CAPSD_BPAL3
ID CAPSD_BPAL3 Reviewed; 431 AA.
AC P08767;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 2.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Capsid protein F;
DE AltName: Full=F protein;
DE AltName: Full=GPF;
GN Name=F;
OS Escherichia phage alpha3 (Bacteriophage alpha-3).
OC Viruses; Monodnaviria; Sangervirae; Phixviricota; Malgrandaviricetes;
OC Petitvirales; Microviridae; Bullavirinae; Alphatrevirus.
OX NCBI_TaxID=10849;
OH NCBI_TaxID=562; Escherichia coli.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1532908; DOI=10.1016/0167-4781(92)90440-b;
RA Kodaira K., Nakano K., Okada S., Taketo A.;
RT "Nucleotide sequence of the genome of the bacteriophage alpha 3:
RT interrelationship of the genome structure and the gene products with those
RT of the phages, phi X174, G4 and phi K.";
RL Biochim. Biophys. Acta 1130:277-288(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-13.
RX PubMed=6088949; DOI=10.1007/bf00341460;
RA Kodaira K., Taketo A.;
RT "Isolation and some properties of bacteriophage alpha3 gene J mutant.";
RL Mol. Gen. Genet. 195:541-543(1984).
RN [3] {ECO:0007744|PDB:1M06, ECO:0007744|PDB:1M0F}
RP X-RAY CRYSTALLOGRAPHY (3.50 ANGSTROMS).
RX PubMed=12473449; DOI=10.1016/s0022-2836(02)01201-9;
RA Bernal R.A., Hafenstein S., Olson N.H., Bowman V.D., Chipman P.R.,
RA Baker T.S., Fane B.A., Rossmann M.G.;
RT "Structural studies of bacteriophage alpha3 assembly.";
RL J. Mol. Biol. 325:11-24(2003).
CC -!- FUNCTION: Assembles to form an icosahedral capsid with a T=1 symmetry,
CC about 30 nm in diameter, and consisting of 60 capsid proteins F. Upon
CC virus binding to host cell, one of the spikes dissociates from the
CC capsid and the virus interacts with LPS through the exposed EF loops on
CC the F proteins. After the genome had been ejected, the channel formed
CC by the F proteins at the unique fivefold axis remains open.
CC {ECO:0000250|UniProtKB:P03641}.
CC -!- SUBUNIT: Pentamerizes and interacts with H protein, G and B pentamers
CC to form 12S pre-assembly complex. By binding with protein D, induces
CC joining of twelve 12S complex to form the procapsid. The procapsid has
CC an external scaffold made of 240 copies of protein D, 60 copies of the
CC internally located B protein, and contains 60 copies of each of the
CC viral structural proteins F and G. Upon genome packaging, interacts
CC with protein J. The mature virion is composed of 60 copies each of the
CC F, G, and J proteins, and 12 copies of the H protein.
CC {ECO:0000250|UniProtKB:P03641}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000250|UniProtKB:P03641}.
CC -!- SIMILARITY: Belongs to the microviridae F protein family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC structure;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1rb8";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X60322; CAA42881.1; -; Genomic_DNA.
DR EMBL; X00774; CAA25350.1; -; Genomic_DNA.
DR PIR; S22330; S22330.
DR RefSeq; NP_039597.1; NC_001330.1.
DR PDB; 1M06; X-ray; 3.50 A; F=1-431.
DR PDB; 1M0F; EM; 16.00 A; F=1-431.
DR PDB; 1RB8; X-ray; 3.50 A; F=1-431.
DR PDBsum; 1M06; -.
DR PDBsum; 1M0F; -.
DR PDBsum; 1RB8; -.
DR SMR; P08767; -.
DR GeneID; 1260697; -.
DR KEGG; vg:1260697; -.
DR EvolutionaryTrace; P08767; -.
DR Proteomes; UP000002137; Genome.
DR GO; GO:0039615; C:T=1 icosahedral viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR Gene3D; 2.60.169.10; -; 1.
DR InterPro; IPR016184; Capsid/spike_ssDNA_virus.
DR InterPro; IPR003514; Microviridae_protein_F.
DR InterPro; IPR037002; Microviridae_protein_F_sf.
DR Pfam; PF02305; Phage_F; 2.
DR SUPFAM; SSF88645; SSF88645; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Capsid protein; Reference proteome;
KW T=1 icosahedral capsid protein;
KW Viral genome ejection through host cell envelope;
KW Viral penetration into host cytoplasm; Virion; Virus entry into host cell.
