位置:首页 > 蛋白库 > CAPSD_BPH75
CAPSD_BPH75
ID   CAPSD_BPH75             Reviewed;          46 AA.
AC   P82889;
DT   29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   29-AUG-2001, sequence version 1.
DT   02-JUN-2021, entry version 82.
DE   RecName: Full=Capsid protein G8P;
DE   AltName: Full=Coat protein B;
DE   AltName: Full=Gene 8 protein;
DE            Short=G8P;
DE   AltName: Full=Major coat protein;
GN   Name=VIII;
OS   Thermus phage PH75 (Bacteriophage PH75).
OC   Viruses; Monodnaviria; Loebvirae; Hofneiviricota; Faserviricetes;
OC   Tubulavirales; Inoviridae; unclassified Inoviridae.
OX   NCBI_TaxID=144736;
OH   NCBI_TaxID=274; Thermus thermophilus.
RN   [1]
RP   PROTEIN SEQUENCE, X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS), AND FORMYLATION AT
RP   MET-1.
RX   PubMed=11371161; DOI=10.1006/jmbi.2001.4685;
RA   Pederson D.M., Welsh L.C., Marvin D.A., Sampson M., Perham R.N., Yu M.,
RA   Slater M.R.;
RT   "The protein capsid of filamentous bacteriophage PH75 from Thermus
RT   thermophilus.";
RL   J. Mol. Biol. 309:401-421(2001).
CC   -!- FUNCTION: Self assembles to form a helical capsid wrapping up the viral
CC       genomic DNA. The capsid displays a filamentous structure with a length
CC       of 760-1950 nm and a width of 6-8 nm. The virion assembly and budding
CC       take place at the host inner membrane (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homomultimerizes. There are several thousands of this protein
CC       in the phage capsid (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000305}. Host membrane; Single-pass
CC       membrane protein. Note=prior to assembly, the major capsid protein is
CC       found associated with the bacterial host inner membrane. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the inovirus capsid protein family.
CC       {ECO:0000305}.
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   PDB; 1HGV; Fiber; 2.40 A; A=1-46.
DR   PDB; 1HGZ; Fiber; 2.40 A; A=1-46.
DR   PDB; 1HH0; Fiber; 2.40 A; A=1-46.
DR   PDBsum; 1HGV; -.
DR   PDBsum; 1HGZ; -.
DR   PDBsum; 1HH0; -.
DR   SMR; P82889; -.
DR   EvolutionaryTrace; P82889; -.
DR   GO; GO:0019029; C:helical viral capsid; IEA:UniProtKB-KW.
DR   GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.5.80; -; 1.
DR   InterPro; IPR023390; Phage_M13_G8P_capsid_dom_sf.
PE   1: Evidence at protein level;
KW   3D-structure; Capsid protein; Direct protein sequencing; Formylation;
KW   Helical capsid protein; Host membrane; Membrane; Transmembrane;
KW   Transmembrane helix; Virion.
FT   CHAIN           1..46
FT                   /note="Capsid protein G8P"
FT                   /id="PRO_0000098233"
FT   TOPO_DOM        1..17
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        18..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        38..46
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         1
FT                   /note="N-formylmethionine; by host"
FT                   /evidence="ECO:0000269|PubMed:11371161"
FT   HELIX           6..13
FT                   /evidence="ECO:0007829|PDB:1HGV"
FT   TURN            14..16
FT                   /evidence="ECO:0007829|PDB:1HGV"
FT   HELIX           17..42
FT                   /evidence="ECO:0007829|PDB:1HGV"
FT   HELIX           43..45
FT                   /evidence="ECO:0007829|PDB:1HH0"
SQ   SEQUENCE   46 AA;  4813 MW;  1E2EBFA950C7ACBE CRC64;
     MDFNPSEVAS QVTNYIQAIA AAGVGVLALA IGLSAAWKYA KRFLKG
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2025