ID   SCAF_BPP2               Reviewed;         284 AA.
AC   P25478;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Capsid assembly scaffolding protein {ECO:0000305};
DE   AltName: Full=Gene product O;
DE            Short=GpO;
DE   AltName: Full=Head morphogenesis protein {ECO:0000305};
DE   AltName: Full=Scaffold protein {ECO:0000305};
DE   Contains:
DE     RecName: Full=Maturation protease {ECO:0000305|PubMed:19064277};
DE              EC=3.4.21.- {ECO:0000305|PubMed:19064277};
GN   Name=O;
OS   Escherichia phage P2 (Bacteriophage P2).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Myoviridae; Peduovirinae; Peduovirus.
OX   NCBI_TaxID=10679;
OH   NCBI_TaxID=543; Enterobacteriaceae.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1837355; DOI=10.1093/nar/19.25.7207;
RA   Linderoth N.A., Ziermann R., Haggaard-Ljungquist E., Christie G.E.,
RA   Calendar R.;
RT   "Nucleotide sequence of the DNA packaging and capsid synthesis genes of
RT   bacteriophage P2.";
RL   Nucleic Acids Res. 19:7207-7214(1991).
RN   [2]
RP   PROTEOLYTIC CLEAVAGE.
RX   PubMed=17931675; DOI=10.1016/j.virol.2007.08.039;
RA   Chang J.R., Poliakov A., Prevelige P.E., Mobley J.A., Dokland T.;
RT   "Incorporation of scaffolding protein gpO in bacteriophages P2 and P4.";
RL   Virology 370:352-361(2008).
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, AND SUBUNIT.
RX   PubMed=19064277; DOI=10.1016/j.virol.2008.11.016;
RA   Chang J.R., Spilman M.S., Rodenburg C.M., Dokland T.;
RT   "Functional domains of the bacteriophage P2 scaffolding protein:
RT   identification of residues involved in assembly and protease activity.";
RL   Virology 384:144-150(2009).
CC   -!- FUNCTION: Scaffolding protein and protease involved in the icosahedric
CC       procapsid assembly. Coassembles with the capsid proteins to form the
CC       procapsid, in which the scaffolding protein is found within the
CC       external shell of icosahedrally arranged capsid protein subunits. In a
CC       subsequent step the scaffolding protein molecules are cleaved by the
CC       viral protease activity. {ECO:0000305|PubMed:19064277}.
CC   -!- SUBUNIT: [Capsid assembly scaffolding protein]: Homomultimer.
CC       {ECO:0000269|PubMed:19064277}.
CC   -!- PTM: Autocleaves itself into an N-terminal fragment containing the
CC       protease activity, that remains in the capsid following maturation.
CC       {ECO:0000269|PubMed:17931675}.
CC   -!- SIMILARITY: Belongs to the P2likevirus scaffolding protein family.
CC       {ECO:0000305}.
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DR   EMBL; AF063097; AAD03270.1; -; Genomic_DNA.
DR   PIR; S22798; S22798.
DR   RefSeq; NP_046759.1; NC_001895.1.
DR   SMR; P25478; -.
DR   MEROPS; S73.001; -.
DR   GeneID; 1261524; -.
DR   KEGG; vg:1261524; -.
DR   Proteomes; UP000009092; Genome.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0046797; P:viral procapsid maturation; IEA:UniProtKB-KW.
DR   InterPro; IPR009228; Capsid_scaffold_GpO.
DR   Pfam; PF05929; Phage_GPO; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Hydrolase; Protease; Reference proteome; Serine protease;
KW   Viral capsid assembly; Viral capsid maturation;
KW   Viral release from host cell.
FT   CHAIN           1..141
FT                   /note="Maturation protease"
FT                   /id="PRO_0000433203"
FT   CHAIN           142..284
FT                   /note="Capsid assembly scaffolding protein"
FT                   /id="PRO_0000165258"
FT   REGION          258..284
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          206..243
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        258..272
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        19
FT                   /evidence="ECO:0000269|PubMed:19064277"
FT   ACT_SITE        48
FT                   /evidence="ECO:0000269|PubMed:19064277"
FT   ACT_SITE        107
FT                   /evidence="ECO:0000269|PubMed:19064277"
FT   SITE            141..142
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000269|PubMed:17931675"
SQ   SEQUENCE   284 AA;  31446 MW;  E2914F3C3E0763E3 CRC64;
     MAKKVSKFFR IGVEGDTCDG RVISAQDIQE MAETFDPRVY GCRINLEHLR GILPDGIFKR
     YGDVAELKAE KIDDDSALKG KWALFAKITP TDDLIAMNKA AQKVYTSMEI QPNFANTGKC
     YLVGLAVTDD PASLGTEYLE FCRTAKHNPL NRFKLSPENL ISVATPVELE FEDLPETVFT
     ALTEKVKSIF GRKQASDDAR LNDVHEAVTA VAEHVQEKLS ATEQRLAEME TAFSALKQEV
     TDRADETSQA FTRLKNSLDH TESLTQQRRS KATGGGGDAL MTNC