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P00573

- RPOL_BPT7

UniProt

P00573 - RPOL_BPT7

Protein

T7 RNA polymerase

Gene

1

Organism
Enterobacteria phage T7 (Bacteriophage T7)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 120 (01 Oct 2014)
      Sequence version 2 (11 Jan 2001)
      Previous versions | rss
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    Functioni

    Highly processive DNA-dependent RNA polymerase that catalyzes the transcription of class II and class III viral genes. Recognizes a specific promoter sequence and enters first into an "abortive phase" where very short transcripts are synthesized and released before proceeding to the processive transcription of long RNA chains. Unwinds the double-stranded DNA to expose the coding strand for templating. Participates in the initiation of viral DNA replication presumably by making primers accessible to the DNA polymerase, thus facilitating the DNA opening. Plays also a role in viral DNA packaging, probably by pausing the transcripiton at the right end of concatemer junction to allow packaging complex recruitment and beginning of the packaging process.5 Publications

    Catalytic activityi

    Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).PROSITE-ProRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei537 – 5371
    Active sitei631 – 63111 Publication
    Active sitei812 – 8121

    GO - Molecular functioni

    1. DNA binding Source: InterPro
    2. DNA-directed RNA polymerase activity Source: UniProtKB-KW

    GO - Biological processi

    1. transcription, DNA-templated Source: InterPro

    Keywords - Molecular functioni

    Nucleotidyltransferase, Transferase

    Keywords - Biological processi

    Transcription

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    T7 RNA polymerase
    Alternative name(s):
    DNA-directed RNA polymerase (EC:2.7.7.6)
    Gene namesi
    Ordered Locus Names:1
    OrganismiEnterobacteria phage T7 (Bacteriophage T7)
    Taxonomic identifieri10760 [NCBI]
    Taxonomic lineageiVirusesdsDNA viruses, no RNA stageCaudoviralesPodoviridaeAutographivirinaeT7likevirus
    Virus hostiEscherichia coli [TaxID: 562]
    ProteomesiUP000000840: Genome

    Subcellular locationi

    Keywords - Cellular componenti

    DNA-directed RNA polymerase

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi172 – 1721K → L or G: No change in activity. 1 Publication
    Mutagenesisi563 – 5631P → A or T: Inactivated.
    Mutagenesisi571 – 5711Y → S: Inactivated.
    Mutagenesisi631 – 6311K → G: Partially inactivated. 1 Publication
    Mutagenesisi631 – 6311K → L: Partially inactivated. 1 Publication
    Mutagenesisi631 – 6311K → R: Partially inactivated. 1 Publication
    Mutagenesisi636 – 6361T → P: Inactivated.
    Mutagenesisi639 – 6391Y → D: Inactivated.
    Mutagenesisi646 – 6461F → C: Inactivated.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 883883T7 RNA polymerasePRO_0000087749Add
    BLAST

    Proteomic databases

    PRIDEiP00573.

    Miscellaneous databases

    PMAP-CutDBP00573.

    Interactioni

    Subunit structurei

    Monomer. Interacts with T7 lysozyme; this interaction inhibits transcriptional function of T7 RNA polymerase.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    3.5P008061EBI-1026948,EBI-1026942

    Protein-protein interaction databases

    DIPiDIP-6091N.
    IntActiP00573. 1 interaction.
    MINTiMINT-1513587.

