KM=32 µM for ampicillin1 Publication
    2. KM=210 µM for cephaloridine1 Publication
    3. KM=500 µM for aztreonam1 Publication
    4. KM=30 µM for ceftazidime1 Publication

    Vmax=0.366 µmol/min/µg enzyme with ampicillin as substrate1 Publication

    Vmax=0.434 µmol/min/µg enzyme with cephaloridine as substrate1 Publication

    Vmax=0.135 µmol/min/µg enzyme with aztreonam as substrate1 Publication

    Vmax=0.008 µmol/min/µg enzyme with ceftazidime as substrate1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei66 – 661Acyl-ester intermediatePROSITE-ProRule annotation
    Active sitei164 – 1641Proton acceptorBy similarity

    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-RKQ9S169.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Beta-lactamase SHV-24 (EC:3.5.2.6)
    Gene namesi
    Name:bla
    Synonyms:shv24
    OrganismiEscherichia coli
    Taxonomic identifieri562 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2121Sequence AnalysisAdd
    BLAST
    Chaini22 – 286265Beta-lactamase SHV-24PRO_0000016988Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi73 ↔ 119By similarity

    Keywords - PTMi

    Disulfide bond

    Structurei

    3D structure databases

    ProteinModelPortaliQ9S169.
    SMRiQ9S169. Positions 22-286.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni230 – 2323Substrate 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.
    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.

    Q9S169-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRYIRLCIIS LLATLPLAVH ASPQPLEQIK LSESQLSGRV GMIEMDLASG    50
    RTLTAWRADE RFPMMSTFKV VLCGAVLARV DAGDEQLERK IHYRQQDLVD 100
    YSPVSEKHLA DGMTVGELCA AAITMSDNSA ANLLLATVGG PAGLTAFLRQ 150
    IGDNVTRLDR WETELNEALP GDARGTTTPA SMAATLRKLL TSQRLSARSQ 200
    RQLLQWMVDD RVAGPLIRSV LPAGWFIADK TGAGERGARG IVALLGPNNK 250
    AERIVVIYLR DTPASMAERN QQIAGIGAAL IEHWQR 286
    Length:286
    Mass (Da):31,166
    Last modified:May 1, 2000 - v1
    Checksum:i5EA9990BC8B0AAFF
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB023477 Genomic DNA. Translation: BAA84973.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB023477 Genomic DNA. Translation: BAA84973.1 .

    3D structure databases

    ProteinModelPortali Q9S169.
    SMRi Q9S169. Positions 22-286.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    SABIO-RK Q9S169.

    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. "A new SHV-derived extended-spectrum beta-lactamase (SHV-24) that hydrolyzes ceftazidime through a single-amino-acid substitution (D179G) in the omega-loop."
      Kurokawa H., Yagi T., Shibata N., Shibayama K., Kamachi K., Arakawa Y.
      Antimicrob. Agents Chemother. 44:1725-1727(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
      Strain: HKY453.

    Entry informationi

    Entry nameiBLA24_ECOLX
    AccessioniPrimary (citable) accession number: Q9S169
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 54 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3