SCAFB_BPS13
ID SCAFB_BPS13 Reviewed; 120 AA.
AC P07929;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 03-AUG-2022, entry version 72.
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 Enterobacteria phage S13 (Bacteriophage S13).
OC Viruses; Monodnaviria; Sangervirae; Phixviricota; Malgrandaviricetes;
OC Petitvirales; Microviridae; Bullavirinae; Sinsheimervirus;
OC unclassified Sinsheimervirus.
OX NCBI_TaxID=10844;
OH NCBI_TaxID=590; Salmonella.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3007293; DOI=10.1016/0378-1119(85)90050-2;
RA Lau P.C.K., Spencer J.H.;
RT "Nucleotide sequence and genome organization of bacteriophage S13 DNA.";
RL Gene 40:273-284(1985).
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; M14428; AAA32584.1; -; Genomic_DNA.
DR PIR; JS0451; JS0451.
DR SMR; P07929; -.
DR Proteomes; UP000002129; 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..120
FT /note="Internal scaffolding protein B"
FT /id="PRO_0000164871"
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 76..77
FT /note="Cleavage; by host"
FT /evidence="ECO:0000250|UniProtKB:P03633"
FT SITE 77..78
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250|UniProtKB:P03633"
FT SITE 93..94
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250|UniProtKB:P03633"
FT SITE 108..109
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250|UniProtKB:P03633"
SQ SEQUENCE 120 AA; 13919 MW; 67B02AA24214A0E1 CRC64;
MEQLTKNQAV ATSQEAFQNQ NEPQLRDENV HNDKSVHGVL NPTYQAGLRR DAVQPDIEAE
RKKRDEIEAG KSYCSRRFGG ATCDDKSAQI YARFDKNDWR IQPAEFYRFH DAEVNTFGYF
