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P62593

- BLAT_ECOLX

UniProt

P62593 - BLAT_ECOLX

Protein

Beta-lactamase TEM

Gene

bla

more
Organism
Escherichia coli
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 82 (01 Oct 2014)
      Sequence version 1 (21 Jul 1986)
      Previous versions | rss
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    • Comment

    Functioni

    TEM-type are the most prevalent beta-lactamases in enterobacteria; they hydrolyze the beta-lactam bond in susceptible beta-lactam antibiotics, thus conferring resistance to penicillins and cephalosporins. TEM-3 and TEM-4 are capable of hydrolyzing cefotaxime and ceftazidime. TEM-5 is capable of hydrolyzing ceftazidime. TEM-6 is capable of hydrolyzing ceftazidime and aztreonam. TEM-8/CAZ-2, TEM-16/CAZ-7 and TEM-24/CAZ-6 are markedly active against ceftazidime. IRT-4 shows resistance to beta-lactamase inhibitors.

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei68 – 681Acyl-ester intermediate
    Active sitei166 – 1661Proton acceptor

    GO - Molecular functioni

    1. beta-lactamase activity Source: UniProtKB-EC
    2. protein binding Source: IntAct

    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-RKP62593.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Beta-lactamase TEM (EC:3.5.2.6)
    Alternative name(s):
    IRT-4
    Penicillinase
    TEM-1
    TEM-16/CAZ-7
    TEM-2
    TEM-24/CAZ-6
    TEM-3
    TEM-4
    TEM-5
    TEM-6
    TEM-8/CAZ-2
    Gene namesi
    Name:bla
    AND
    Name:blaT-3
    AND
    Name:blaT-4
    AND
    Name:blaT-5
    AND
    Name:blaT-6
    Encoded oniPlasmid R1 (R7268)2 Publications
    Plasmid IncFII R100 (NR1)1 Publication
    Plasmid R6K1 Publication
    Plasmid pUD161 Publication
    Plasmid pCFF042 Publications
    Plasmid pCFF140 Publication
    OrganismiEscherichia coli
    Taxonomic identifieri562 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

    Pathology & Biotechi

    Biotechnological usei

    This protein is used as a marker in many commonly used cloning vectors, such as pBR322 and the pUC series.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 23232 PublicationsAdd
    BLAST
    Chaini24 – 286263Beta-lactamase TEMPRO_0000016978Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi75 ↔ 121

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    PRIDEiP62593.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    P358042EBI-1031989,EBI-1031985From a different organism.

    Protein-protein interaction databases

    IntActiP62593. 1 interaction.

    Structurei

    Secondary structure

    1
    286
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi25 – 3814
    Beta strandi40 – 489
    Turni49 – 513
    Beta strandi54 – 596
    Helixi67 – 693
    Helixi70 – 8314
    Helixi97 – 993
    Helixi107 – 1093
    Turni111 – 1133
    Helixi117 – 12610
    Helixi130 – 13910
    Helixi143 – 15210
    Helixi166 – 1683
    Turni171 – 1733
    Helixi181 – 19313
    Beta strandi194 – 1974
    Helixi199 – 21012
    Beta strandi213 – 2153
    Turni216 – 2183
    Helixi219 – 2224
    Beta strandi228 – 2358
    Turni237 – 2393
    Beta strandi241 – 2499
    Beta strandi250 – 2523
    Beta strandi255 – 2639
    Beta strandi264 – 2663
    Helixi268 – 28417

