ID   HCP16_BPSPP             Reviewed;         109 AA.
AC   O48446;
DT   02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   29-SEP-2021, entry version 66.
DE   RecName: Full=Head completion protein gp16 {ECO:0000305};
DE   AltName: Full=Connector protein gp16;
DE   AltName: Full=Gene product 16;
DE            Short=Gp16;
DE   AltName: Full=Stopper protein gp16;
GN   Name=16;
OS   Bacillus phage SPP1 (Bacteriophage SPP1).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Siphoviridae.
OX   NCBI_TaxID=10724;
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   INTERACTION WITH THE HEAD-TAIL JOINING PROTEIN GP17.
RX   PubMed=22072538; DOI=10.1002/prot.23191;
RA   Chagot B., Auzat I., Gallopin M., Petitpas I., Gilquin B., Tavares P.,
RA   Zinn-Justin S.;
RT   "Solution structure of gp17 from the Siphoviridae bacteriophage SPP1:
RT   insights into its role in virion assembly.";
RL   Proteins 80:319-326(2012).
RN   [3] {ECO:0007744|PDB:2KCA}
RP   STRUCTURE BY NMR.
RX   PubMed=19433794; DOI=10.1073/pnas.0812407106;
RA   Lhuillier S., Gallopin M., Gilquin B., Brasiles S., Lancelot N.,
RA   Letellier G., Gilles M., Dethan G., Orlova E.V., Couprie J., Tavares P.,
RA   Zinn-Justin S.;
RT   "Structure of bacteriophage SPP1 head-to-tail connection reveals mechanism
RT   for viral DNA gating.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:8507-8512(2009).
RN   [4] {ECO:0007744|PDB:5A20, ECO:0007744|PDB:5A21}
RP   STRUCTURE BY ELECTRON MICROSCOPY (7.20 ANGSTROMS), SUBCELLULAR LOCATION,
RP   INTERACTION WITH THE CONNECTOR PROTEIN GP15, INTERACTION WITH THE HEAD-TAIL
RP   JOINING PROTEIN GP17, AND FUNCTION.
RX   PubMed=25991862; DOI=10.1073/pnas.1504039112;
RA   Chaban Y., Lurz R., Brasiles S., Cornilleau C., Karreman M.,
RA   Zinn-Justin S., Tavares P., Orlova E.V.;
RT   "Structural rearrangements in the phage head-to-tail interface during
RT   assembly and infection.";
RL   Proc. Natl. Acad. Sci. U.S.A. 112:7009-7014(2015).
CC   -!- FUNCTION: Functions as a stopper that is part of the head-tail
CC       connector and that locks the viral DNA in the capsid. Following tail
CC       attachment to the entry receptor, seems to open by a diaphragm-like
CC       motion, allowing the genome to exit the capsid through the tail tube to
CC       the host cell. During assembly, functions as a docking platform which
CC       the preassembled tail tapered by the head-tail joining protein gp17 can
CC       bind to. {ECO:0000269|PubMed:25991862}.
CC   -!- SUBUNIT: Homododecamer (PubMed:25991862). Interacts with the connector
CC       protein gp15 (PubMed:25991862). Interacts with the head-tail joining
CC       protein gp17 (PubMed:22072538, PubMed:25991862).
CC       {ECO:0000269|PubMed:22072538, ECO:0000269|PubMed:25991862}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:25991862}. Note=Part
CC       of the connector between the portal and the tail.
CC       {ECO:0000269|PubMed:25991862}.
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DR   EMBL; X97918; CAA66547.1; -; Genomic_DNA.
DR   PIR; T42286; T42286.
DR   RefSeq; NP_690677.1; NC_004166.2.
DR   PDB; 2KCA; NMR; -; A=1-109.
DR   PDB; 5A20; EM; 7.60 A; E/F=1-109.
DR   PDB; 5A21; EM; 7.20 A; E/F=1-109.
DR   PDBsum; 2KCA; -.
DR   PDBsum; 5A20; -.
DR   PDBsum; 5A21; -.
DR   SMR; O48446; -.
DR   DIP; DIP-48858N; -.
DR   GeneID; 955315; -.
DR   KEGG; vg:955315; -.
DR   EvolutionaryTrace; O48446; -.
DR   Proteomes; UP000002559; Genome.
DR   GO; GO:0099001; P:viral genome ejection through host cell envelope, long flexible tail mechanism; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.10.270; -; 1.
DR   InterPro; IPR008767; Phage_SPP1_head-tail_adaptor.
DR   InterPro; IPR038666; SSP1_head-tail_sf.
DR   Pfam; PF05521; Phage_H_T_join; 1.
DR   TIGRFAMs; TIGR01563; gp16_SPP1; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Reference proteome;
KW   Viral genome ejection through host cell envelope;
KW   Viral long flexible tail ejection system;
KW   Viral penetration into host cytoplasm; Virion; Virus entry into host cell.
FT   CHAIN           1..109
FT                   /note="Head completion protein gp16"
FT                   /id="PRO_0000438141"
FT   STRAND          7..16
FT                   /evidence="ECO:0007829|PDB:2KCA"
FT   STRAND          18..20
FT                   /evidence="ECO:0007829|PDB:2KCA"
FT   STRAND          23..25
FT                   /evidence="ECO:0007829|PDB:2KCA"
FT   STRAND          27..40
FT                   /evidence="ECO:0007829|PDB:2KCA"
FT   TURN            42..44
FT                   /evidence="ECO:0007829|PDB:2KCA"
FT   STRAND          57..64
FT                   /evidence="ECO:0007829|PDB:2KCA"
FT   STRAND          68..76
FT                   /evidence="ECO:0007829|PDB:2KCA"
FT   STRAND          79..89
FT                   /evidence="ECO:0007829|PDB:2KCA"
FT   STRAND          96..102
FT                   /evidence="ECO:0007829|PDB:2KCA"
SQ   SEQUENCE   109 AA;  12542 MW;  7B719398FE5CB757 CRC64;
     MYEEFPDVIT FQSYVEQSNG EGGKTYKWVD EFTAAAHVQP ISQEEYYKAQ QLQTPIGYNI
     YTPYDDRIDK KMRVIYRGKI VTFIGDPVDL SGLQEITRIK GKEDGAYVG