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P00573 (RPOL_BPT7) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
T7 RNA polymerase
Alternative name(s):
DNA-directed RNA polymerase
EC=2.7.7.6
Gene names
Ordered Locus Names:1
OrganismEnterobacteria phage T7 (Bacteriophage T7) [Reference proteome]
Taxonomic identifier10760 [NCBI]
Taxonomic lineageVirusesdsDNA viruses, no RNA stageCaudoviralesPodoviridaeAutographivirinaeT7likevirus
Virus hostEscherichia coli [TaxID: 562]

Protein attributes

Sequence length883 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.6 Ref.7 Ref.8 Ref.14 Ref.15

Catalytic activity

Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).

Subunit structure

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

Sequence similarities

Belongs to the phage and mitochondrial RNA polymerase family.

Ontologies

Keywords
   Biological processTranscription
   Cellular componentDNA-directed RNA polymerase
   Molecular functionNucleotidyltransferase
Transferase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processtranscription, DNA-templated

Inferred from electronic annotation. Source: InterPro

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: InterPro

DNA-directed RNA polymerase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

3.5P008061EBI-1026948,EBI-1026942

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 883883T7 RNA polymerase
PRO_0000087749

Regions

Compositional bias380 – 3834Poly-Ala

Sites

Active site5371
Active site6311 Ref.9
Active site8121

Experimental info

Mutagenesis1721K → L or G: No change in activity. Ref.10
Mutagenesis5631P → A or T: Inactivated.
Mutagenesis5711Y → S: Inactivated.
Mutagenesis6311K → G: Partially inactivated. Ref.9
Mutagenesis6311K → L: Partially inactivated. Ref.9
Mutagenesis6311K → R: Partially inactivated. Ref.9
Mutagenesis6361T → P: Inactivated.
Mutagenesis6391Y → D: Inactivated.
Mutagenesis6461F → C: Inactivated.
Sequence conflict388 – 42437DKARK…MDWRG → TRLASLAVSALSSCLSKPIS LLTIRPSGSLTTWTGAV Ref.3
Sequence conflict3891K → R in AAA32569. Ref.4
Sequence conflict4431L → R in CAA24333. Ref.3
Sequence conflict4741P → S in CAA24333. Ref.3
Sequence conflict6231Y → H in AAA32569. Ref.4
Sequence conflict6651L → P in AAA32569. Ref.4

Secondary structure

..................................................................................................................................................................... 883
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00573 [UniParc].

Last modified January 11, 2001. Version 2.
Checksum: 7FBDEAC457842549

FASTA88398,855
        10         20         30         40         50         60 
MNTINIAKND FSDIELAAIP FNTLADHYGE RLAREQLALE HESYEMGEAR FRKMFERQLK 

        70         80         90        100        110        120 
AGEVADNAAA KPLITTLLPK MIARINDWFE EVKAKRGKRP TAFQFLQEIK PEAVAYITIK 

       130        140        150        160        170        180 
TTLACLTSAD NTTVQAVASA IGRAIEDEAR FGRIRDLEAK HFKKNVEEQL NKRVGHVYKK 

       190        200        210        220        230        240 
AFMQVVEADM LSKGLLGGEA WSSWHKEDSI HVGVRCIEML IESTGMVSLH RQNAGVVGQD 

       250        260        270        280        290        300 
SETIELAPEY AEAIATRAGA LAGISPMFQP CVVPPKPWTG ITGGGYWANG RRPLALVRTH 

       310        320        330        340        350        360 
SKKALMRYED VYMPEVYKAI NIAQNTAWKI NKKVLAVANV ITKWKHCPVE DIPAIEREEL 

       370        380        390        400        410        420 
PMKPEDIDMN PEALTAWKRA AAAVYRKDKA RKSRRISLEF MLEQANKFAN HKAIWFPYNM 

       430        440        450        460        470        480 
DWRGRVYAVS MFNPQGNDMT KGLLTLAKGK PIGKEGYYWL KIHGANCAGV DKVPFPERIK 

       490        500        510        520        530        540 
FIEENHENIM ACAKSPLENT WWAEQDSPFC FLAFCFEYAG VQHHGLSYNC SLPLAFDGSC 

       550        560        570        580        590        600 
SGIQHFSAML RDEVGGRAVN LLPSETVQDI YGIVAKKVNE ILQADAINGT DNEVVTVTDE 

       610        620        630        640        650        660 
NTGEISEKVK LGTKALAGQW LAYGVTRSVT KRSVMTLAYG SKEFGFRQQV LEDTIQPAID 

       670        680        690        700        710        720 
SGKGLMFTQP NQAAGYMAKL IWESVSVTVV AAVEAMNWLK SAAKLLAAEV KDKKTGEILR 

       730        740        750        760        770        780 
KRCAVHWVTP DGFPVWQEYK KPIQTRLNLM FLGQFRLQPT INTNKDSEID AHKQESGIAP 

       790        800        810        820        830        840 
NFVHSQDGSH LRKTVVWAHE KYGIESFALI HDSFGTIPAD AANLFKAVRE TMVDTYESCD 

       850        860        870        880 
VLADFYDQFA DQLHESQLDK MPALPAKGNL NLRDILESDF AFA 

« Hide

References

« Hide 'large scale' references
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
V01146 Genomic DNA. Translation: CAA24390.1.
V01127 Genomic DNA. Translation: CAA24333.1.
M38308 Genomic DNA. Translation: AAA32569.1.
PIRRNBP17. A94615.
RefSeqNP_041960.1. NC_001604.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP00573.
SMRP00573. Positions 6-883.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-6091N.
IntActP00573. 1 interaction.
MINTMINT-1513587.

Chemistry

BindingDBP00573.
ChEMBLCHEMBL1075072.

Proteomic databases

PRIDEP00573.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1261050.

Family and domain databases

Gene3D1.10.1320.10. 1 hit.
1.10.287.260. 1 hit.
InterProIPR024075. DNA-dir_RNA_pol_helix_hairpin.
IPR002092. DNA-dir_Rpol_phage-type.
IPR029262. RPOL_N.
[Graphical view]
PANTHERPTHR10102. PTHR10102. 1 hit.
PfamPF00940. RNA_pol. 1 hit.
PF14700. RPOL_N. 1 hit.
[Graphical view]
PROSITEPS00900. RNA_POL_PHAGE_1. 1 hit.
PS00489. RNA_POL_PHAGE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP00573.
PMAP-CutDBP00573.

Entry information

Entry nameRPOL_BPT7
AccessionPrimary (citable) accession number: P00573
Secondary accession number(s): Q38543
Entry history
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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references