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Head completion protein gp16 (Connector protein gp16) (Gene product 16) (Gp16) (Stopper protein gp16)

 HCP16_BPSPP             Reviewed;         109 AA.
O48446;
02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
01-JUN-1998, sequence version 1.
11-DEC-2019, entry version 62.
RecName: Full=Head completion protein gp16 {ECO:0000305};
AltName: Full=Connector protein gp16;
AltName: Full=Gene product 16;
Short=Gp16;
AltName: Full=Stopper protein gp16;
Name=16;
Bacillus phage SPP1 (Bacteriophage SPP1).
Viruses; Caudovirales; Siphoviridae.
NCBI_TaxID=10724;
NCBI_TaxID=1423; Bacillus subtilis.
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=9434185; DOI=10.1016/s0378-1119(97)00547-7;
Alonso J.C., Luder G., Stiege A.C., Chai S., Weise F., Trautner T.A.;
"The complete nucleotide sequence and functional organization of Bacillus
subtilis bacteriophage SPP1.";
Gene 204:201-212(1997).
[2]
INTERACTION WITH THE HEAD-TAIL JOINING PROTEIN GP17.
PubMed=22072538; DOI=10.1002/prot.23191;
Chagot B., Auzat I., Gallopin M., Petitpas I., Gilquin B., Tavares P.,
Zinn-Justin S.;
"Solution structure of gp17 from the Siphoviridae bacteriophage SPP1:
insights into its role in virion assembly.";
Proteins 80:319-326(2012).
[3] {ECO:0000244|PDB:2KCA}
STRUCTURE BY NMR.
PubMed=19433794; DOI=10.1073/pnas.0812407106;
Lhuillier S., Gallopin M., Gilquin B., Brasiles S., Lancelot N.,
Letellier G., Gilles M., Dethan G., Orlova E.V., Couprie J., Tavares P.,
Zinn-Justin S.;
"Structure of bacteriophage SPP1 head-to-tail connection reveals mechanism
for viral DNA gating.";
Proc. Natl. Acad. Sci. U.S.A. 106:8507-8512(2009).
[4] {ECO:0000244|PDB:5A20, ECO:0000244|PDB:5A21}
STRUCTURE BY ELECTRON MICROSCOPY (7.20 ANGSTROMS), SUBCELLULAR LOCATION,
INTERACTION WITH THE CONNECTOR PROTEIN GP15, INTERACTION WITH THE HEAD-TAIL
JOINING PROTEIN GP17, AND FUNCTION.
PubMed=25991862; DOI=10.1073/pnas.1504039112;
Chaban Y., Lurz R., Brasiles S., Cornilleau C., Karreman M.,
Zinn-Justin S., Tavares P., Orlova E.V.;
"Structural rearrangements in the phage head-to-tail interface during
assembly and infection.";
Proc. Natl. Acad. Sci. U.S.A. 112:7009-7014(2015).
-!- FUNCTION: Functions as a stopper that is part of the head-tail
connector and that locks the viral DNA in the capsid. Following tail
attachment to the entry receptor, seems to open by a diaphragm-like
motion, allowing the genome to exit the capsid through the tail tube to
the host cell. During assembly, functions as a docking platform which
the preassembled tail tapered by the head-tail joining protein gp17 can
bind to. {ECO:0000269|PubMed:25991862}.
-!- SUBUNIT: Homododecamer (PubMed:25991862). Interacts with the connector
protein gp15 (PubMed:25991862). Interacts with the head-tail joining
protein gp17 (PubMed:22072538, PubMed:25991862).
{ECO:0000269|PubMed:22072538, ECO:0000269|PubMed:25991862}.
-!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:25991862}. Note=Part
of the connector between the portal and the tail.
{ECO:0000269|PubMed:25991862}.
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EMBL; X97918; CAA66547.1; -; Genomic_DNA.
PIR; T42286; T42286.
RefSeq; NP_690677.1; NC_004166.2.
PDB; 2KCA; NMR; -; A=1-109.
PDB; 5A20; EM; 7.60 A; E/F=1-109.
PDB; 5A21; EM; 7.20 A; E/F=1-109.
PDBsum; 2KCA; -.
PDBsum; 5A20; -.
PDBsum; 5A21; -.
SMR; O48446; -.
DIP; DIP-48858N; -.
GeneID; 955315; -.
KEGG; vg:955315; -.
EvolutionaryTrace; O48446; -.
Proteomes; UP000002559; Genome.
GO; GO:0019012; C:virion; IEA:UniProtKB-SubCell.
GO; GO:0099001; P:viral genome ejection through host cell envelope, long flexible tail mechanism; IEA:UniProtKB-KW.
Gene3D; 2.40.10.270; -; 1.
InterPro; IPR008767; Phage_SPP1_head-tail_adaptor.
InterPro; IPR038666; SSP1_head-tail_sf.
Pfam; PF05521; Phage_H_T_join; 1.
TIGRFAMs; TIGR01563; gp16_SPP1; 1.
1: Evidence at protein level;
3D-structure; Reference proteome;
Viral genome ejection through host cell envelope;
Viral long flexible tail ejection system;
Viral penetration into host cytoplasm; Virion; Virus entry into host cell.
CHAIN 1..109
/note="Head completion protein gp16"
/id="PRO_0000438141"
STRAND 7..16
/evidence="ECO:0000244|PDB:2KCA"
STRAND 18..20
/evidence="ECO:0000244|PDB:2KCA"
STRAND 23..25
/evidence="ECO:0000244|PDB:2KCA"
STRAND 27..40
/evidence="ECO:0000244|PDB:2KCA"
TURN 42..44
/evidence="ECO:0000244|PDB:2KCA"
STRAND 57..64
/evidence="ECO:0000244|PDB:2KCA"
STRAND 68..76
/evidence="ECO:0000244|PDB:2KCA"
STRAND 79..89
/evidence="ECO:0000244|PDB:2KCA"
STRAND 96..102
/evidence="ECO:0000244|PDB:2KCA"
SEQUENCE 109 AA; 12542 MW; 7B719398FE5CB757 CRC64;
MYEEFPDVIT FQSYVEQSNG EGGKTYKWVD EFTAAAHVQP ISQEEYYKAQ QLQTPIGYNI
YTPYDDRIDK KMRVIYRGKI VTFIGDPVDL SGLQEITRIK GKEDGAYVG


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Bibliography :