    Structurei

    Secondary structure

    1
    883
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi7 – 104
    Helixi12 – 143
    Helixi18 – 247
    Turni25 – 284
    Helixi30 – 5930
    Turni60 – 623
    Helixi64 – 663
    Turni68 – 703
    Helixi71 – 9424
    Turni101 – 1077
    Helixi111 – 12818
    Beta strandi129 – 1313
    Helixi134 – 15623
    Helixi162 – 1654
    Helixi168 – 1725
    Helixi176 – 18914
    Turni191 – 1988
    Turni205 – 2073
    Helixi208 – 22316
    Beta strandi227 – 2304
    Beta strandi231 – 2333
    Turni237 – 2393
    Beta strandi243 – 2464
    Helixi248 – 26114
    Beta strandi271 – 2733
    Beta strandi279 – 2835
    Beta strandi285 – 2884
    Beta strandi289 – 2913
    Beta strandi295 – 2984
    Helixi304 – 3074
    Turni308 – 3103
    Helixi314 – 32411
    Beta strandi328 – 3303
    Helixi332 – 34110
    Beta strandi344 – 3463
    Beta strandi348 – 3514
    Beta strandi365 – 3684
    Turni370 – 3723
    Helixi374 – 3774
    Helixi379 – 40224
    Turni403 – 4053
    Beta strandi406 – 4105
    Beta strandi418 – 4214
    Beta strandi422 – 4243
    Beta strandi426 – 4327
    Beta strandi434 – 4363
    Helixi438 – 4436
    Beta strandi444 – 4485
    Helixi453 – 46715
    Helixi475 – 48410
    Helixi486 – 4949
    Helixi496 – 4994
    Helixi501 – 5044
    Beta strandi505 – 5073
    Helixi508 – 52417
    Helixi525 – 5273
    Beta strandi528 – 5303
    Beta strandi534 – 5374
    Helixi541 – 55010
    Helixi555 – 5584
    Beta strandi559 – 5646
    Helixi570 – 58617
    Beta strandi594 – 5963
    Beta strandi597 – 6026
    Beta strandi605 – 6106
    Helixi613 – 6219
    Helixi627 – 6359
    Helixi636 – 6394
    Helixi643 – 65311
    Helixi655 – 6606
    Turni662 – 6665
    Helixi670 – 68819
    Helixi690 – 70718
    Turni713 – 7153
    Beta strandi718 – 7203
    Beta strandi725 – 7284
    Turni730 – 7323
    Beta strandi734 – 7374
    Beta strandi740 – 7467
    Beta strandi747 – 7493
    Beta strandi750 – 7523
    Beta strandi755 – 7573
    Beta strandi760 – 76910
    Helixi771 – 80131
    Beta strandi807 – 8093
    Beta strandi811 – 8166
    Helixi818 – 8203
    Helixi821 – 83818
    Helixi841 – 8499
    Turni852 – 8543
    Turni855 – 8584
    Beta strandi859 – 8613
    Helixi872 – 8765
    Turni879 – 8813

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1AROX-ray2.80P1-883[»]
    1CEZX-ray2.40A1-883[»]
    1H38X-ray2.90A/B/C/D1-883[»]
    1MSWX-ray2.10D1-883[»]
    1QLNX-ray2.40A1-883[»]
    1S0VX-ray3.20A/B/C/D1-883[»]
    1S76X-ray2.88D1-883[»]
    1S77X-ray2.69D1-883[»]
    2PI4X-ray2.50A6-883[»]
    2PI5X-ray2.90A6-883[»]
    3E2EX-ray3.00A1-883[»]
    3E3JX-ray6.70B/C1-883[»]
    4RNPX-ray3.00A/B/C1-883[»]
    ProteinModelPortaliP00573.
    SMRiP00573. Positions 6-883.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00573.