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1AXBX-ray2.00A24-286[»]
    1BT5X-ray1.80A24-286[»]
    1BTLX-ray1.80A24-286[»]
    1CK3X-ray2.28A24-284[»]
    1ERMX-ray1.70A24-286[»]
    1EROX-ray2.10A24-286[»]
    1ERQX-ray1.90A24-286[»]
    1ESUX-ray2.00A24-284[»]
    1FQGX-ray1.70A24-286[»]
    1JTDX-ray2.30A24-286[»]
    1JTGX-ray1.73A/C24-286[»]
    1JVJX-ray1.73A24-286[»]
    1JWPX-ray1.75A24-286[»]
    1JWVX-ray1.85A24-286[»]
    1JWZX-ray1.80A24-286[»]
    1LHYX-ray2.00A24-284[»]
    1LI0X-ray1.61A24-284[»]
    1LI9X-ray1.52A24-284[»]
    1M40X-ray0.85A24-286[»]
    1NXYX-ray1.60A24-286[»]
    1NY0X-ray1.75A24-286[»]
    1NYMX-ray1.20A24-286[»]
    1NYYX-ray1.90A24-286[»]
    1PZOX-ray1.90A24-284[»]
    1PZPX-ray1.45A24-284[»]
    1S0WX-ray2.30A/B24-286[»]
    1TEMX-ray1.95A24-286[»]
    1XPBX-ray1.90A24-286[»]
    1XXMX-ray1.90A/B24-286[»]
    1YT4X-ray1.40A24-284[»]
    1ZG4X-ray1.55A1-284[»]
    1ZG6X-ray2.10A1-284[»]
    2B5RX-ray1.65A/B24-286[»]
    2V1ZX-ray1.60A25-286[»]
    2V20X-ray1.67A25-286[»]
    3C7UX-ray2.20A/C24-286[»]
    3C7VX-ray2.07A/C24-286[»]
    3CMZX-ray1.92A24-286[»]
    3DTMX-ray2.00A24-286[»]
    3JYIX-ray2.70A/B/C/D/E/F24-286[»]
    3TOIX-ray1.90A/B39-283[»]
    4DXBX-ray2.29A/B24-286[»]
    4DXCX-ray2.30A24-286[»]
    4GKUX-ray1.92A24-286[»]
    4IBRX-ray2.20A24-286[»]
    4IBXX-ray2.68A/B/C/D/E24-286[»]
    4ID4X-ray1.05A24-147[»]
    A185-286[»]
    ProteinModelPortaliP62593.
    SMRiP62593. Positions 24-286.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP62593.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni232 – 2343Substrate 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.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P62593-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSIQHFRVAL IPFFAAFCLP VFAHPETLVK VKDAEDQLGA RVGYIELDLN    50
    SGKILESFRP EERFPMMSTF KVLLCGAVLS RVDAGQEQLG RRIHYSQNDL 100
    VEYSPVTEKH LTDGMTVREL CSAAITMSDN TAANLLLTTI GGPKELTAFL 150
    HNMGDHVTRL DRWEPELNEA IPNDERDTTM PAAMATTLRK LLTGELLTLA 200
    SRQQLIDWME ADKVAGPLLR SALPAGWFIA DKSGAGERGS RGIIAALGPD 250
    GKPSRIVVIY TTGSQATMDE RNRQIAEIGA SLIKHW 286
    Length:286
    Mass (Da):31,515
