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UniProtKB - P14647 (RDRP_BPQBE)
Protein
RNA-directed RNA polymerase subunit beta
Gene
N/A
Organism
Escherichia virus Qbeta (Bacteriophage Q-beta)
Status
Functioni
This is the catalytic subunit of the viral RNA-dependent RNA polymerase complex. This complex is involved in viral RNA replication that produces (+)-stranded genomes via a complementary, (-)-stranded intermediate. Binds RNA cooperatively with the host ribosomal protein S1.
9 PublicationsMiscellaneous
In order to produce high amounts of RNA polymerase catalytic core, a fusion protein consisting of tsf-tufB-replicase with a cleavable linker between tufB and the viral replicase subunit is frequently used.5 Publications
Catalytic activityi
- a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)PROSITE-ProRule annotation1 PublicationEC:2.7.7.48PROSITE-ProRule annotation1 Publication
Cofactori
Mg2+3 PublicationsNote: Binds 2 Mg2+ per subunit, Ca2+ is used in crystallization to prevent RNA polymerase activity.3 Publications
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 274 | Magnesium 13 Publications | 1 | |
Metal bindingi | 274 | Magnesium 23 Publications | 1 | |
Metal bindingi | 359 | Magnesium 13 Publications | 1 | |
Metal bindingi | 359 | Magnesium 23 Publications | 1 | |
Metal bindingi | 360 | Magnesium 13 Publications | 1 | |
Metal bindingi | 360 | Magnesium 23 Publications | 1 |
GO - Molecular functioni
- metal ion binding Source: UniProtKB-KW
- nucleotide binding Source: UniProtKB-KW
- RNA binding Source: UniProtKB-KW
- RNA-directed 5'-3' RNA polymerase activity Source: UniProtKB-KW
GO - Biological processi
- viral RNA genome replication Source: InterPro
Keywordsi
Molecular function | Nucleotidyltransferase, RNA-binding, RNA-directed RNA polymerase, Transferase |
Biological process | Viral RNA replication |
Ligand | Magnesium, Metal-binding, Nucleotide-binding |
Names & Taxonomyi
Protein namesi | Recommended name: RNA-directed RNA polymerase subunit beta (EC:2.7.7.481 Publication)Alternative name(s): RNA replicase beta chain RNA-directed RNA polymerase subunit II1 Publication |
Organismi | Escherichia virus Qbeta (Bacteriophage Q-beta) |
Taxonomic identifieri | 39803 [NCBI] |
Taxonomic lineagei | Viruses › Riboviria › Orthornavirae › Lenarviricota › Allassoviricetes › Levivirales › Leviviridae › Allolevivirus |
Virus hosti | Escherichia coli [TaxID: 562] |
Proteomesi |
|
Pathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 78 | K → A: Loss of RNA polymerase activity. 1 Publication | 1 | |
Mutagenesisi | 132 | R → M: Complete loss of infectivity; when associated with M-133. 1 Publication | 1 | |
Mutagenesisi | 133 | R → M: Complete loss of infectivity; when associated with M-132. 1 Publication | 1 | |
Mutagenesisi | 134 | K → A: Complete loss of infectivity. 1 Publication | 1 | |
Mutagenesisi | 137 | K → M: Complete loss of infectivity. 1 Publication | 1 | |
Mutagenesisi | 153 | R → A: Loss of RNA polymerase activity. 1 Publication | 1 | |
Mutagenesisi | 164 | R → A: 80% loss of RNA polymerase activity. 1 Publication | 1 | |
Mutagenesisi | 168 | H → A: 80% loss of RNA polymerase activity. 1 Publication | 1 | |
Mutagenesisi | 214 | K → A: Loss of RNA polymerase activity. 1 Publication | 1 | |
Mutagenesisi | 220 | R → A: Loss of RNA polymerase activity. 1 Publication | 1 | |