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi380 – 3834Poly-Ala

    Sequence similaritiesi

    Family and domain databases

    Gene3Di1.10.1320.10. 1 hit.
    1.10.287.260. 1 hit.
    InterProiIPR024075. DNA-dir_RNA_pol_helix_hairpin.
    IPR002092. DNA-dir_Rpol_phage-type.
    IPR029262. RPOL_N.
    [Graphical view]
    PANTHERiPTHR10102. PTHR10102. 1 hit.
    PfamiPF00940. RNA_pol. 1 hit.
    PF14700. RPOL_N. 1 hit.
    [Graphical view]
    PROSITEiPS00900. RNA_POL_PHAGE_1. 1 hit.
    PS00489. RNA_POL_PHAGE_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P00573-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNTINIAKND FSDIELAAIP FNTLADHYGE RLAREQLALE HESYEMGEAR    50
    FRKMFERQLK AGEVADNAAA KPLITTLLPK MIARINDWFE EVKAKRGKRP 100
    TAFQFLQEIK PEAVAYITIK TTLACLTSAD NTTVQAVASA IGRAIEDEAR 150
    FGRIRDLEAK HFKKNVEEQL NKRVGHVYKK AFMQVVEADM LSKGLLGGEA 200
    WSSWHKEDSI HVGVRCIEML IESTGMVSLH RQNAGVVGQD SETIELAPEY 250
    AEAIATRAGA LAGISPMFQP CVVPPKPWTG ITGGGYWANG RRPLALVRTH 300
    SKKALMRYED VYMPEVYKAI NIAQNTAWKI NKKVLAVANV ITKWKHCPVE 350
    DIPAIEREEL PMKPEDIDMN PEALTAWKRA AAAVYRKDKA RKSRRISLEF 400
    MLEQANKFAN HKAIWFPYNM DWRGRVYAVS MFNPQGNDMT KGLLTLAKGK 450
    PIGKEGYYWL KIHGANCAGV DKVPFPERIK FIEENHENIM ACAKSPLENT 500
    WWAEQDSPFC FLAFCFEYAG VQHHGLSYNC SLPLAFDGSC SGIQHFSAML 550
    RDEVGGRAVN LLPSETVQDI YGIVAKKVNE ILQADAINGT DNEVVTVTDE 600
    NTGEISEKVK LGTKALAGQW LAYGVTRSVT KRSVMTLAYG SKEFGFRQQV 650
    LEDTIQPAID SGKGLMFTQP NQAAGYMAKL IWESVSVTVV AAVEAMNWLK 700
    SAAKLLAAEV KDKKTGEILR KRCAVHWVTP DGFPVWQEYK KPIQTRLNLM 750
    FLGQFRLQPT INTNKDSEID AHKQESGIAP NFVHSQDGSH LRKTVVWAHE 800
    KYGIESFALI HDSFGTIPAD AANLFKAVRE TMVDTYESCD VLADFYDQFA 850
    DQLHESQLDK MPALPAKGNL NLRDILESDF AFA 883
    Length:883
    Mass (Da):98,855
    Last modified:January 11, 2001 - v2
    Checksum:i7FBDEAC457842549
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti388 – 42437DKARK…MDWRG → TRLASLAVSALSSCLSKPIS LLTIRPSGSLTTWTGAV(PubMed:7310873)CuratedAdd
    BLAST
    Sequence conflicti389 – 3891K → R in AAA32569. (PubMed:6093820)Curated
    Sequence conflicti443 – 4431L → R in CAA24333. (PubMed:7310873)Curated
    Sequence conflicti474 – 4741P → S in CAA24333. (PubMed:7310873)Curated
    Sequence conflicti623 – 6231Y → H in AAA32569. (PubMed:6093820)Curated
    Sequence conflicti665 – 6651L → P in AAA32569. (PubMed:6093820)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    V01146 Genomic DNA. Translation: CAA24390.1.
    V01127 Genomic DNA. Translation: CAA24333.1.
    M38308 Genomic DNA. Translation: AAA32569.1.
    PIRiA94615. RNBP17.
    RefSeqiNP_041960.1. NC_001604.1.

    Genome annotation databases

    GeneIDi1261050.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    V01146 Genomic DNA. Translation: CAA24390.1 .
    V01127 Genomic DNA. Translation: CAA24333.1 .
    M38308 Genomic DNA. Translation: AAA32569.1 .
    PIRi A94615. RNBP17.
    RefSeqi NP_041960.1. NC_001604.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1ARO X-ray 2.80 P 1-883 [» ]
    1CEZ X-ray 2.40 A 1-883 [» ]
    1H38 X-ray 2.90 A/B/C/D 1-883 [» ]
    1MSW X-ray 2.10 D 1-883 [» ]
    1QLN X-ray 2.40 A 1-883 [» ]
    1S0V X-ray 3.20 A/B/C/D 1-883 [» ]
    1S76 X-ray 2.88 D 1-883 [» ]
    1S77 X-ray 2.69 D 1-883 [» ]
    2PI4 X-ray 2.50 A 6-883 [» ]
    2PI5 X-ray 2.90 A 6-883 [» ]
    3E2E X-ray 3.00 A 1-883 [» ]
    3E3J X-ray 6.70 B/C 1-883 [» ]
    4RNP X-ray 3.00 A/B/C 1-883 [» ]
    ProteinModelPortali P00573.
    SMRi P00573. Positions 6-883.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-6091N.
    IntActi P00573. 1 interaction.
    MINTi MINT-1513587.

    Chemistry

    BindingDBi P00573.
    ChEMBLi CHEMBL1075072.

    Proteomic databases

    PRIDEi P00573.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 1261050.

    Miscellaneous databases

    EvolutionaryTracei P00573.
    PMAP-CutDB P00573.