    Last modified:July 21, 1986 - v1
    Checksum:iBB678943BB18934B
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti19 – 191L → F in TEM-4.
    Natural varianti37 – 371Q → K in TEM-2, TEM-3, TEM-8, TEM-16 and TEM-24.
    Natural varianti67 – 671M → L in IRT-4.
    Natural varianti102 – 1021E → K in TEM-3, TEM-4, TEM-6, TEM-8, TEM-16 and TEM-24.
    Natural varianti162 – 1621R → H in TEM-6 and TEM-16.
    Natural varianti162 – 1621R → S in TEM-5, TEM-8 and TEM-24.
    Natural varianti235 – 2351A → T in TEM-5 and TEM-24.
    Natural varianti236 – 2361G → S in TEM-3, TEM-4 and TEM-8.
    Natural varianti237 – 2371E → K in TEM-5 and TEM-24.
    Natural varianti261 – 2611T → M in TEM-4.
    Natural varianti272 – 2721N → D in IRT-4.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J01749 Genomic DNA. Translation: AAB59737.1.
    V00613 Genomic DNA. Translation: CAA23886.1.
    X64523 Genomic DNA. Translation: CAA45828.1.
    X57972 Genomic DNA. Translation: CAA41038.1.
    X65252 Genomic DNA. Translation: CAA46344.1.
    X65253 Genomic DNA. Translation: CAA46345.1.
    X65254 Genomic DNA. Translation: CAA46346.1.
    U89928 Genomic DNA. Translation: AAB64386.1.
    U66885 Genomic DNA. Translation: AAC48875.1.
    PIRiA93821. PNECP.
    S30113.
    RefSeqiNP_943295.1. NC_005248.1.
    NP_957565.1. NC_005327.1.
    YP_001096393.1. NC_009132.1.
    YP_001693174.1. NC_010378.1.
    YP_001816609.1. NC_010558.1.
    YP_003108102.1. NC_013120.1.
    YP_003108210.1. NC_013121.1.
    YP_003829069.1. NC_014383.1.
    YP_003829170.1. NC_014384.1.
    YP_003937675.1. NC_014615.1.
    YP_004119720.1. NC_014843.1.
    YP_004119734.1. NC_014843.1.
    YP_006903139.1. NC_019047.1.
    YP_006939984.1. NC_018994.1.
    YP_006940092.1. NC_018995.1.
    YP_006952181.1. NC_019056.1.
    YP_006952421.1. NC_019062.1.
    YP_006952427.1. NC_019063.1.
    YP_006953479.1. NC_019073.1.
    YP_006953762.1. NC_019088.1.
    YP_006953988.1. NC_019091.1.
    YP_006954235.1. NC_019095.1.
    YP_007447512.1. NC_020278.2.
    YP_008766498.1. NC_022742.1.
    YP_008864019.1. NC_022992.1.
    YP_008864686.1. NC_022996.1.
    YP_008995211.1. NC_023277.2.
    YP_190222.1. NC_006671.1.

