ID   SCAF_BPSPP              Reviewed;         214 AA.
AC   Q38580;
DT   24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   02-JUN-2021, entry version 66.
DE   RecName: Full=Capsid assembly scaffolding protein {ECO:0000305};
DE   AltName: Full=Gene product 11;
DE            Short=Gp11;
DE   AltName: Full=Head morphogenesis protein {ECO:0000305};
DE   AltName: Full=Scaffold protein {ECO:0000305};
GN   Name=11 {ECO:0000312|EMBL:CAA61868.1};
OS   Bacillus phage SPP1 (Bacteriophage SPP1).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Siphoviridae.
OX   NCBI_TaxID=10724 {ECO:0000312|EMBL:CAA61868.1};
OH   NCBI_TaxID=1423; Bacillus subtilis.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=9434185; DOI=10.1016/s0378-1119(97)00547-7;
RA   Alonso J.C., Luder G., Stiege A.C., Chai S., Weise F., Trautner T.A.;
RT   "The complete nucleotide sequence and functional organization of Bacillus
RT   subtilis bacteriophage SPP1.";
RL   Gene 204:201-212(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND IDENTIFICATION.
RX   PubMed=9180375; DOI=10.1006/jmbi.1997.0997;
RA   Becker B., de la Fuente N., Gassel M., Guenther D., Tavares P., Lurz R.,
RA   Trautner T.A., Alonso J.C.;
RT   "Head morphogenesis genes of the Bacillus subtilis bacteriophage SPP1.";
RL   J. Mol. Biol. 268:822-839(1997).
RN   [3]
RP   INTERACTION WITH THE CAPSID PROTEIN GP13.
RX   PubMed=10656821; DOI=10.1006/jmbi.1999.3450;
RA   Droege A., Santos M.A., Stiege A.C., Alonso J.C., Lurz R., Trautner T.A.,
RA   Tavares P.;
RT   "Shape and DNA packaging activity of bacteriophage SPP1 procapsid: protein
RT   components and interactions during assembly.";
RL   J. Mol. Biol. 296:117-132(2000).
RN   [4]
RP   SUBUNIT, AND FUNCTION.
RX   PubMed=18377930; DOI=10.1016/j.jmb.2008.02.028;
RA   Poh S.L., el Khadali F., Berrier C., Lurz R., Melki R., Tavares P.;
RT   "Oligomerization of the SPP1 scaffolding protein.";
RL   J. Mol. Biol. 378:551-564(2008).
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 (PubMed:18377930). In a
CC       subsequent step the scaffolding protein molecules are released from the
CC       procapsid (Probable). {ECO:0000305|PubMed:18377930}.
CC   -!- SUBUNIT: Homodimer (PubMed:10656821). Interacts with the capsid protein
CC       gp13 (PubMed:18377930). {ECO:0000269|PubMed:10656821,
CC       ECO:0000269|PubMed:18377930}.
CC   -!- SIMILARITY: Belongs to the SPP1-like scaffolding protein family.
CC       {ECO:0000305}.
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DR   EMBL; X89721; CAA61868.1; -; Genomic_DNA.
DR   EMBL; X97918; CAA66589.1; -; Genomic_DNA.
DR   PIR; S58140; S58140.
DR   RefSeq; NP_690671.1; NC_004166.2.
DR   SMR; Q38580; -.
DR   GeneID; 955293; -.
DR   KEGG; vg:955293; -.
DR   Proteomes; UP000002559; Genome.
DR   GO; GO:0019069; P:viral capsid assembly; IDA:UniProtKB.
DR   InterPro; IPR009636; SCAF.
DR   Pfam; PF06810; Phage_GP20; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Reference proteome; Viral capsid assembly;
KW   Viral release from host cell.
FT   CHAIN           1..214
FT                   /note="Capsid assembly scaffolding protein"
FT                   /id="PRO_0000433209"
FT   REGION          154..190
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          36..105
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   214 AA;  23463 MW;  60F89B6BB8CCF0FC CRC64;
     MSLKEQLGEE LYGQVLAKLG EGAKLVDISD GSFIPKEKFD AVNSEKKSLE QQLTDRDQQL
     QELSTKATGH DELSAKIADL QKANEEAKQA FEAEKQQLKY EHALETALRD SGAKNPKAVK
     ALLDTESIKL DGDKLLGFED QIKALKEQED YLFKGTEPNG GVQGTPPPGK GADLGGLPTK
     KNPFKQGPDF NLTEQGILFR ENPELAKKLQ AEAQ