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P00807

- BLAC_STAAU

UniProt

P00807 - BLAC_STAAU

Protein

Beta-lactamase

Gene

blaZ

Organism
Staphylococcus aureus
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 111 (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 sitei63 – 631Acyl-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-RKP00807.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Beta-lactamase (EC:3.5.2.6)
    Alternative name(s):
    Penicillinase
    Gene namesi
    Name:blaZ
    Encoded oniPlasmid pI2582 Publications
    OrganismiStaphylococcus aureus
    Taxonomic identifieri1280 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus

    Pathology & Biotechi

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 24241 PublicationPROSITE-ProRule annotationAdd
    BLAST
    Chaini25 – 281257Beta-lactamasePRO_0000017020Add
    BLAST

    Proteomic databases

    PRIDEiP00807.

    Interactioni

    Structurei

    Secondary structure

    1
    281
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi26 – 338
    Beta strandi37 – 448
    Turni45 – 473
    Beta strandi50 – 545
    Helixi62 – 643
    Helixi65 – 7612
    Helixi79 – 835
    Beta strandi85 – 884
    Helixi90 – 923
    Helixi100 – 1034
    Beta strandi106 – 1094
    Helixi110 – 12011
    Helixi123 – 13311
    Helixi136 – 14510
    Helixi159 – 1613
    Beta strandi170 – 1723
    Helixi174 – 18411
    Beta strandi187 – 1904
    Helixi192 – 20413
    Helixi206 – 2083
    Turni209 – 2113
    Helixi212 – 2154
    Beta strandi220 – 2289
    Beta strandi230 – 2323
    Beta strandi235 – 2428
    Beta strandi250 – 2578
    Helixi267 – 27812

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1ALQX-ray1.80A24-244[»]
    1BLCX-ray2.20A25-281[»]
    1BLHX-ray2.30A25-281[»]
    1BLPX-ray2.30A25-281[»]
    1DJAX-ray1.90A25-281[»]
    1DJBX-ray2.10A25-281[»]
    1DJCX-ray2.00A25-281[»]
    1GHIX-ray2.30A25-281[»]
    1GHMX-ray1.86A25-281[»]
    1GHPX-ray1.76A25-281[»]
    1KGEX-ray2.00A25-281[»]
    1KGFX-ray2.20A25-281[»]
    1KGGX-ray2.30A24-281[»]
    1OMEX-ray2.30A/B25-281[»]
    1PIOX-ray2.80A/B25-281[»]
    3BLMX-ray2.00A25-281[»]
    ProteinModelPortaliP00807.
    SMRiP00807. Positions 25-281.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00807.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni225 – 2273Substrate 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.

    P00807-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKKLIFLIVI ALVLSACNSN SSHAKELNDL EKKYNAHIGV YALDTKSGKE    50
    VKFNSDKRFA YASTSKAINS AILLEQVPYN KLNKKVHINK DDIVAYSPIL 100
    EKYVGKDITL KALIEASMTY SDNTANNKII KEIGGIKKVK QRLKELGDKV 150
    TNPVRYEIEL NYYSPKSKKD TSTPAAFGKT LNKLIANGKL SKENKKFLLD 200
    LMLNNKSGDT LIKDGVPKDY KVADKSGQAI TYASRNDVAF VYPKGQSEPI 250
    VLVIFTNKDN KSDKPNDKLI SETAKSVMKE F 281
    Length:281
    Mass (Da):31,349
    Last modified:July 21, 1986 - v1
    Checksum:iF82A836773C275FE
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X04121 Genomic DNA. Translation: CAA27733.1.
    X16471 Genomic DNA. Translation: CAA34491.1.
    M15526 Genomic DNA. Translation: AAA98239.1.
    X52734 Genomic DNA. Translation: CAA36953.1.
    PIRiA01002. PNSAP.
    RefSeqiNP_878023.1. NC_005054.1.
    YP_003329488.1. NC_013550.1.
    YP_006937602.1. NC_013319.1.
    YP_006937751.1. NC_013323.1.
    YP_006938263.1. NC_013337.1.
    YP_006938770.1. NC_013352.1.
    YP_008709799.1. NC_022598.1.

