SCAFB_BPAL3
ID SCAFB_BPAL3 Reviewed; 117 AA.
AC P31278;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Internal scaffolding protein B;
DE EC=3.4.-.- {ECO:0000250|UniProtKB:P03633};
DE AltName: Full=Scaffolding protein B;
DE Short=GPB;
GN Name=B;
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).
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. Autoproteolytic activity cleaves
CC protein B and probably facilitates its removal through the pores of the
CC procapsid. {ECO:0000250|UniProtKB:P03633}.
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:0000250|UniProtKB:P03633}.
CC -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000250|UniProtKB:P03633}.
CC -!- PTM: The proteolytic cleavage of the internal scaffolding protein B
CC releases the scaffold protein in order to continue virion assembly.
CC {ECO:0000250|UniProtKB:P03633}.
CC -!- SIMILARITY: Belongs to the microviridae B protein family.
CC {ECO:0000305}.
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DR EMBL; X60322; CAA42875.1; -; Genomic_DNA.
DR PIR; S22325; S22325.
DR RefSeq; NP_039591.1; NC_001330.1.
DR GeneID; 1260691; -.
DR KEGG; vg:1260691; -.
DR Proteomes; UP000002137; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0019069; P:viral capsid assembly; IEA:InterPro.
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 3: Inferred from homology;
KW Autocatalytic cleavage; Host cytoplasm; Hydrolase; Protease;
KW Reference proteome; Viral capsid assembly; Viral release from host cell.
FT CHAIN 1..117
FT /note="Internal scaffolding protein B"
FT /id="PRO_0000164867"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 74..75
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250|UniProtKB:P03633"
FT SITE 90..91
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250|UniProtKB:P03633"
FT SITE 105..106
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250|UniProtKB:P03633"
SQ SEQUENCE 117 AA; 13335 MW; D699CA916507C633 CRC64;
MQESINGNLS EERISGTQQS ETRNGAPVNG SSEQQGTSGT EPNQLRFQSS VSDSERERQK
AIDLEHRRAA FARHFGCAPG SEKHVENYSS FDEKDTRVQL AEFYRFNDGH FKKWGYF
