DECO_BPT5
ID DECO_BPT5 Reviewed; 164 AA.
AC Q6QGD6;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Decoration protein {ECO:0000303|PubMed:24198424};
DE AltName: Full=Capsid protein pb10;
GN Name=N5 {ECO:0000312|EMBL:AAU05286.1};
GN ORFNames=T5.151 {ECO:0000312|EMBL:AAS77190.1},
GN T5p147 {ECO:0000312|EMBL:AAU05286.1};
OS Escherichia phage T5 (Enterobacteria phage T5).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Demerecviridae; Markadamsvirinae; Tequintavirus.
OX NCBI_TaxID=2695836;
OH NCBI_TaxID=562; Escherichia coli.
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Ksenzenko V.N., Kaliman A.V., Krutilina A.I., Shlyapnikov M.G.;
RT "Bacteriophage T5 complete genome.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND INDUCTION.
RC STRAIN=ATCC 11303-B5 {ECO:0000312|EMBL:AAX12077.1};
RX PubMed=15661140; DOI=10.1016/j.virol.2004.10.049;
RA Wang J., Jiang Y., Vincent M., Sun Y., Yu H., Wang J., Bao Q., Kong H.,
RA Hu S.;
RT "Complete genome sequence of bacteriophage T5.";
RL Virology 332:45-65(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SUBCELLULAR LOCATION.
RC STRAIN=St0 deletion mutant;
RX PubMed=24198424; DOI=10.1128/jvi.02262-13;
RA Zivanovic Y., Confalonieri F., Ponchon L., Lurz R., Chami M., Flayhan A.,
RA Renouard M., Huet A., Decottignies P., Davidson A.R., Breyton C.,
RA Boulanger P.;
RT "Insights into bacteriophage T5 structure from analysis of its
RT morphogenesis genes and protein components.";
RL J. Virol. 88:1162-1174(2014).
RN [4]
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=16876823; DOI=10.1016/j.jmb.2006.06.081;
RA Effantin G., Boulanger P., Neumann E., Letellier L., Conway J.F.;
RT "Bacteriophage T5 structure reveals similarities with HK97 and T4
RT suggesting evolutionary relationships.";
RL J. Mol. Biol. 361:993-1002(2006).
RN [5]
RP STRUCTURE BY ELECTRON MICROSCOPY (30.0 ANGSTROMS) OF THE CAPSID, FUNCTION,
RP AND INTERACTION WITH THE MAJOR CAPSID PROTEIN.
RX PubMed=26616586; DOI=10.1016/j.jmb.2015.11.019;
RA Huet A., Duda R.L., Hendrix R.W., Boulanger P., Conway J.F.;
RT "Correct assembly of the bacteriophage T5 procapsid requires both the
RT maturation protease and the portal complex.";
RL J. Mol. Biol. 428:165-181(2016).
RN [6]
RP STRUCTURE BY NMR, INTERACTION WITH THE MAJOR CAPSID PROTEIN, FUNCTION, AND
RP DOMAIN.
RX PubMed=28165000; DOI=10.1038/srep41662;
RA Vernhes E., Renouard M., Gilquin B., Cuniasse P., Durand D., England P.,
RA Hoos S., Huet A., Conway J.F., Glukhov A., Ksenzenko V., Jacquet E.,
RA Nhiri N., Zinn-Justin S., Boulanger P.;
RT "High affinity anchoring of the decoration protein pb10 onto the
RT bacteriophage T5 capsid.";
RL Sci. Rep. 7:41662-41662(2017).
CC -!- FUNCTION: Decoration protein that binds asymmetrically to the center of
CC each capsid protein hexamer after capsid expansion. Stabilizes the
CC capsid and protects from DNA release. {ECO:0000269|PubMed:16876823,
CC ECO:0000269|PubMed:26616586, ECO:0000269|PubMed:28165000}.
CC -!- SUBUNIT: Interacts with the major capsid protein; each hexon binds a
CC single copy of the decoration protein. {ECO:0000269|PubMed:26616586,
CC ECO:0000269|PubMed:28165000}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:16876823,
CC ECO:0000269|PubMed:24198424}. Note=120 copies of the decoration protein
CC are localized on the exterior of the capsid.
CC {ECO:0000269|PubMed:16876823}.
CC -!- DOMAIN: The N-terminus binds to the capsid proteins with high affinity
CC and high cooperativity while the C-terminus displays an IG-like fold.
CC {ECO:0000269|PubMed:28165000}.
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DR EMBL; AY543070; AAS77190.1; -; Genomic_DNA.
DR EMBL; AY692264; AAU05286.1; -; Genomic_DNA.
DR EMBL; AY587007; AAX12077.1; -; Genomic_DNA.
DR RefSeq; YP_006979.1; NC_005859.1.
DR PDB; 5LXK; NMR; -; A=73-164.
DR PDB; 5LXL; NMR; -; A=2-77.
DR PDBsum; 5LXK; -.
DR PDBsum; 5LXL; -.
DR BMRB; Q6QGD6; -.
DR SMR; Q6QGD6; -.
DR GeneID; 2777675; -.
DR KEGG; vg:2777675; -.
DR Proteomes; UP000002107; Genome.
DR Proteomes; UP000002141; Genome.
DR Proteomes; UP000002503; Genome.
DR GO; GO:0098021; C:viral capsid, decoration; IDA:UniProtKB.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR Pfam; PF13895; Ig_2; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Capsid decoration protein; Capsid protein; Late protein;
KW Reference proteome; Virion.
FT CHAIN 1..164
FT /note="Decoration protein"
FT /id="PRO_0000435555"
FT DOMAIN 71..164
FT /note="Ig-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:28165000"
FT REGION 1..72
FT /note="Binding to the capsid hexamer"
FT /evidence="ECO:0000269|PubMed:28165000"
FT STRAND 2..4
FT /evidence="ECO:0007829|PDB:5LXL"
FT HELIX 5..10
FT /evidence="ECO:0007829|PDB:5LXL"
FT HELIX 18..23
FT /evidence="ECO:0007829|PDB:5LXL"
FT HELIX 25..28
FT /evidence="ECO:0007829|PDB:5LXL"
FT HELIX 34..40
FT /evidence="ECO:0007829|PDB:5LXL"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:5LXL"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:5LXL"
FT HELIX 49..59
FT /evidence="ECO:0007829|PDB:5LXL"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:5LXK"
FT STRAND 82..87
FT /evidence="ECO:0007829|PDB:5LXK"
FT STRAND 89..94
FT /evidence="ECO:0007829|PDB:5LXK"
FT STRAND 97..111
FT /evidence="ECO:0007829|PDB:5LXK"
FT STRAND 120..128
FT /evidence="ECO:0007829|PDB:5LXK"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:5LXK"
FT STRAND 134..142
FT /evidence="ECO:0007829|PDB:5LXK"
FT TURN 143..145
FT /evidence="ECO:0007829|PDB:5LXK"
FT STRAND 146..160
FT /evidence="ECO:0007829|PDB:5LXK"
SQ SEQUENCE 164 AA; 17247 MW; ED556D7D2FE3B298 CRC64;
MIDYSGLRTI FGEKLPESHI FFATVAAHKY VPSYAFLRRE LGLSSAHTNR KVWKKFVEAY
GKAIPPAPPA PPLTLSKDLT ASMSVEEGAA LTLSVTATGG TGPYTYAWTK DGSPIPDASG
ATYTKPTAAA EDAGSYKVTV TDSKQVSKDS TTCAVTVNPT VPGG
