CAPSD_BPGA
ID CAPSD_BPGA Reviewed; 130 AA.
AC P07234;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Capsid protein;
DE Short=CP;
DE AltName: Full=Coat protein;
OS Enterobacteria phage GA (Bacteriophage GA).
OC Viruses; Riboviria; Orthornavirae; Lenarviricota; Leviviricetes;
OC Norzivirales; Fiersviridae; Emesvirus; Emesvirus japonicum.
OX NCBI_TaxID=12018;
OH NCBI_TaxID=562; Escherichia coli.
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3711059; DOI=10.1093/oxfordjournals.jbchem.a135580;
RA Inokuchi Y., Takahashi R., Hirose T., Inayama S., Jacobson A.B.,
RA Hirashima A.;
RT "The complete nucleotide sequence of the group II RNA coliphage GA.";
RL J. Biochem. 99:1169-1180(1986).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS).
RX PubMed=9299325; DOI=10.1006/jmbi.1997.1214;
RA Tars K., Bundule M., Fridborg K., Liljas L.;
RT "The crystal structure of bacteriophage GA and a comparison of
RT bacteriophages belonging to the major groups of Escherichia coli
RT leviviruses.";
RL J. Mol. Biol. 271:759-773(1997).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RX PubMed=8976557; DOI=10.1002/pro.5560051211;
RA Ni C.-Z., White C.A., Mitchell R.S., Wickersham J., Kodandapani R.,
RA Peabody D.S., Ely K.R.;
RT "Crystal structure of the coat protein from the GA bacteriophage: model of
RT the unassembled dimer.";
RL Protein Sci. 5:2485-2493(1996).
CC -!- FUNCTION: Capsid protein self-assembles to form an icosahedral capsid
CC with a T=3 symmetry, about 26 nm in diameter, and consisting of 89
CC capsid proteins dimers (178 capsid proteins). Involved in viral genome
CC encapsidation through the interaction between a capsid protein dimer
CC and the multiple packaging signals present in the RNA genome. The
CC capsid contains also 1 copy of the A2 maturation protein.
CC {ECO:0000250|UniProtKB:P03612}.
CC -!- FUNCTION: Acts as a translational repressor of viral replicase
CC synthesis late in infection. This latter function is the result of
CC capsid protein interaction with an RNA hairpin which contains the
CC replicase ribosome-binding site. {ECO:0000250|UniProtKB:P03612}.
CC -!- SUBUNIT: Homodimer. The capsid proteins form dimers that assemble by
CC group of 5. Twelve such pentamers are linked together with free dimers.
CC The homodimers binds to the viral RNA via an operator hairpin, but also
CC to many other RNA sequences in the viral genome; this interaction
CC probably shifts the virus from the replicative to the assembly phase
CC and ensures specific encapsidation of the viral genome.
CC {ECO:0000250|UniProtKB:P03612}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000250|UniProtKB:P03612}. Note=The
CC shell is composed of 178 copies of the capsid protein and 1 copy of the
CC maturation protein. {ECO:0000250|UniProtKB:P03612}.
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC structure with 4 residue deletion FG loop;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1gav";
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DR EMBL; X03869; CAA27497.1; -; mRNA.
DR PIR; A29178; VCBPGA.
DR PDB; 1GAV; X-ray; 3.40 A; 0/1/2/3/4/5/6/7/8/9/A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z/a/b/c/d/e/f/g/h/i=2-130.
DR PDB; 1UNA; X-ray; 2.80 A; A/B=2-130.
DR PDBsum; 1GAV; -.
DR PDBsum; 1UNA; -.
DR SMR; P07234; -.
DR EvolutionaryTrace; P07234; -.
DR Proteomes; UP000002126; Genome.
DR GO; GO:0039617; C:T=3 icosahedral viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR Gene3D; 3.30.380.10; -; 1.
DR InterPro; IPR002703; Levivir_coat.
DR InterPro; IPR015954; Phage_RNA-type_capsid.
DR Pfam; PF01819; Levi_coat; 1.
DR SUPFAM; SSF55405; SSF55405; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Capsid protein; Reference proteome; RNA-binding;
KW T=3 icosahedral capsid protein; Translation regulation; Virion.
FT INIT_MET 1
FT /note="Removed; by host"
FT /evidence="ECO:0000250|UniProtKB:P69171"
FT CHAIN 2..130
FT /note="Capsid protein"
FT /id="PRO_0000164841"
FT REGION 31..104
FT /note="Viral RNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P03612"
FT STRAND 7..10
FT /evidence="ECO:0007829|PDB:1UNA"
FT STRAND 12..16
FT /evidence="ECO:0007829|PDB:1UNA"
FT STRAND 18..24
FT /evidence="ECO:0007829|PDB:1UNA"
FT HELIX 26..28
FT /evidence="ECO:0007829|PDB:1UNA"
FT STRAND 30..36
FT /evidence="ECO:0007829|PDB:1UNA"
FT HELIX 38..40
FT /evidence="ECO:0007829|PDB:1UNA"
FT STRAND 43..51
FT /evidence="ECO:0007829|PDB:1UNA"
FT TURN 52..54
FT /evidence="ECO:0007829|PDB:1UNA"
FT STRAND 55..65
FT /evidence="ECO:0007829|PDB:1UNA"
FT STRAND 83..93
FT /evidence="ECO:0007829|PDB:1UNA"
FT HELIX 102..111
FT /evidence="ECO:0007829|PDB:1UNA"
FT HELIX 117..124
FT /evidence="ECO:0007829|PDB:1UNA"
SQ SEQUENCE 130 AA; 13683 MW; 4FBB64DCC866CDA9 CRC64;
MATLRSFVLV DNGGTGNVTV VPVSNANGVA EWLSNNSRSQ AYRVTASYRA SGADKRKYAI
KLEVPKIVTQ VVNGVELPGS AWKAYASIDL TIPIFAATDD VTVISKSLAG LFKVGNPIAE
AISSQSGFYA