Mutagenesisi | 241 | R → A: Decreased initiation of RNA polymerase activity. 1 Publication | 1 | |
Mutagenesisi | 274 | D → A: Loss of RNA polymerase activity. 1 Publication | 1 | |
Mutagenesisi | 279 | S → A: Loss of RNA polymerase activity. 1 Publication | 1 | |
Mutagenesisi | 329 | F → A: Decreased initiation of RNA polymerase activity. 1 Publication | 1 | |
Mutagenesisi | 345 | E → A: Almost complete loss of infectivity. 1 Publication | 1 | |
Mutagenesisi | 348 | D → A: 80% loss of infectivity. 1 Publication | 1 | |
Mutagenesisi | 350 | D → A: 95% loss of infectivity. 1 Publication | 1 | |
Mutagenesisi | 357 | Y → A: Decreased initiation of RNA polymerase activity. 2 Publications | 1 | |
Mutagenesisi | 359 | D → A: Loss of RNA polymerase activity. 1 Publication | 1 | |
Mutagenesisi | 360 | D → A: Loss of RNA polymerase activity. 1 Publication | 1 | |
Mutagenesisi | 395 | E → A: Loss of RNA polymerase activity. 1 Publication | 1 | |
Mutagenesisi | 411 | Y → A: 60% loss of RNA polymerase activity. 1 Publication | 1 | |
Mutagenesisi | 413 | R → A: Loss of RNA polymerase activity. 1 Publication | 1 | |
Mutagenesisi | 511 | Y → A: 50% loss of RNA polymerase activity. 1 Publication | 1 | |
Mutagenesisi | 549 | N → A: 25% loss of RNA polymerase activity. 1 Publication | 1 | |
Mutagenesisi | 549 | N → G: 50% loss of RNA polymerase activity. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000164855 | 1 – 589 | RNA-directed RNA polymerase subunit betaAdd BLAST | 589 |
Interactioni
Subunit structurei
Homodimer; the replicase complex can dimerize. Part of the viral RNA-dependent RNA polymerase complex, the other subunits are the host ribosomal protein S1, EF-Tu and EF-Ts. S1 is needed for the initiation of genomic RNA (+)-strand replication.
9 PublicationsBinary interactionsi
P14647
With | #Exp. | IntAct |
---|---|---|
tsf [P0A6P1] from Escherichia coli (strain K12). | 2 | EBI-9010000,EBI-301164 |
tufA [P0CE47] from Escherichia coli (strain K12). | 2 | EBI-9010000,EBI-301077 |
Protein-protein interaction databases
DIPi | DIP-59375N |
IntActi | P14647, 2 interactors |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P14647 |
ModBasei | Search... |
PDBe-KBi | Search... |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 259 – 391 | RdRp catalyticPROSITE-ProRule annotationAdd BLAST | 133 |
Family and domain databases
InterProi | View protein in InterPro IPR043502, DNA/RNA_pol_sf IPR007096, RNA-dir_Rpol_phage_catalytic IPR005093, RNArep_beta |
Pfami | View protein in Pfam PF03431, RNA_replicase_B, 1 hit |
SUPFAMi | SSF56672, SSF56672, 1 hit |
PROSITEi | View protein in PROSITE PS50522, RDRP_PHAGE, 1 hit |
i Sequence
Sequence statusi: Complete.
P14647-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MSKTASSRNS LSAQLRRAAN TRIEVEGNLA LSIANDLLLA YGQSPFNSEA
60 70 80 90 100
ECISFSPRFD GTPDDFRINY LKAEIMSKYD DFSLGIDTEA VAWEKFLAAE
110 120 130 140 150
AECALTNARL YRPDYSEDFN FSLGESCIHM ARRKIAKLIG DVPSVEGMLR
160 170 180 190 200
HCRFSGGATT TNNRSYGHPS FKFALPQACT PRALKYVLAL RASTHFDIRI
210 220 230 240 250
SDISPFNKAV TVPKNSKTDR CIAIEPGWNM FFQLGIGGIL RDRLRCWGID
260 270 280 290 300
LNDQTINQRR AHEGSVTNNL ATVDLSAASD SISLALCELL LPPGWFEVLM
310 320 330 340 350
DLRSPKGRLP DGSVVTYEKI SSMGNGYTFE LESLIFASLA RSVCEILDLD
360 370 380 390 400
SSEVTVYGDD IILPSCAVPA LREVFKYVGF TTNTKKTFSE GPFRESCGKH
