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Database: UniProt
Entry: SCAF_BPSPP
LinkDB: SCAF_BPSPP
Original site: SCAF_BPSPP 
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   23-MAY-2018, entry version 58.
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; dsDNA viruses, no RNA stage; Caudovirales; Siphoviridae;
OC   Lambdavirus; unclassified Lambda-like viruses.
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
RT   Bacillus 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.,
RA   Lurz R., Trautner T.A., Alonso J.C.;
RT   "Head morphogenesis genes of the Bacillus subtilis bacteriophage
RT   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.,
RA   Trautner T.A., Tavares P.;
RT   "Shape and DNA packaging activity of bacteriophage SPP1 procapsid:
RT   protein 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
CC       procapsid assembly. Coassembles with the capsid proteins to form
CC       the procapsid, in which the scaffolding protein is found within
CC       the external shell of icosahedrally arranged capsid protein
CC       subunits (PubMed:18377930). In a subsequent step the scaffolding
CC       protein molecules are released from the procapsid (Probable).
CC       {ECO:0000305|PubMed:18377930}.
CC   -!- SUBUNIT: Homodimer (PubMed:10656821). Interacts with the capsid
CC       protein 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}.
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   OrthoDB; VOG090001D2; -.
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; Complete proteome; Reference proteome;
KW   Viral capsid assembly; Viral release from host cell.
FT   CHAIN         1    214       Capsid assembly scaffolding protein.
FT                                /FTId=PRO_0000433209.
FT   COILED       36    105       {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
//
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