    Genome annotation databases

    GeneIDi13874750.
    13874903.
    13875430.
    13875951.
    17363239.
    2598287.
    8655740.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X04121 Genomic DNA. Translation: CAA27733.1 .
    X16471 Genomic DNA. Translation: CAA34491.1 .
    M15526 Genomic DNA. Translation: AAA98239.1 .
    X52734 Genomic DNA. Translation: CAA36953.1 .
    PIRi A01002. PNSAP.
    RefSeqi NP_878023.1. NC_005054.1.
    YP_003329488.1. NC_013550.1.
    YP_006937602.1. NC_013319.1.
    YP_006937751.1. NC_013323.1.
    YP_006938263.1. NC_013337.1.
    YP_006938770.1. NC_013352.1.
    YP_008709799.1. NC_022598.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1ALQ X-ray 1.80 A 24-244 [» ]
    1BLC X-ray 2.20 A 25-281 [» ]
    1BLH X-ray 2.30 A 25-281 [» ]
    1BLP X-ray 2.30 A 25-281 [» ]
    1DJA X-ray 1.90 A 25-281 [» ]
    1DJB X-ray 2.10 A 25-281 [» ]
    1DJC X-ray 2.00 A 25-281 [» ]
    1GHI X-ray 2.30 A 25-281 [» ]
    1GHM X-ray 1.86 A 25-281 [» ]
    1GHP X-ray 1.76 A 25-281 [» ]
    1KGE X-ray 2.00 A 25-281 [» ]
    1KGF X-ray 2.20 A 25-281 [» ]
    1KGG X-ray 2.30 A 24-281 [» ]
    1OME X-ray 2.30 A/B 25-281 [» ]
    1PIO X-ray 2.80 A/B 25-281 [» ]
    3BLM X-ray 2.00 A 25-281 [» ]
    ProteinModelPortali P00807.
    SMRi P00807. Positions 25-281.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    BindingDBi P00807.
    ChEMBLi CHEMBL4114.
    DrugBanki DB00766. Clavulanate.
    DB01598. Imipenem.

    Proteomic databases

    PRIDEi P00807.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 13874750.
    13874903.
    13875430.
    13875951.
    17363239.
    2598287.
    8655740.

    Enzyme and pathway databases

    SABIO-RK P00807.

    Miscellaneous databases

    EvolutionaryTracei P00807.

    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. "Nucleotide sequence of the Staphylococcus aureus PC1 beta-lactamase gene."
      Chan P.T.
      Nucleic Acids Res. 14:5940-5940(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: PC-1.
      Plasmid: pI258
    2. "Nucleotide sequence of the blaZ gene of the Staphylococcus aureus beta-lactamase transposon Tn4002."
      Gillspie M.T., Skurray R.A.
      Nucleic Acids Res. 17:8854-8854(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: SK456.
      Transposon: Tn4002.
    3. "Tn552, a novel transposable element from Staphylococcus aureus."
      Rowland S.J., Dyke K.G.H.
      Mol. Microbiol. 4:961-975(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: NCTC 9789.
      Transposon: Tn552.
    4. "Nucleotide sequence and expression of the beta-lactamase gene from Staphylococcus aureus plasmid pI258 in Escherichia coli, Bacillus subtilis, and Staphylococcus aureus."
      Wang P.-Z., Novick R.P.
      J. Bacteriol. 169:1763-1766(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Plasmid: pI258
    5. "Unique features in the ribosome binding site sequence of the Gram-positive Staphylococcus aureus beta-lactamase gene."
      McLaughlin J.R., Murray C.L., Rabinowitz J.C.
      J. Biol. Chem. 256:11283-11291(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-47.
    6. "The amino acid sequence of Staphylococcus aureus penicillinase."
      Ambler R.P.
      Biochem. J. 151:197-218(1975) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 25-281.
    7. "Bacterial resistance to beta-lactam antibiotics: crystal structure of beta-lactamase from Staphylococcus aureus PC1 at 2.5-A resolution."
      Herzberg O., Moult J.
      Science 236:694-701(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
    8. "Refined crystal structure of beta-lactamase from Staphylococcus aureus PC1 at 2.0-A resolution."
      Herzberg O.
      J. Mol. Biol. 217:701-719(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
    9. "Role of the omega-loop in the activity, substrate specificity, and structure of class A beta-lactamase."
      Banerjee S., Pieper U., Kapadia G., Pannell L.K., Herzberg O.
      Biochemistry 37:3286-3296(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
    10. "Relocation of the catalytic carboxylate group in class A beta-lactamase: the structure and function of the mutant enzyme Glu166-->Gln:Asn170-->Asp."
      Chen C.C., Herzberg O.
      Protein Eng. 12:573-579(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).

    Entry informationi

    Entry nameiBLAC_STAAU
    AccessioniPrimary (citable) accession number: P00807
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 111 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, 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