    Genome annotation databases

    GeneIDi10076131.
    10076142.
    13876868.
    13877052.
    13903673.
    13905334.
    13905363.
    13906404.
    13906709.
    13906924.
    13909533.
    13909568.
    14612524.
    17500215.
    17824300.
    17824435.
    18157686.
    2716540.
    3244915.
    3722457.
    4924718.
    5961992.
    6276043.
    8319064.
    8319163.
    9537966.
    9538101.
    9846067.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J01749 Genomic DNA. Translation: AAB59737.1 .
    V00613 Genomic DNA. Translation: CAA23886.1 .
    X64523 Genomic DNA. Translation: CAA45828.1 .
    X57972 Genomic DNA. Translation: CAA41038.1 .
    X65252 Genomic DNA. Translation: CAA46344.1 .
    X65253 Genomic DNA. Translation: CAA46345.1 .
    X65254 Genomic DNA. Translation: CAA46346.1 .
    U89928 Genomic DNA. Translation: AAB64386.1 .
    U66885 Genomic DNA. Translation: AAC48875.1 .
    PIRi A93821. PNECP.
    S30113.
    RefSeqi NP_943295.1. NC_005248.1.
    NP_957565.1. NC_005327.1.
    YP_001096393.1. NC_009132.1.
    YP_001693174.1. NC_010378.1.
    YP_001816609.1. NC_010558.1.
    YP_003108102.1. NC_013120.1.
    YP_003108210.1. NC_013121.1.
    YP_003829069.1. NC_014383.1.
    YP_003829170.1. NC_014384.1.
    YP_003937675.1. NC_014615.1.
    YP_004119720.1. NC_014843.1.
    YP_004119734.1. NC_014843.1.
    YP_006903139.1. NC_019047.1.
    YP_006939984.1. NC_018994.1.
    YP_006940092.1. NC_018995.1.
    YP_006952181.1. NC_019056.1.
    YP_006952421.1. NC_019062.1.
    YP_006952427.1. NC_019063.1.
    YP_006953479.1. NC_019073.1.
    YP_006953762.1. NC_019088.1.
    YP_006953988.1. NC_019091.1.
    YP_006954235.1. NC_019095.1.
    YP_007447512.1. NC_020278.2.
    YP_008766498.1. NC_022742.1.
    YP_008864019.1. NC_022992.1.
    YP_008864686.1. NC_022996.1.
    YP_008995211.1. NC_023277.2.
    YP_190222.1. NC_006671.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AXB X-ray 2.00 A 24-286 [» ]
    1BT5 X-ray 1.80 A 24-286 [» ]
    1BTL X-ray 1.80 A 24-286 [» ]
    1CK3 X-ray 2.28 A 24-284 [» ]
    1ERM X-ray 1.70 A 24-286 [» ]
    1ERO X-ray 2.10 A 24-286 [» ]
    1ERQ X-ray 1.90 A 24-286 [» ]
    1ESU X-ray 2.00 A 24-284 [» ]
    1FQG X-ray 1.70 A 24-286 [» ]
    1JTD X-ray 2.30 A 24-286 [» ]
    1JTG X-ray 1.73 A/C 24-286 [» ]
    1JVJ X-ray 1.73 A 24-286 [» ]
    1JWP X-ray 1.75 A 24-286 [» ]
    1JWV X-ray 1.85 A 24-286 [» ]
    1JWZ X-ray 1.80 A 24-286 [» ]
    1LHY X-ray 2.00 A 24-284 [» ]
    1LI0 X-ray 1.61 A 24-284 [» ]
    1LI9 X-ray 1.52 A 24-284 [» ]
    1M40 X-ray 0.85 A 24-286 [» ]
    1NXY X-ray 1.60 A 24-286 [» ]
    1NY0 X-ray 1.75 A 24-286 [» ]
    1NYM X-ray 1.20 A 24-286 [» ]
    1NYY X-ray 1.90 A 24-286 [» ]
    1PZO X-ray 1.90 A 24-284 [» ]
    1PZP X-ray 1.45 A 24-284 [» ]
    1S0W X-ray 2.30 A/B 24-286 [» ]
    1TEM X-ray 1.95 A 24-286 [» ]
    1XPB X-ray 1.90 A 24-286 [» ]
    1XXM X-ray 1.90 A/B 24-286 [» ]
    1YT4 X-ray 1.40 A 24-284 [» ]
    1ZG4 X-ray 1.55 A 1-284 [» ]
    1ZG6 X-ray 2.10 A 1-284 [» ]
    2B5R X-ray 1.65 A/B 24-286 [» ]
    2V1Z X-ray 1.60 A 25-286 [» ]
    2V20 X-ray 1.67 A 25-286 [» ]
    3C7U X-ray 2.20 A/C 24-286 [» ]
    3C7V X-ray 2.07 A/C 24-286 [» ]
    3CMZ X-ray 1.92 A 24-286 [» ]
    3DTM X-ray 2.00 A 24-286 [» ]
    3JYI X-ray 2.70 A/B/C/D/E/F 24-286 [» ]
    3TOI X-ray 1.90 A/B 39-283 [» ]
    4DXB X-ray 2.29 A/B 24-286 [» ]
    4DXC X-ray 2.30 A 24-286 [» ]
    4GKU X-ray 1.92 A 24-286 [» ]
    4IBR X-ray 2.20 A 24-286 [» ]
    4IBX X-ray 2.68 A/B/C/D/E 24-286 [» ]
    4ID4 X-ray 1.05 A 24-147 [» ]
    A 185-286 [» ]
    ProteinModelPortali P62593.
    SMRi P62593. Positions 24-286.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P62593. 1 interaction.

