CAPSD_BPXF
ID CAPSD_BPXF Reviewed; 44 AA.
AC P03622;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 02-JUN-2021, entry version 83.
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 Xanthomonas phage Xf (Bacteriophage Xf).
OC Viruses; Monodnaviria; Loebvirae; Hofneiviricota; Faserviricetes;
OC Tubulavirales; Inoviridae; unclassified Inoviridae.
OX NCBI_TaxID=356629;
OH NCBI_TaxID=314227; Xanthomonas campestris pv. oryzae.
RN [1]
RP PROTEIN SEQUENCE, AND ACETYLATION AT SER-1.
RX PubMed=729805; DOI=10.1016/0014-5793(78)80442-6;
RA Frangione B., Nakashima Y., Konigsberg W., Wiseman R.L.;
RT "The amino acid sequence of the major coat protein subunit of the
RT filamentous virus Xf.";
RL FEBS Lett. 96:381-384(1978).
RN [2]
RP 3D-STRUCTURE MODELING.
RX PubMed=2078529; DOI=10.1016/0141-8130(90)90064-h;
RA Marvin D.A.;
RT "Model-building studies of Inovirus: genetic variations on a geometric
RT theme.";
RL Int. J. Biol. Macromol. 12:125-138(1990).
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}.
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DR PIR; A04230; VCBPXF.
DR PDB; 2IFO; Fiber; -; A=5-44.
DR PDBsum; 2IFO; -.
DR SMR; P03622; -.
DR iPTMnet; P03622; -.
DR EvolutionaryTrace; P03622; -.
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 InterPro; IPR008020; G8P.
DR Pfam; PF05356; Phage_Coat_B; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Capsid protein; Direct protein sequencing;
KW Helical capsid protein; Host membrane; Membrane; Transmembrane;
KW Transmembrane helix; Virion.
FT CHAIN 1..44
FT /note="Capsid protein G8P"
FT /id="PRO_0000098187"
FT TOPO_DOM 1..19
FT /note="Periplasmic"
FT TRANSMEM 20..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 38..44
FT /note="Cytoplasmic"
FT MOD_RES 1
FT /note="N-acetylserine; by host"
FT /evidence="ECO:0000269|PubMed:729805"
FT NON_TER 1
FT HELIX 6..42
FT /evidence="ECO:0007829|PDB:2IFO"
SQ SEQUENCE 44 AA; 4342 MW; ACC9223F5DE63D28 CRC64;
SGVGDGVDVV SAIEGAAGPI AAIGGAVLTV MVGIKVYKWV RRAM