SCAF_BPT3
ID SCAF_BPT3 Reviewed; 310 AA.
AC P20324;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 23-FEB-2022, entry version 52.
DE RecName: Full=Capsid assembly scaffolding protein;
DE AltName: Full=Capsid assembly protein;
DE AltName: Full=Gene product 9;
DE Short=Gp9;
DE AltName: Full=Head morphogenesis protein;
DE AltName: Full=Scaffold protein;
DE AltName: Full=Scaffolding protein;
GN Name=9;
OS Enterobacteria phage T3 (Bacteriophage T3).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Autographiviridae; Studiervirinae; Teetrevirus;
OC Escherichia virus T3.
OX NCBI_TaxID=10759;
OH NCBI_TaxID=562; Escherichia coli.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Luria;
RX PubMed=2614843; DOI=10.1016/0022-2836(89)90102-2;
RA Beck P.J., Gonzalez S., Ward C.L., Molineux I.J.;
RT "Sequence of bacteriophage T3 DNA from gene 2.5 through gene 9.";
RL J. Mol. Biol. 210:687-701(1989).
CC -!- FUNCTION: Scaffolding protein involved in the icosahedric procapsid
CC assembly. Coassembles with the capsid proteins to form the procapsid,
CC in which the scaffolding protein is found within the external shell of
CC icosahedrally arranged capsid protein subunits. In a subsequent step
CC the scaffolding protein molecules are released from the procapsid.
CC Facilitates assembly by binding to gp10 hexamers but not the pentamers
CC and locking them into a morphogenically correct conformation.
CC {ECO:0000250|UniProtKB:P03716}.
CC -!- SIMILARITY: Belongs to the T7likevirus capsid assembly scaffolding
CC protein family. {ECO:0000305}.
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DR EMBL; X17255; CAA35153.1; -; Genomic_DNA.
DR PIR; S07522; S07522.
DR RefSeq; NP_523333.1; NC_003298.1.
DR GeneID; 927415; -.
DR KEGG; vg:927415; -.
DR GO; GO:0019069; P:viral capsid assembly; IEA:InterPro.
DR InterPro; IPR008768; Phage_T7_capsid.
DR Pfam; PF05396; Phage_T7_Capsid; 1.
PE 3: Inferred from homology;
KW Viral capsid assembly; Viral release from host cell.
FT CHAIN 1..310
FT /note="Capsid assembly scaffolding protein"
FT /id="PRO_0000106518"
FT REGION 46..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..102
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 310 AA; 33729 MW; 5BD281A34B8DEF29 CRC64;
MAESNADVYA SFGVNNAVMT GSTPTEHEQN MLSLDVAARD GDDAIVLSDE PTSHNDDPYA
AGVDPFADGE DDEGRIQVRI SEDGNEAGFD TDGDNSEVET EGEDVEFEPL GDTPEELSQV
TEQLGQHEEG FQAMVEQAVE RGLSADSVSR IYEEYEADGI SEKSYAELEA AGYSRAFVDS
YISGQEALVD QYVNQVVAFA GGQERFSAIH THLEATNPAA AESLESAMMN RDLATVKAII
NLAGESYTKK FGKPANRSVT KRATPVKPVA RQKEGFTNQA EMIKAMSDPR YRSDSAYRQM
VEQKVIDSSF