ID   SCAF_BPT7               Reviewed;         307 AA.
AC   P03716;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   23-FEB-2022, entry version 71.
DE   RecName: Full=Capsid assembly scaffolding protein {ECO:0000305};
DE   AltName: Full=Gene product 9;
DE            Short=Gp9;
DE   AltName: Full=Head morphogenesis protein {ECO:0000305};
DE   AltName: Full=Scaffold protein {ECO:0000305};
GN   OrderedLocusNames=9;
OS   Escherichia phage T7 (Bacteriophage T7).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Autographiviridae; Studiervirinae; Teseptimavirus.
OX   NCBI_TaxID=10760;
OH   NCBI_TaxID=562; Escherichia coli.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=6864790; DOI=10.1016/s0022-2836(83)80282-4;
RA   Dunn J.J., Studier F.W.;
RT   "Complete nucleotide sequence of bacteriophage T7 DNA and the locations of
RT   T7 genetic elements.";
RL   J. Mol. Biol. 166:477-535(1983).
RN   [2]
RP   FUNCTION IN VIRION MATURATION.
RX   PubMed=13677051; DOI=10.1016/s0065-3233(03)01008-8;
RA   Cerritelli M.E., Conway J.F., Cheng N., Trus B.L., Steven A.C.;
RT   "Molecular mechanisms in bacteriophage T7 procapsid assembly, maturation,
RT   and DNA containment.";
RL   Adv. Protein Chem. 64:301-323(2003).
RN   [3]
RP   FUNCTION.
RX   PubMed=16211007; DOI=10.1038/sj.emboj.7600840;
RA   Agirrezabala X., Martin-Benito J., Caston J.R., Miranda R., Valpuesta J.M.,
RA   Carrascosa J.L.;
RT   "Maturation of phage T7 involves structural modification of both shell and
RT   inner core components.";
RL   EMBO J. 24:3820-3829(2005).
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:0000305|PubMed:13677051, ECO:0000305|PubMed:16211007}.
CC   -!- SIMILARITY: Belongs to the T7likevirus capsid assembly scaffolding
CC       protein family. {ECO:0000305}.
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DR   EMBL; V01146; CAA24426.1; -; Genomic_DNA.
DR   PIR; A04343; ACBPT7.
DR   RefSeq; NP_041996.1; NC_001604.1.
DR   IntAct; P03716; 1.
DR   MINT; P03716; -.
DR   GeneID; 1261027; -.
DR   KEGG; vg:1261027; -.
DR   Proteomes; UP000000840; Genome.
DR   GO; GO:0019069; P:viral capsid assembly; IEA:InterPro.
DR   InterPro; IPR008768; Phage_T7_capsid.
DR   Pfam; PF05396; Phage_T7_Capsid; 1.
PE   1: Evidence at protein level;
KW   Reference proteome; Viral capsid assembly; Viral release from host cell.
FT   CHAIN           1..307
FT                   /note="Capsid assembly scaffolding protein"
FT                   /id="PRO_0000106519"
FT   REGION          45..105
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        45..77
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   307 AA;  33898 MW;  D2183755D7005717 CRC64;
     MAESNADVYA SFGVNSAVMS GGSVEEHEQN MLALDVAARD GDDAIELASD EVETERDLYD
     NSDPFGQEDD EGRIQVRIGD GSEPTDVDTG EEGVEGTEGS EEFTPLGETP EELVAASEQL
     GEHEEGFQEM INIAAERGMS VETIEAIQRE YEENEELSAE SYAKLAEIGY TKAFIDSYIR
     GQEALVEQYV NSVIEYAGGR ERFDALYNHL ETHNPEAAQS LDNALTNRDL ATVKAIINLA
     GESRAKAFGR KPTRSVTNRA IPAKPQATKR EGFADRSEMI KAMSDPRYRT DANYRRQVEQ
     KVIDSNF