410 420 430 440 450
YYSGVDVTPF YIRHRIVSPA DLILVLNNLY RWATIDGVWD PRAHSVYLKY
460 470 480 490 500
RKLLPKQLQR NTIPDGYGDG ALVGSVLINP FAKNRGWIRY VPVITDHTRD
510 520 530 540 550
RERAELGSYL YDLFSRCLSE SNDGLPLRGP SGCDSADLFA IDQLICRSNP
560 570 580
TKISRSTGKF DIQYIACSSR VLAPYGVFQG TKVASLHEA
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural varianti | 71 | L → F in strain:QB_1. 1 Publication | 1 | |
Natural varianti | 130 | M → I in strain: QB_ancestral, QB_1, QB_2, Qbeta_1_FR and Qbeta_2_FR. 2 Publications | 1 | |
Natural varianti | 198 | I → T2 Publications | 1 | |
Natural varianti | 251 | L → R in strain:QB_1 and Qbeta_2_FR. 2 Publications | 1 | |
Natural varianti | 418 | S → G in strain:QB_1 and Qbeta_2_FR. 1 Publication | 1 | |
Natural varianti | 500 | D → G in strain:QB_2 and Qbeta_2_FR. 2 Publications | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X14764 mRNA Translation: CAA32872.1 AY099114 Genomic RNA Translation: AAM33128.1 GQ153928 Genomic RNA Translation: ACY07225.1 GQ153929 Genomic RNA Translation: ACY07229.1 AB971354 Genomic RNA Translation: BAP18765.1 JF719735 Genomic RNA Translation: AEQ25543.1 JF719736 Genomic RNA Translation: AEQ25547.1 GQ153931 Genomic RNA Translation: ACY07237.1 M24876 Genomic RNA Translation: AAA50307.1 |
PIRi | S03340, RRBPBQ |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X14764 mRNA Translation: CAA32872.1 AY099114 Genomic RNA Translation: AAM33128.1 GQ153928 Genomic RNA Translation: ACY07225.1 GQ153929 Genomic RNA Translation: ACY07229.1 AB971354 Genomic RNA Translation: BAP18765.1 JF719735 Genomic RNA Translation: AEQ25543.1 JF719736 Genomic RNA Translation: AEQ25547.1 GQ153931 Genomic RNA Translation: ACY07237.1 M24876 Genomic RNA Translation: AAA50307.1 |
PIRi | S03340, RRBPBQ |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
3AGP | X-ray | 2.80 | A | 1-589 | [»] | |
3AGQ | X-ray | 3.22 | A | 1-589 | [»] | |
3AVT | X-ray | 2.61 | A | 1-589 | [»] | |
3AVU | X-ray | 2.91 | A | 1-589 | [»] | |
3AVV | X-ray | 3.12 | A | 1-589 | [»] | |
3AVW | X-ray | 2.60 | A | 1-589 | [»] | |
3AVX | X-ray | 2.41 | A | 1-589 | [»] | |
3AVY | X-ray | 2.62 | A | 1-589 | [»] | |
3MMP | X-ray | 2.50 | F/G | 1-589 | [»] | |
3VNU | X-ray | 3.20 | A | 1-589 | [»] | |
3VNV | X-ray | 2.60 | A | 1-589 | [»] | |
4FWT | X-ray | 3.20 | A | 1-589 | [»] | |
4Q7J | X-ray | 2.90 | C/G | 2-589 | [»] | |
4R71 | X-ray | 3.21 | B/D | 1-589 | [»] | |
SMRi | P14647 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
DIPi | DIP-59375N |
IntActi | P14647, 2 interactors |
Family and domain databases
InterProi | View protein in InterPro IPR043502, DNA/RNA_pol_sf IPR007096, RNA-dir_Rpol_phage_catalytic IPR005093, RNArep_beta |
Pfami | View protein in Pfam PF03431, RNA_replicase_B, 1 hit |
SUPFAMi | SSF56672, SSF56672, 1 hit |
PROSITEi | View protein in PROSITE PS50522, RDRP_PHAGE, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | RDRP_BPQBE | |
Accessioni | P14647Primary (citable) accession number: P14647 Secondary accession number(s): D0U1F4 Q8LTE0 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | April 1, 1990 |
Last sequence update: | February 15, 2017 | |
Last modified: | September 29, 2021 | |
This is version 87 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Viral Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references