COMPL_BPSPP
ID COMPL_BPSPP Reviewed; 134 AA.
AC O48448;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 02-JUN-2021, entry version 62.
DE RecName: Full=Tail completion protein gp17 {ECO:0000305};
DE AltName: Full=Gene product 17;
DE Short=gp17;
DE AltName: Full=Head-tail joining protein gp17 {ECO:0000305};
DE AltName: Full=Tail-to-head joining protein {ECO:0000303|PubMed:24443902};
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 FUNCTION.
RX PubMed=24443902; DOI=10.1111/mmi.12526;
RA Auzat I., Petitpas I., Lurz R., Weise F., Tavares P.;
RT "A touch of glue to complete bacteriophage assembly: the tail-to-head
RT joining protein (THJP) family.";
RL Mol. Microbiol. 91:1164-1178(2014).
RN [3] {ECO:0007744|PDB:2LFP}
RP STRUCTURE BY NMR OF 2-134, INTERACTION WITH GP16 CONNECTOR, FUNCTION, AND
RP SUBUNIT.
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 [4] {ECO:0007744|PDB:5A20, ECO:0007744|PDB:5A21}
RP STRUCTURE BY ELECTRON MICROSCOPY (7.20 ANGSTROMS), INTERACTION WITH GP16
RP CONNECTOR, FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
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: Tail completion protein that caps the tail and interacts with
CC the connector gp16, thereby attaching the tail to the capsid.
CC {ECO:0000269|PubMed:22072538, ECO:0000269|PubMed:24443902,
CC ECO:0000269|PubMed:25991862}.
CC -!- SUBUNIT: Homohexamer (PubMed:25991862, PubMed:22072538). Interacts with
CC gp16 connector protein (PubMed:22072538, PubMed:25991862).
CC {ECO:0000269|PubMed:22072538, ECO:0000269|PubMed:25991862}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:25991862}. Note=Forms
CC a thin ring-like structure at the proximal tip of the tail.
CC {ECO:0000269|PubMed:25991862}.
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DR EMBL; X97918; CAA66549.1; -; Genomic_DNA.
DR PIR; T42288; T42288.
DR RefSeq; NP_690679.1; NC_004166.2.
DR PDB; 2LFP; NMR; -; A=2-134.
DR PDB; 5A20; EM; 7.60 A; G=1-134.
DR PDB; 5A21; EM; 7.20 A; G=1-134.
DR PDBsum; 2LFP; -.
DR PDBsum; 5A20; -.
DR PDBsum; 5A21; -.
DR SMR; O48448; -.
DR GeneID; 955319; -.
DR KEGG; vg:955319; -.
DR EvolutionaryTrace; O48448; -.
DR Proteomes; UP000002559; Genome.
DR GO; GO:0098015; C:virus tail; IDA:UniProtKB.
DR GO; GO:0098004; P:virus tail fiber assembly; IDA:UniProtKB.
DR InterPro; IPR021508; Gp17-like.
DR Pfam; PF11367; DUF3168; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Reference proteome; Viral release from host cell;
KW Viral tail assembly; Viral tail protein; Virion.
FT CHAIN 1..134
FT /note="Tail completion protein gp17"
FT /id="PRO_0000438143"
FT HELIX 5..20
FT /evidence="ECO:0007829|PDB:2LFP"
FT TURN 22..27
FT /evidence="ECO:0007829|PDB:2LFP"
FT STRAND 31..34
FT /evidence="ECO:0007829|PDB:2LFP"
FT STRAND 41..47
FT /evidence="ECO:0007829|PDB:2LFP"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:2LFP"
FT STRAND 64..71
FT /evidence="ECO:0007829|PDB:2LFP"
FT HELIX 76..90
FT /evidence="ECO:0007829|PDB:2LFP"
FT STRAND 122..130
FT /evidence="ECO:0007829|PDB:2LFP"
SQ SEQUENCE 134 AA; 15010 MW; B8153CFC946C991D CRC64;
MTWKLASRAL QKATVENLES YQPLMEMVNQ VTESPGKDDP YPYVVIGDQS STPFETKSSF
GENITMDFHV WGGTTRAEAQ DISSRVLEAL TYKPLMFEGF TFVAKKLVLA QVITDTDGVT
KHGIIKVRFT INNN