    Chemistry

    BindingDBi P62593.
    ChEMBLi CHEMBL2364670.

    Proteomic databases

    PRIDEi P62593.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 10076131.
    10076142.
    13876868.
    13877052.
    13903673.
    13905334.
    13905363.
    13906404.
    13906709.
    13906924.
    13909533.
    13909568.
    14612524.
    17500215.
    17824300.
    17824435.
    18157686.
    2716540.
    3244915.
    3722457.
    4924718.
    5961992.
    6276043.
    8319064.
    8319163.
    9537966.
    9538101.
    9846067.

    Enzyme and pathway databases

    SABIO-RK P62593.

    Miscellaneous databases

    EvolutionaryTracei P62593.

    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.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequence of the ampicillin resistance gene of Escherichia coli plasmid pBR322."
      Sutcliffe J.G.
      Proc. Natl. Acad. Sci. U.S.A. 75:3737-3741(1978) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (TEM-1).
      Transposon: Tn3.
      Plasmid: R1 (R7268)
    2. "Complete nucleotide sequence of the Escherichia coli plasmid pBR322."
      Sutcliffe J.G.
      Cold Spring Harb. Symp. Quant. Biol. 43:77-90(1979) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (TEM-1).
      Transposon: Tn3.
      Plasmid: R1 (R7268)
    3. "DNA replication of the resistance plasmid R100 and its control."
      Ohtsubo H., Ryder T.B., Maeda Y., Armstrong K., Ohtsubo E.
      Adv. Biophys. 21:115-133(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (TEM-1).
      Plasmid: IncFII R100 (NR1)
    4. "Partial amino acid sequence of penicillinase coded by Escherichia coli plasmid R6K."
      Ambler R.P., Scott G.K.
      Proc. Natl. Acad. Sci. U.S.A. 75:3732-3736(1978) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 24-286 (TEM-2).
      Transposon: Tn1.
      Plasmid: R6K
    5. "The TEM-3 beta-lactamase, which hydrolyzes broad-spectrum cephalosporins, is derived from the TEM-2 penicillinase by two amino acid substitutions."
      Sougakoff W., Goussard S., Courvalin P.
      FEMS Microbiol. Lett. 56:343-348(1988)
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (TEM-3).
    6. "A new example of physical linkage between Tn1 and Tn21: the antibiotic multiple-resistance region of plasmid pCFF04 encoding extended-spectrum beta-lactamase TEM-3."
      Mabilat C., Lourencao-Vital J., Goussard S., Courvalin P.
      Mol. Gen. Genet. 235:113-121(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (TEM-3).
      Plasmid: pCFF04
    7. "Characterization of the plasmid genes blaT-4 and blaT-5 which encode the broad-spectrum beta-lactamases TEM-4 and TEM-5 in enterobacteriaceae."
      Sougakoff W., Petit A., Goussard S., Sirot D., Bure A., Courvalin P.
      Gene 78:339-348(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (TEM-4 AND TEM-5).
      Strain: CB86134.
      Plasmid: pCFF04 pUD16
    8. "An IS1-like element is responsible for high-level synthesis of extended-spectrum beta-lactamase TEM-6 in Enterobacteriaceae."
      Goussard S., Sougakoff W., Mabilat C., Bauernfeind A., Courvalin P.
      J. Gen. Microbiol. 137:2681-2687(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (TEM-6).
      Strain: HB251.
    9. "Nucleotide sequences of CAZ-2, CAZ-6, and CAZ-7 beta-lactamase genes."
      Chanal C., Poupart M.C., Sirot D., Labia R., Sirot J., Cluzel R.
      Antimicrob. Agents Chemother. 36:1817-1820(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (TEM-8; TEM-16 AND TEM-24).
    10. "Characterization and amino acid sequence of IRT-4, a novel TEM-type enzyme with a decreased susceptibility to beta-lactamase inhibitors."
      Brun T., Peduzzi J., Canica M.M., Paul G., Nevot P., Barthelemy M., Labia R.
      FEMS Microbiol. Lett. 120:111-117(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 24-286 (IRT-4).
      Strain: PEY.
    11. "Beta-lactamase TEM1 of E. coli. Crystal structure determination at 2.5-A resolution."
      Jelsch C., Lenfant F., Masson J.-M., Samama J.-P.
      FEBS Lett. 299:135-142(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF TEM-1.
    12. "Crystal structure of Escherichia coli TEM1 beta-lactamase at 1.8-A resolution."
      Jelsch C., Mourey L., Masson J.-M., Samama J.-P.
      Proteins 16:364-383(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF TEM-1.
    13. "A potent new mode of beta-lactamase inhibition revealed by the 1.7 A X-ray crystallographic structure of the TEM-1-BLIP complex."
      Strynadka N.C.J., Jensen S.E., Alzari P.M., James M.N.G.
      Nat. Struct. Biol. 3:290-297(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF TEM-1 COMPLEXED WITH BLIP.
    14. "Crystal structure of an acylation transition-state analog of the TEM-1 beta-lactamase. Mechanistic implications for class A beta-lactamases."
      Maveyraud L., Pratt R.F., Samama J.-P.
      Biochemistry 37:2622-2628(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF TEM-1.
    15. "X-ray structure of the Asn276Asp variant of the Escherichia coli TEM-1 beta-lactamase: direct observation of electrostatic modulation in resistance to inactivation by clavulanic acid."
      Swaren P., Golemi D., Cabantous S., Bulychev A., Maveyraud L., Mobashery S., Samama J.-P.
      Biochemistry 38:9570-9576(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) OF TEM-1.

    Entry informationi

    Entry nameiBLAT_ECOLX
    AccessioniPrimary (citable) accession number: P62593
    Secondary accession number(s): P00810, Q47313
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 82 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The beta-lactamase present on pBR322 was cloned from plasmid R1 (R7268).

    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