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CAPSD_BPM13
ID   CAPSD_BPM13             Reviewed;          73 AA.
AC   P69541; P03617;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   02-JUN-2021, entry version 91.
DE   RecName: Full=Capsid protein G8P;
DE   AltName: Full=Coat protein B;
DE   AltName: Full=Gene 8 protein;
DE            Short=G8P;
DE   AltName: Full=M13 procoat;
DE   AltName: Full=Major coat protein;
DE   Flags: Precursor;
GN   Name=VIII;
OS   Enterobacteria phage M13 (Bacteriophage M13).
OC   Viruses; Monodnaviria; Loebvirae; Hofneiviricota; Faserviricetes;
OC   Tubulavirales; Inoviridae; Inovirus.
OX   NCBI_TaxID=1977402;
OH   NCBI_TaxID=562; Escherichia coli.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6254849; DOI=10.1016/0378-1119(80)90093-1;
RA   van Wezenbeek P.M.G.F., Hulsebos T.J.M., Schoenmakers J.G.G.;
RT   "Nucleotide sequence of the filamentous bacteriophage M13 DNA genome:
RT   comparison with phage fd.";
RL   Gene 11:129-148(1980).
RN   [2]
RP   INSERTION IN MEMBRANE.
RX   PubMed=3317833; DOI=10.1126/science.3317833;
RA   Kuhn A.;
RT   "Bacteriophage M13 procoat protein inserts into the plasma membrane as a
RT   loop structure.";
RL   Science 238:1413-1415(1987).
RN   [3]
RP   MEMBRANE INSERTION DEPENDS ON YIDC.
RX   PubMed=10949305; DOI=10.1038/35020586;
RA   Samuelson J.C., Chen M., Jiang F., Moeller I., Wiedmann M., Kuhn A.,
RA   Phillips G.J., Dalbey R.E.;
RT   "YidC mediates membrane protein insertion in bacteria.";
RL   Nature 406:637-641(2000).
RN   [4]
RP   MEMBRANE INSERTION DEPENDS ON YIDC.
RX   PubMed=12707259; DOI=10.1074/jbc.m301008200;
RA   Chen M., Xie K., Nouwen N., Driessen A.J., Dalbey R.E.;
RT   "Conditional lethal mutations separate the M13 procoat and Pf3 coat
RT   functions of YidC: different YidC structural requirements for membrane
RT   protein insertion.";
RL   J. Biol. Chem. 278:23295-23300(2003).
RN   [5]
RP   STRUCTURE BY NMR.
RX   PubMed=1606152; DOI=10.1021/bi00138a007;
RA   Henry G.D., Sykes B.D.;
RT   "Assignment of amide 1H and 15N NMR resonances in detergent-solubilized M13
RT   coat protein: a model for the coat protein dimer.";
RL   Biochemistry 31:5284-5297(1992).
RN   [6]
RP   STRUCTURE BY NMR.
RX   PubMed=7556198; DOI=10.1111/j.1432-1033.1995.490zz.x;
RA   Papavoine C.H.M., Aelen J.M.A., Konings R.N.H., Hilbers C.W.,
RA   van de Ven F.J.M.;
RT   "NMR studies of the major coat protein of bacteriophage M13. Structural
RT   information of gVIIIp in dodecylphosphocholine micelles.";
RL   Eur. J. Biochem. 232:490-500(1995).
RN   [7]
RP   STRUCTURE BY NMR.
RX   PubMed=9735296; DOI=10.1006/jmbi.1998.1860;
RA   Papavoine C.H., Christiaans B.E., Folmer R.H., Konings R.N., Hilbers C.W.;
RT   "Solution structure of the M13 major coat protein in detergent micelles: a
RT   basis for a model of phage assembly involving specific residues.";
RL   J. Mol. Biol. 282:401-419(1998).
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.
CC   -!- SUBUNIT: Homomultimerizes. There are about 2,700 copies of this protein
CC       in the phage capsid.
CC   -!- SUBCELLULAR LOCATION: Virion. Host cell inner membrane; Single-pass
CC       type I membrane protein. Note=Insertion into the host inner membrane
CC       requires YidC but not the Sec translocon. Virion assembly occurs after
CC       insertion.
CC   -!- SIMILARITY: Belongs to the inovirus capsid protein family.
CC       {ECO:0000305}.
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DR   EMBL; V00604; CAA23861.1; -; Genomic_DNA.
DR   PIR; D04226; VCBPM3.
DR   PDB; 2CPB; NMR; -; A=24-73.
DR   PDB; 2CPS; NMR; -; A=24-73.
DR   PDB; 2MJZ; NMR; -; 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=24-73.
DR   PDBsum; 2CPB; -.
DR   PDBsum; 2CPS; -.
DR   PDBsum; 2MJZ; -.
DR   BMRB; P69541; -.
DR   SMR; P69541; -.
DR   EvolutionaryTrace; P69541; -.
DR   Proteomes; UP000002111; Genome.
DR   GO; GO:0019029; C:helical viral capsid; IEA:UniProtKB-KW.
DR   GO; GO:0020002; C:host cell plasma 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; IPR008020; G8P.
DR   InterPro; IPR023390; Phage_M13_G8P_capsid_dom_sf.
DR   Pfam; PF19199; Phage_coatGP8; 1.
DR   PIRSF; PIRSF004117; Phage_coat_B; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Capsid protein; Helical capsid protein;
KW   Host cell inner membrane; Host cell membrane; Host membrane; Membrane;
KW   Reference proteome; Signal; Transmembrane; Transmembrane helix; Virion.
FT   SIGNAL          1..23
FT   CHAIN           24..73
FT                   /note="Capsid protein G8P"
FT                   /id="PRO_0000003298"
FT   TOPO_DOM        24..47
FT                   /note="Periplasmic"
FT   TRANSMEM        48..68
FT                   /note="Helical"
FT   TOPO_DOM        69..73
FT                   /note="Cytoplasmic"
FT   HELIX           29..39
FT                   /evidence="ECO:0007829|PDB:2CPB"
FT   HELIX           41..46
FT                   /evidence="ECO:0007829|PDB:2CPB"
FT   HELIX           48..67
FT                   /evidence="ECO:0007829|PDB:2CPB"
FT   TURN            68..72
FT                   /evidence="ECO:0007829|PDB:2CPB"
SQ   SEQUENCE   73 AA;  7625 MW;  D12EF68DB18E645C CRC64;
     MKKSLVLKAS VAVATLVPML SFAAEGDDPA KAAFNSLQAS ATEYIGYAWA MVVVIVGATI
     GIKLFKKFTS KAS
 
 
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