SCAFB_BPPHS
ID SCAFB_BPPHS Reviewed; 120 AA.
AC P03633;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Internal scaffolding protein B;
DE EC=3.4.-.- {ECO:0000269|PubMed:12473449};
DE AltName: Full=Scaffolding protein B;
DE Short=GPB;
GN Name=B;
OS Enterobacteria phage phiX174 (Isolate Sanger) (Bacteriophage phi-X174).
OC Viruses; Monodnaviria; Sangervirae; Phixviricota; Malgrandaviricetes;
OC Petitvirales; Microviridae; Bullavirinae; Sinsheimervirus.
OX NCBI_TaxID=1217068;
OH NCBI_TaxID=498388; Escherichia coli C.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=870828; DOI=10.1038/265687a0;
RA Sanger F., Air G.M., Barrell B.G., Brown N.L., Coulson A.R., Fiddes J.C.,
RA Hutchison C.A. III, Slocombe P.M., Smith M.;
RT "Nucleotide sequence of bacteriophage phi X174 DNA.";
RL Nature 265:687-695(1977).
RN [2]
RP FUNCTION, AND PROCAPSID STRUCTURE.
RX PubMed=159449; DOI=10.1073/pnas.76.10.4877;
RA Mukai R., Hamatake R.K., Hayashi M.;
RT "Isolation and identification of bacteriophage phi X174 prohead.";
RL Proc. Natl. Acad. Sci. U.S.A. 76:4877-4881(1979).
RN [3]
RP CLEAVAGE SITE, AND PROTEIN SEQUENCE OF 1-5.
RX PubMed=2973457; DOI=10.1128/jb.170.12.5564-5571.1988;
RA Richardson D.L. Jr., Aoyama A., Hayashi M.;
RT "Proteolysis of bacteriophage phi X174 prohead protein gpB by a protease
RT located in the Escherichia coli outer membrane.";
RL J. Bacteriol. 170:5564-5571(1988).
RN [4]
RP CATALYTIC ACTIVITY, FUNCTION, AND PROTEOLYTIC CLEAVAGE.
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).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS), AND SUBUNIT.
RX PubMed=9305849; DOI=10.1038/38537;
RA Dokland T., McKenna R., Ilag L.L., Bowman B.R., Incardona N.L., Fane B.A.,
RA Rossmann M.G.;
RT "Structure of a viral procapsid with molecular scaffolding.";
RL Nature 389:308-313(1997).
CC -!- FUNCTION: Participates in the assembly of the viral procapsid in the
CC cytoplasm. Forms first a 12S pre-assembly complex with protein H, and F
CC and G pentamers, then twelve 12S complexes are joined by the D protein
CC to form the procapsid. Internal scaffold protein B is released from the
CC procapsid upon genome packaging (PubMed:159449). Autoproteolytic
CC activity cleaves protein B and probably facilitates its removal through
CC the pores of the procapsid (PubMed:12473449).
CC {ECO:0000269|PubMed:12473449, ECO:0000269|PubMed:159449}.
CC -!- SUBUNIT: Component of the procapsid complex composed of 60 copies of
CC the internally located B, 240 copies of the external scaffolding
CC protein D, 60 copies of each of the viral structural proteins F and G
CC proteins, and 12 copies of H. {ECO:0000269|PubMed:9305849}.
CC -!- SUBCELLULAR LOCATION: Host cytoplasm.
CC -!- PTM: The proteolytic cleavage of the internal scaffolding protein B
CC releases the scaffold protein in order to continue virion assembly.
CC {ECO:0000269|PubMed:12473449}.
CC -!- SIMILARITY: Belongs to the microviridae B protein family.
CC {ECO:0000305}.
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DR EMBL; J02482; AAA32572.1; -; Genomic_DNA.
DR PIR; A04241; ZBBPF4.
DR PDB; 1AL0; X-ray; 3.50 A; B=1-120.
DR PDB; 1CD3; X-ray; 3.50 A; B=1-120.
DR PDBsum; 1AL0; -.
DR PDBsum; 1CD3; -.
DR SMR; P03633; -.
DR EvolutionaryTrace; P03633; -.
DR Proteomes; UP000005893; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046806; C:viral scaffold; IDA:UniProtKB.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0046807; P:viral scaffold assembly and maintenance; IDA:UniProtKB.
DR Gene3D; 4.10.1260.10; -; 1.
DR InterPro; IPR003513; Phage_B.
DR InterPro; IPR038149; Phage_B_sf.
DR Pfam; PF02304; Phage_B; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Autocatalytic cleavage; Direct protein sequencing;
KW Host cytoplasm; Hydrolase; Protease; Reference proteome;
KW Viral capsid assembly; Viral release from host cell.
FT CHAIN 1..120
FT /note="Internal scaffolding protein B"
FT /id="PRO_0000164870"
FT REGION 1..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 77..78
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000269|PubMed:12473449"
FT SITE 93..94
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000269|PubMed:12473449"
FT SITE 108..109
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000269|PubMed:12473449"
FT HELIX 62..79
FT /evidence="ECO:0007829|PDB:1CD3"
FT HELIX 87..90
FT /evidence="ECO:0007829|PDB:1AL0"
FT HELIX 112..115
FT /evidence="ECO:0007829|PDB:1AL0"
SQ SEQUENCE 120 AA; 13843 MW; D8E52894116497ED CRC64;
MEQLTKNQAV ATSQEAVQNQ NEPQLRDENA HNDKSVHGVL NPTYQAGLRR DAVQPDIEAE
RKKRDEIEAG KSYCSRRFGG ATCDDKSAQI YARFDKNDWR IQPAEFYRFH DAEVNTFGYF
