UniProtKB - P03615 (CAPSD_BPQBE)
Capsid protein
Functioni
Capsid protein self-assembles to form an icosahedral capsid with a T=3 symmetry, about 26 nm in diameter, and consisting of 89 capsid proteins dimers (178 capsid proteins) (PubMed:27671640, PubMed:19913556).
Involved in viral genome encapsidation through the interaction between a capsid protein dimer and the multiple packaging signals present in the RNA genome (PubMed:8943226, PubMed:27671640).
Binding of the capsid proteins to the viral RNA induces a conformational change required for efficient T=3 shell formation (PubMed:19913556).
The capsid contains also 1 copy of the A2 maturation protein (PubMed:27671640).
3 PublicationsActs as a translational repressor of viral replicase synthesis late in infection. This latter function is the result of capsid protein interaction with an RNA hairpin which contains the replicase ribosome-binding site.
1 PublicationSites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 90 | RNA-binding1 Publication | 1 |
GO - Molecular functioni
- RNA binding Source: UniProtKB
- structural molecule activity Source: InterPro
- translation repressor activity Source: UniProtKB
Keywordsi
Molecular function | RNA-binding |
Biological process | Translation regulation |
Names & Taxonomyi
Protein namesi | Recommended name: Capsid proteinShort name: CP Alternative name(s): Coat protein |
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 |
|
Subcellular locationi
- Virion 2 Publications Note: The shell is composed of 89 dimers of the capsid protein, one of them being sequestered inside the virion, and 1 copy of the maturation protein.2 Publications
Keywords - Cellular componenti
Capsid protein, T=3 icosahedral capsid protein, VirionPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 33 | V → A: Decreased RNA-binding to the viral operator and loss of repressor activity. 1 Publication | 1 | |
Mutagenesisi | 50 | T → A: Decreased RNA-binding to the viral operator and loss of repressor activity. 1 Publication | 1 | |
Mutagenesisi | 57 | S → P: Decreased RNA-binding to the viral operator and loss of repressor activity. 1 Publication | 1 | |
Mutagenesisi | 60 | R → C: Decreased RNA-binding to the viral operator and loss of repressor activity. 1 Publication | 1 | |
Mutagenesisi | 62 | N → D: Decreased RNA-binding to the viral operator and loss of repressor activity. 1 Publication | 1 | |
Mutagenesisi | 64 | K → E: Decreased RNA-binding to the viral operator and loss of repressor activity. 1 Publication | 1 | |
Mutagenesisi | 90 | Y → H: Decreased RNA-binding to the viral operator and loss of repressor activity. 1 Publication | 1 | |
Mutagenesisi | 96 | S → L: Decreased RNA-binding to the viral operator and loss of repressor activity. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | Removed; by host1 Publication | |||
ChainiPRO_0000164846 | 2 – 133 | Capsid proteinAdd BLAST | 132 |
Interactioni
Subunit structurei
Homodimer (PubMed:16531233). The homodimers binds to the viral RNA via an operator hairpin, but also to many other RNA sequences in the viral genome; this interaction probably shifts the virus from the replicative to the assembly phase and ensures specific encapsidation of the viral genome (PubMed:8943226, PubMed:16531233).
Interacts with the maturation protein A2 (PubMed:28111107, PubMed:29078304).
