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P00573

- RPOL_BPT7

UniProt

P00573 - RPOL_BPT7

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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

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).

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
Complete GO annotation...

GO - Biological processi

  1. transcription, DNA-templated Source: InterPro
Complete GO annotation...

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 polymerase
PRO_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

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.

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti388 – 42437DKARK…MDWRG → TRLASLAVSALSSCLSKPIS LLTIRPSGSLTTWTGAV1 Publication
Add
BLAST
Sequence conflicti389 – 3891K → R in AAA32569. 1 Publication
Sequence conflicti443 – 4431L → R in CAA24333. 1 Publication
Sequence conflicti474 – 4741P → S in CAA24333. 1 Publication
Sequence conflicti623 – 6231Y → H in AAA32569. 1 Publication
Sequence conflicti665 – 6651L → P in AAA32569. 1 Publication

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...

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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 119 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

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