FT INIT_MET 1
FT /note="Removed; by host"
FT /evidence="ECO:0000250|UniProtKB:P03641"
FT CHAIN 2..431
FT /note="Capsid protein F"
FT /id="PRO_0000164887"
FT STRAND 11..14
FT /evidence="ECO:0007829|PDB:1M06"
FT STRAND 17..23
FT /evidence="ECO:0007829|PDB:1M06"
FT STRAND 25..36
FT /evidence="ECO:0007829|PDB:1M06"
FT STRAND 41..52
FT /evidence="ECO:0007829|PDB:1M06"
FT STRAND 55..58
FT /evidence="ECO:0007829|PDB:1M06"
FT STRAND 63..73
FT /evidence="ECO:0007829|PDB:1M06"
FT HELIX 74..78
FT /evidence="ECO:0007829|PDB:1M06"
FT HELIX 80..88
FT /evidence="ECO:0007829|PDB:1M06"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:1M06"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:1M06"
FT TURN 104..107
FT /evidence="ECO:0007829|PDB:1M06"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:1M06"
FT STRAND 118..121
FT /evidence="ECO:0007829|PDB:1M06"
FT HELIX 122..135
FT /evidence="ECO:0007829|PDB:1M06"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:1M06"
FT HELIX 154..159
FT /evidence="ECO:0007829|PDB:1M06"
FT TURN 169..171
FT /evidence="ECO:0007829|PDB:1M06"
FT HELIX 193..212
FT /evidence="ECO:0007829|PDB:1M06"
FT HELIX 216..222
FT /evidence="ECO:0007829|PDB:1M06"
FT TURN 229..233
FT /evidence="ECO:0007829|PDB:1M06"
FT STRAND 236..245
FT /evidence="ECO:0007829|PDB:1M06"
FT STRAND 247..251
FT /evidence="ECO:0007829|PDB:1M06"
FT TURN 255..259
FT /evidence="ECO:0007829|PDB:1M06"
FT STRAND 261..277
FT /evidence="ECO:0007829|PDB:1M06"
FT STRAND 280..291
FT /evidence="ECO:0007829|PDB:1M06"
FT HELIX 302..305
FT /evidence="ECO:0007829|PDB:1M06"
FT HELIX 311..314
FT /evidence="ECO:0007829|PDB:1M06"
FT HELIX 318..321
FT /evidence="ECO:0007829|PDB:1M06"
FT STRAND 327..330
FT /evidence="ECO:0007829|PDB:1M06"
FT HELIX 331..333
FT /evidence="ECO:0007829|PDB:1M06"
FT STRAND 343..346
FT /evidence="ECO:0007829|PDB:1M06"
FT HELIX 350..352
FT /evidence="ECO:0007829|PDB:1M06"
FT HELIX 361..365
FT /evidence="ECO:0007829|PDB:1M06"
FT TURN 376..380
FT /evidence="ECO:0007829|PDB:1M06"
FT HELIX 384..388
FT /evidence="ECO:0007829|PDB:1M06"
FT HELIX 392..398
FT /evidence="ECO:0007829|PDB:1M06"
FT STRAND 406..419
FT /evidence="ECO:0007829|PDB:1M06"
FT HELIX 424..428
FT /evidence="ECO:0007829|PDB:1M06"
SQ SEQUENCE 431 AA; 49337 MW; 72B2ED90676E81C5 CRC64;
MSNVQTSAER EIVDLSHLAF DCGMLGRLKT VSWTPVIAGD SFELDAVGAL RLSPLRRGLA
IDSKVDFFTF YIPHRHVYGD QWIQFMRDGV NAQPLPSVTC NRYPDHAGYV GTIVPANNRI
PKFLHQSYLN IYNNYFRAPW MPERTEANPS NLNEDDARYR FRCCHLKNIW SAPLPPETKL
AEEMGIESNS IDIMGLQAAY AQLHTEQERT YFMQRYRDVI SSFGGSTSYD ADNRPLLVMH
TDFWASGYDV DGTDQSSLGQ FSGRVQQTFK HSVPRFFVPE HGVMMTLALI RFPPISPLEH
HYLAGKSQLT YTDLAGDPAL IGNLPPREIS YRDLFRDGRS GIKIKVAESI WYRTHPDYVN
FKYHDLHGFP FLDDAPGTST GDNLQEAILV RHQDYDACFQ SQQLLQWNKQ ARYNVSVYRH
MPTVRDSIMT S
