ID   SCAF_BPHC1              Reviewed;         298 AA.
AC   P51719;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Capsid assembly scaffolding protein {ECO:0000250|UniProtKB:P25478};
DE   AltName: Full=Gene product 17;
DE            Short=Gp17;
DE   AltName: Full=Head morphogenesis protein {ECO:0000250|UniProtKB:P25478};
DE   AltName: Full=Scaffold protein {ECO:0000250|UniProtKB:P25478};
DE   Contains:
DE     RecName: Full=Maturation protease {ECO:0000250|UniProtKB:P25478};
DE              EC=3.4.21.- {ECO:0000250|UniProtKB:P25478};
OS   Haemophilus phage HP1 (strain HP1c1) (Bacteriophage HP1).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Myoviridae; Peduovirinae; Hpunavirus.
OX   NCBI_TaxID=1289570;
OH   NCBI_TaxID=727; Haemophilus influenzae.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=8710508; DOI=10.1093/nar/24.12.2360;
RA   Esposito D., Fitzmaurice W.P., Benjamin R.C., Goodman S.D., Waldman A.S.,
RA   Scocca J.J.;
RT   "The complete nucleotide sequence of bacteriophage HP1 DNA.";
RL   Nucleic Acids Res. 24:2360-2368(1996).
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:0000250|UniProtKB:P25478}.
CC   -!- SUBUNIT: [Capsid assembly scaffolding protein]: Homomultimer.
CC       {ECO:0000250|UniProtKB:P25478}.
CC   -!- PTM: Autocleaves itself into an N-terminal fragment containing the
CC       protease activity, that remains in the capsid following maturation.
CC       {ECO:0000250|UniProtKB:P25478}.
CC   -!- SIMILARITY: Belongs to the P2likevirus scaffolding protein family.
CC       {ECO:0000305}.
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DR   EMBL; U24159; AAB09202.1; -; Genomic_DNA.
DR   PIR; S69523; S69523.
DR   RefSeq; NP_043486.1; NC_001697.1.
DR   SMR; P51719; -.
DR   GeneID; 1261138; -.
DR   KEGG; vg:1261138; -.
DR   Proteomes; UP000001713; 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   3: Inferred from homology;
KW   Hydrolase; Protease; Reference proteome; Serine protease;
KW   Viral capsid assembly; Viral capsid maturation;
KW   Viral release from host cell.
FT   PROPEP          1..2
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000441100"
FT   CHAIN           3..131
FT                   /note="Maturation protease"
FT                   /evidence="ECO:0000250|UniProtKB:P25478"
FT                   /id="PRO_0000433204"
FT   CHAIN           132..298
FT                   /note="Capsid assembly scaffolding protein"
FT                   /id="PRO_0000165312"
FT   REGION          223..243
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        223..241
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        21
FT                   /evidence="ECO:0000250|UniProtKB:P25478"
FT   ACT_SITE        50
FT                   /evidence="ECO:0000250|UniProtKB:P25478"
FT   ACT_SITE        97
FT                   /evidence="ECO:0000250|UniProtKB:P25478"
FT   SITE            131..132
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000250|UniProtKB:P25478"
SQ   SEQUENCE   298 AA;  33703 MW;  6D2841468D700C1F CRC64;
     MNKSKLKTDF ICIATSGYTV DGRQITAQEL HEMAETYDPE HYTANLWPEH RRWFNMGQVI
     ELKAEENEKG ETQLFAIIAP NKELIEYNRA GQYLFTSIEI TPNFRNSGKA YLSGLGVTDS
     PASVGTTELK FFNAEQKGSV CGEFIKVDFS AKEDVEEEKA LRTLANVFKK LFSILRPNGK
     NEPNPNNNNH KEDHAMNDKQ FAQLIEAVKG LDAKIDNHFS AKVETKEPEN KPEEKKDEQP
     QSVTAEQFNQ LLITVQALDK KFNELSQEQT TVPSGVPTVE KENVYSLNGY NIDLSKGF