    Family and domain databases

    Gene3Di 1.10.1320.10. 1 hit.
    1.10.287.260. 1 hit.
    InterProi IPR024075. DNA-dir_RNA_pol_helix_hairpin.
    IPR002092. DNA-dir_Rpol_phage-type.
    IPR029262. RPOL_N.
    [Graphical view ]
    PANTHERi PTHR10102. PTHR10102. 1 hit.
    Pfami PF00940. RNA_pol. 1 hit.
    PF14700. RPOL_N. 1 hit.
    [Graphical view ]
    PROSITEi PS00900. RNA_POL_PHAGE_1. 1 hit.
    PS00489. RNA_POL_PHAGE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Complete nucleotide sequence of bacteriophage T7 DNA and the locations of T7 genetic elements."
      Dunn J.J., Studier F.W.
      J. Mol. Biol. 166:477-535(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    2. "Nucleotide sequence of the gene for bacteriophage T7 RNA polymerase."
      Moffatt B.A., Dunn J.J., Studier F.W.
      J. Mol. Biol. 173:265-269(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION.
    3. "Nucleotide sequence of the cloned gene for bacteriophage T7 RNA polymerase."
      Stahl S.J., Zinn K.
      J. Mol. Biol. 148:481-485(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "Phage T7 RNA-polymerase: gene cloning and its structure."
      Grachev M.A., Pletnev A.G.
      Bioorg. Khim. 10:824-843(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. "Nucleotide sequence from the genetic left end of bacteriophage T7 DNA to the beginning of gene 4."
      Dunn J.J., Studier F.W.
      J. Mol. Biol. 148:303-330(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-59 AND 829-883.
    6. "Evidence for direct involvement of T7 RNA polymerase bacteriophage DNA replication."
      Hinkle D.C.
      J. Virol. 34:136-141(1980) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN DNA REPLICATION.
    7. "Initiation of DNA replication at the primary origin of bacteriophage T7 by purified proteins: requirement for T7 RNA polymerase."
      Romano L.J., Tamanoi F., Richardson C.C.
      Proc. Natl. Acad. Sci. U.S.A. 78:4107-4111(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN DNA REPLICATION.
    8. "Processivity in early stages of transcription by T7 RNA polymerase."
      Martin C.T., Muller D.K., Coleman J.E.
      Biochemistry 27:3966-3974(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "Lys631 residue in the active site of the bacteriophage T7 RNA polymerase. Affinity labeling and site-directed mutagenesis."
      Maksimova T.G., Mustayev A.A., Zaychikov E.F., Lyakhov D.L., Tunitskaya V.L., Akbarov A.K., Luchin S.V., Rechinsky V.O., Chernov B.K., Kochetkov S.N.
      Eur. J. Biochem. 195:841-847(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACTIVE SITE LYS-631, MUTAGENESIS OF LYS-631.
    10. "Site-specific mutagenesis of residue Lys-172 of phage T7 RNA polymerase: characterization of transcription properties of mutant proteins."
      Lyakhov D.L., Ilgenfrits H., Chernov B.K., Dragan S.M., Rechinsky V.O., Pokholok D.K., Tunitskaya V.L., Kochetkov S.N.
      Mol. Biol. (Mosk.) 26:1022-1035(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF LYS-172.
    11. "Random mutagenesis of the gene for bacteriophage T7 RNA polymerase."
      Rechinsky V.O., Kostyuk D.A., Lyakhov D.L., Chernov B.K., Kochetkov S.N.
      Mol. Gen. Genet. 238:455-458(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS.
    12. "Tyr-571 is involved in the T7 RNA polymerase binding to its promoter."
      Rechinsky V.O., Tunitskaya V.L., Dragan S.M., Kostyuk D.A., Kochetkov S.N.
      FEBS Lett. 320:9-12(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS.
    13. "Bacteriophage T7 RNA polymerase and its active-site mutants. Kinetic, spectroscopic and calorimetric characterization."
      Osumi-Davis P., Sreerama N., Volkin D.B., Middaugh C.R., Woody R.W., Woody A.-Y.M.
      J. Mol. Biol. 237:5-19(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS.
    14. "Mechanism of inhibition of bacteriophage T7 RNA polymerase by T7 lysozyme."
      Zhang X., Studier F.W.
      J. Mol. Biol. 269:10-27(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    15. "Multiple roles of T7 RNA polymerase and T7 lysozyme during bacteriophage T7 infection."
      Zhang X., Studier F.W.
      J. Mol. Biol. 340:707-730(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    16. "Crystal structure of bacteriophage T7 RNA polymerase at 3.3-A resolution."
      Sousa R., Chung Y.J., Rose J.P., Wang B.-C.
      Nature 364:593-599(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS).
    17. "Structure of T7 RNA polymerase complexed to the transcriptional inhibitor T7 lysozyme."
      Jeruzalmi D., Steitz T.A.
      EMBO J. 17:4101-4113(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF COMPLEX WITH LYSOZYME.

    Entry informationi

    Entry nameiRPOL_BPT7
    AccessioniPrimary (citable) accession number: P00573
    Secondary accession number(s): Q38543
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 11, 2001
    Last modified: October 1, 2014
    This is version 120 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    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