CAPSD_BPT5
ID CAPSD_BPT5 Reviewed; 458 AA.
AC Q6QGD8; Q5DMF6;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Major capsid protein;
DE AltName: Full=Capsid protein pb8 {ECO:0000303|PubMed:24198424};
DE AltName: Full=Major head protein;
DE Contains:
DE RecName: Full=Scaffolding domain delta;
DE Flags: Precursor;
GN Name=D20 {ECO:0000312|EMBL:AAS77188.1};
GN ORFNames=ORF138, T5.149 {ECO:0000312|EMBL:AAS77188.1},
GN T5p145 {ECO:0000312|EMBL:AAU05284.1};
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:AAX12075.1};
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 SUBCELLULAR LOCATION.
RX PubMed=4571380; DOI=10.1016/0042-6822(73)90443-1;
RA Zweig M., Cummings D.J.;
RT "Structural proteins of bacteriophage T5.";
RL Virology 51:443-453(1973).
RN [4]
RP PROTEOLYTIC CLEAVAGE.
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 FUNCTION, AND SCAFFOLDING DOMAIN.
RX PubMed=20573812; DOI=10.1128/jvi.00942-10;
RA Huet A., Conway J.F., Letellier L., Boulanger P.;
RT "In vitro assembly of the T=13 procapsid of bacteriophage T5 with its
RT scaffolding domain.";
RL J. Virol. 84:9350-9358(2010).
RN [6]
RP FUNCTION.
RX PubMed=23500494; DOI=10.1016/j.jmb.2013.03.002;
RA Preux O., Durand D., Huet A., Conway J.F., Bertin A., Boulogne C.,
RA Drouin-Wahbi J., Trevarin D., Perez J., Vachette P., Boulanger P.;
RT "A two-state cooperative expansion converts the procapsid shell of
RT bacteriophage T5 into a highly stable capsid isomorphous to the final
RT virion head.";
RL J. Mol. Biol. 425:1999-2014(2013).
RN [7]
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 [8]
RP FUNCTION, AND MUTAGENESIS OF LEU-45; ILE-183; MET-201; MET-208; GLU-260;
RP ILE-283; SER-328 AND TYR-353.
RX PubMed=34644530; DOI=10.1016/j.cell.2021.09.031;
RA Tal N., Morehouse B.R., Millman A., Stokar-Avihail A., Avraham C.,
RA Fedorenko T., Yirmiya E., Herbst E., Brandis A., Mehlman T.,
RA Oppenheimer-Shaanan Y., Keszei A.F.A., Shao S., Amitai G., Kranzusch P.J.,
RA Sorek R.;
RT "Cyclic CMP and cyclic UMP mediate bacterial immunity against phages.";
RL Cell 0:0-0(2021).
RN [9]
RP STRUCTURE BY ELECTRON MICROSCOPY (30.0 ANGSTROMS) OF THE CAPSID, FUNCTION,
RP PROTEOLYTIC PROCESSING, INTERACTION WITH THE DECORATION PROTEIN, AND
RP INTERACTION WITH THE PORTAL 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).
CC -!- FUNCTION: Major capsid protein that self-associates to form 120
CC hexamers and 11 pentamers, building the T=13 icosahedral capsid which
CC about 860 Angstroms in diameter. Responsible for its self-assembly into
CC a procapsid. The phage does not need to encode a separate scaffolfing
CC protein because its capsid protein contains the delta domain that
CC carries that function. The capsid gains its final stability through the
CC reorganization of the subunits that takes place upon expansion. DNA
CC encapsidation through the portal triggers capsid expansion and the
CC binding of the decoration protein to the capsid exterior. Might play a
CC role in counteracting the host Pycsar defense system that is mediated
CC by pyrimidine cyclases and leads to abortive infection.
CC {ECO:0000269|PubMed:20573812, ECO:0000269|PubMed:23500494,
CC ECO:0000269|PubMed:26616586, ECO:0000269|PubMed:34644530}.
CC -!- SUBUNIT: Interacts with the decoration protein; each hexon binds a
CC single copy of the decoration protein. Interacts with the portal
CC protein (Probable). {ECO:0000269|PubMed:26616586}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:24198424,
CC ECO:0000269|PubMed:4571380}. Note=Forms the icosahedral capsid shell
CC which contains 775 major capsid proteins. {ECO:0000269|PubMed:4571380}.
CC -!- DOMAIN: The scaffolding domain delta has a role of scaffold allowing
CC the self-assembly of the capsid protein. {ECO:0000269|PubMed:20573812}.
CC -!- PTM: The scaffolding domain delta is cleaved by the prohead protease
CC and lost after assembly (PubMed:16876823). The major capsid protein
CC precursors together with both the portal complex and the maturation
CC protease form prohead I (PubMed:26616586). All copies of the major
CC capsid protein precursor are cleaved to the mature major capsid protein
CC by release of the scaffolding domain delta, yielding the metastable
CC prohead II (PubMed:26616586). {ECO:0000269|PubMed:16876823,
CC ECO:0000269|PubMed:26616586}.