4 PublicationsStructurei
Secondary structure
3D structure databases
SMRi | P03615 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P03615 |
Family & Domainsi
Family and domain databases
Gene3Di | 3.30.380.10, 1 hit |
InterProi | View protein in InterPro IPR002703, Levivir_coat IPR015954, Phage_RNA-type_capsid |
Pfami | View protein in Pfam PF01819, Levi_coat, 1 hit |
SUPFAMi | SSF55405, SSF55405, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
10 20 30 40 50
MAKLETVTLG NIGKDGKQTL VLNPRGVNPT NGVASLSQAG AVPALEKRVT
60 70 80 90 100
VSVSQPSRNR KNYKVQVKIQ NPTACTANGS CDPSVTRQAY ADVTFSFTQY
110 120 130
STDEERAFVR TELAALLASP LLIDAIDQLN PAY
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 23 | N → D AA sequence (PubMed:5570434).Curated | 1 | |
Sequence conflicti | 57 | Missing AA sequence (PubMed:5570434).Curated | 1 |
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural varianti | 34 | A → S in strain: Qbeta_3_FR. 1 Publication | 1 | |
Natural varianti | 76 | T → A in strain: QB_1 and Qbeta_1_FR. 2 Publications | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M99039 Unassigned DNA Translation: AAA16662.1 AY099114 Genomic RNA Translation: AAM33126.1 GQ153928 Genomic RNA Translation: ACY07224.1 GQ153929 Genomic RNA Translation: ACY07228.1 GQ153930 Genomic RNA Translation: ACY07232.1 GQ153931 Genomic RNA Translation: ACY07236.1 JF719735 Genomic RNA Translation: AEQ25542.1 JF719736 Genomic RNA Translation: AEQ25546.1 JF719737 Genomic RNA Translation: AEQ25550.1 AB971354 Genomic RNA Translation: BAP18764.1 V00643 mRNA Translation: CAA23992.1 |
PIRi | A92240, VCBPQB |
Similar proteinsi
Cross-referencesi
Web resourcesi
Virus Particle ExploreR db Icosahedral capsid structure |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M99039 Unassigned DNA Translation: AAA16662.1 AY099114 Genomic RNA Translation: AAM33126.1 GQ153928 Genomic RNA Translation: ACY07224.1 GQ153929 Genomic RNA Translation: ACY07228.1 GQ153930 Genomic RNA Translation: ACY07232.1 GQ153931 Genomic RNA Translation: ACY07236.1 JF719735 Genomic RNA Translation: AEQ25542.1 JF719736 Genomic RNA Translation: AEQ25546.1 JF719737 Genomic RNA Translation: AEQ25550.1 AB971354 Genomic RNA Translation: BAP18764.1 V00643 mRNA Translation: CAA23992.1 |
PIRi | A92240, VCBPQB |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1QBE | X-ray | 3.50 | A/B/C | 2-133 | [»] | |
4L8H | X-ray | 2.40 | A/B | 2-133 | [»] | |
5KIP | electron microscopy | 3.70 | A/B/C | 1-133 | [»] | |
5VLY | electron microscopy | 3.30 | A/B/C | 1-133 | [»] | |
5VLZ | electron microscopy | 4.40 | AA/AB/AC/AD/AE/AF/AG/AH/AI/AJ/AK/AL/AM/AN/BA/BB/BC/BD/BE/BF/BG/BH/BI/BJ/BK/BL/BM/BN/CA/CB | 1-133 | [»] | |
7LGE | electron microscopy | 5.60 | A/B/C/D | 1-133 | [»] | |
7LGF | electron microscopy | 6.10 | A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U | 1-133 | [»] | |
7LGG | electron microscopy | 6.20 | A/B/C/D/E/F/G/H/I/J/K/L/M/N/O | 1-133 | [»] | |
7LGH | electron microscopy | 8.90 | A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V | 1-133 | [»] | |
7LHD | electron microscopy | 4.60 | B/BA/BB/BC/BD/BE/BF/BG/BH/BI/BJ/BK/BL/BM/BN/CA/CB/CC/CD/CE/CF/CG/CH/CI/CJ/CK/CL/CM/CN/D | 1-133 | [»] | |
SMRi | P03615 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P03615 |
Family and domain databases
Gene3Di | 3.30.380.10, 1 hit |
InterProi | View protein in InterPro IPR002703, Levivir_coat IPR015954, Phage_RNA-type_capsid |
Pfami | View protein in Pfam PF01819, Levi_coat, 1 hit |
SUPFAMi | SSF55405, SSF55405, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | CAPSD_BPQBE | |
Accessioni | P03615Primary (citable) accession number: P03615 Secondary accession number(s): D0U1F3, G4WZR7, Q774G0 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 21, 1986 |
Last sequence update: | January 23, 2007 | |
Last modified: | May 25, 2022 | |
This is version 102 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, Direct protein sequencing, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references