CC -!- SIMILARITY: Belongs to the HK97 phage major capsid protein family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAX12075.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY692264; AAU05284.1; -; Genomic_DNA.
DR EMBL; AY543070; AAS77188.1; -; Genomic_DNA.
DR EMBL; AY587007; AAX12075.1; ALT_INIT; Genomic_DNA.
DR RefSeq; YP_006977.1; NC_005859.1.
DR PDB; 5TJT; EM; 9.00 A; A/B/C/D/E/F=160-458.
DR PDB; 6OKB; EM; 6.70 A; A/B/C/D/E/F/G/H/I/J/K/L/M=160-458.
DR PDB; 6OMA; EM; 7.20 A; A/B/C/D/E/F/G/H/I/J/K/L/M=160-458.
DR PDB; 6OMC; EM; 3.80 A; A/B/C/D/E/F/G/H/I/J/K/L/M=160-458.
DR PDBsum; 5TJT; -.
DR PDBsum; 6OKB; -.
DR PDBsum; 6OMA; -.
DR PDBsum; 6OMC; -.
DR SMR; Q6QGD8; -.
DR GeneID; 2777673; -.
DR KEGG; vg:2777673; -.
DR Proteomes; UP000002107; Genome.
DR Proteomes; UP000002141; Genome.
DR Proteomes; UP000002503; Genome.
DR GO; GO:0039621; C:T=13 icosahedral viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0019028; C:viral capsid; IDA:UniProtKB.
DR GO; GO:0046806; C:viral scaffold; IDA:UniProtKB.
DR GO; GO:0044414; P:suppression of host defenses by symbiont; IDA:UniProtKB.
DR InterPro; IPR024455; Phage_capsid.
DR Pfam; PF05065; Phage_capsid; 1.
DR TIGRFAMs; TIGR01554; major_cap_HK97; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Capsid protein; Coiled coil; Late protein;
KW Reference proteome; T=13 icosahedral capsid protein; Viral capsid assembly;
KW Viral release from host cell; Virion.
FT CHAIN 1..159
FT /note="Scaffolding domain delta"
FT /evidence="ECO:0000269|PubMed:16876823"
FT /id="PRO_0000433205"
FT CHAIN 160..458
FT /note="Major capsid protein"
FT /id="PRO_0000432352"
FT COILED 21..110
FT /evidence="ECO:0000255"
FT SITE 159..160
FT /note="Cleavage; by the prohead protease"
FT /evidence="ECO:0000269|PubMed:16876823, ECO:0000305"
FT MUTAGEN 45
FT /note="L->P: Confers resistance to Pycsar-mediated
FT defense."
FT /evidence="ECO:0000269|PubMed:34644530"
FT MUTAGEN 183
FT /note="I->T: Confers resistance to Pycsar-mediated
FT defense."
FT /evidence="ECO:0000269|PubMed:34644530"
FT MUTAGEN 201
FT /note="M->V: Confers resistance to Pycsar-mediated
FT defense."
FT /evidence="ECO:0000269|PubMed:34644530"
FT MUTAGEN 208
FT /note="M->T: Confers resistance to Pycsar-mediated
FT defense."
FT /evidence="ECO:0000269|PubMed:34644530"
FT MUTAGEN 260
FT /note="E->G: Confers resistance to Pycsar-mediated
FT defense."
FT /evidence="ECO:0000269|PubMed:34644530"
FT MUTAGEN 283
FT /note="I->T: Confers resistance to Pycsar-mediated
FT defense."
FT /evidence="ECO:0000269|PubMed:34644530"
FT MUTAGEN 328
FT /note="S->P: Confers resistance to Pycsar-mediated defense,
FT reduced fitness compared to wild-type phage."
FT /evidence="ECO:0000269|PubMed:34644530"
FT MUTAGEN 353
FT /note="Y->C: Confers resistance to Pycsar-mediated defense,
FT reduced fitness compared to wild-type phage."
FT /evidence="ECO:0000269|PubMed:34644530"
SQ SEQUENCE 458 AA; 50885 MW; F109BB8042B04944 CRC64;
MTIDINKLKE ELGLGDLAKS LEGLTAAQKA QEAERMRKEQ EEKELARMND LVSKAVGEDR
KRLEEALELV KSLDEKSKKS NELFAQTVEK QQETIVGLQD EIKSLLTARE GRSFVGDSVA
KALYGTQENF EDEVEKLVLL SYVMEKGVFE TEHGQRHLKA VNQSSSVEVS SESYETIFSQ
RIIRDLQKEL VVGALFEELP MSSKILTMLV EPDAGKATWV AASTYGTDTT TGEEVKGALK
EIHFSTYKLA AKSFITDETE EDAIFSLLPL LRKRLIEAHA VSIEEAFMTG DGSGKPKGLL
TLASEDSAKV VTEAKADGSV LVTAKTISKL RRKLGRHGLK LSKLVLIVSM DAYYDLLEDE
EWQDVAQVGN DSVKLQGQVG RIYGLPVVVS EYFPAKANSA EFAVIVYKDN FVMPRQRAVT
VERERQAGKQ RDAYYVTQRV NLQRYFANGV VSGTYAAS
