CAPSD_BPHK7
ID CAPSD_BPHK7 Reviewed; 385 AA.
AC P49861;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Major capsid protein {ECO:0000303|PubMed:17098191};
DE AltName: Full=Gene product 5 {ECO:0000305};
DE Short=gp5 {ECO:0000305};
DE AltName: Full=Major head protein {ECO:0000303|PubMed:7723019};
DE Contains:
DE RecName: Full=Scaffolding domain delta;
GN Name=5;
OS Enterobacteria phage HK97 (Bacteriophage HK97).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Siphoviridae; Hendrixvirinae; Byrnievirus.
OX NCBI_TaxID=2681617;
OH NCBI_TaxID=562; Escherichia coli.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS, FUNCTION, AND PROTEOLYTIC
RP CLEAVAGE.
RX PubMed=7723020; DOI=10.1016/s0022-2836(05)80144-5;
RA Duda R.L., Martincic K., Hendrix R.W.;
RT "Genetic basis of bacteriophage HK97 prohead assembly.";
RL J. Mol. Biol. 247:636-647(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10860721; DOI=10.1006/jmbi.2000.3729;
RA Juhala R.J., Ford M.E., Duda R.L., Youlton A., Hatfull G.F., Hendrix R.W.;
RT "Genomic sequences of bacteriophages HK97 and HK022: pervasive genetic
RT mosaicism in the lambdoid bacteriophages.";
RL J. Mol. Biol. 299:27-51(2000).
RN [3]
RP FUNCTION.
RX PubMed=7669350; DOI=10.1111/j.1574-6976.1995.tb00186.x;
RA Duda R.L., Martincic K., Xie Z., Hendrix R.W.;
RT "Bacteriophage HK97 head assembly.";
RL FEMS Microbiol. Rev. 17:41-46(1995).
RN [4]
RP CHARACTERIZATION, AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=7723019; DOI=10.1016/s0022-2836(05)80143-3;
RA Duda R.L., Hempel J., Michel H., Shabanowitz J., Hunt D., Hendrix R.W.;
RT "Structural transitions during bacteriophage HK97 head assembly.";
RL J. Mol. Biol. 247:618-635(1995).
RN [5]
RP CROSS-LINK ASN-LYS INTERCHAIN, SUBCELLULAR LOCATION, FUNCTION, AND SUBUNIT.
RX PubMed=11000116; DOI=10.1126/science.289.5487.2129;
RA Wikoff W.R., Liljas L., Duda R.L., Tsuruta H., Hendrix R.W., Johnson J.E.;
RT "Topologically linked protein rings in the bacteriophage HK97 capsid.";
RL Science 289:2129-2133(2000).
RN [6]
RP STRUCTURE BY ELECTRON MICROSCOPY OF 128-383.
RX PubMed=11326105; DOI=10.1126/science.1058069;
RA Conway J.F., Wikoff W.R., Cheng N., Duda R.L., Hendrix R.W., Johnson J.E.,
RA Steven A.C.;
RT "Virus maturation involving large subunit rotations and local refolding.";
RL Science 292:744-748(2001).
RN [7] {ECO:0007744|PDB:1OHG}
RP X-RAY CRYSTALLOGRAPHY (3.45 ANGSTROMS) OF 104-385.
RX PubMed=14643655; DOI=10.1016/j.jmb.2003.09.035;
RA Helgstrand C., Wikoff W.R., Duda R.L., Hendrix R.W., Johnson J.E.,
RA Liljas L.;
RT "The refined structure of a protein catenane: the HK97 bacteriophage capsid
RT at 3.44 A resolution.";
RL J. Mol. Biol. 334:885-899(2003).
RN [8] {ECO:0007744|PDB:2FRP, ECO:0007744|PDB:2FS3, ECO:0007744|PDB:2FSY, ECO:0007744|PDB:2FT1, ECO:0007744|PDB:2FTE}
RP X-RAY CRYSTALLOGRAPHY (3.80 ANGSTROMS) OF 104-385.
RX PubMed=17098191; DOI=10.1016/j.str.2006.09.006;
RA Gan L., Speir J.A., Conway J.F., Lander G., Cheng N., Firek B.A.,
RA Hendrix R.W., Duda R.L., Liljas L., Johnson J.E.;
RT "Capsid conformational sampling in HK97 maturation visualized by X-ray
RT crystallography and cryo-EM.";
RL Structure 14:1655-1665(2006).
RN [9] {ECO:0007744|PDB:2GP1, ECO:0007744|PDB:3E8K}
RP X-RAY CRYSTALLOGRAPHY (5.20 ANGSTROMS) OF 104-385, AND X-RAY
RP CRYSTALLOGRAPHY (3.65 ANGSTROMS) OF 104-158 AND 172-385.
RX PubMed=19204733; DOI=10.1038/nature07686;
RA Gertsman I., Gan L., Guttman M., Lee K., Speir J.A., Duda R.L.,
RA Hendrix R.W., Komives E.A., Johnson J.E.;
RT "An unexpected twist in viral capsid maturation.";
RL Nature 458:646-650(2009).
RN [10] {ECO:0007744|PDB:3DDX}
RP STRUCTURE BY NMR OF 104-385.
RX PubMed=18940605; DOI=10.1016/j.str.2008.06.014;
RA Lee K.K., Gan L., Tsuruta H., Moyer C., Conway J.F., Duda R.L.,
RA Hendrix R.W., Steven A.C., Johnson J.E.;
RT "Virus capsid expansion driven by the capture of mobile surface loops.";
RL Structure 16:1491-1502(2008).
RN [11] {ECO:0007744|PDB:3QPR}
RP X-RAY CRYSTALLOGRAPHY (5.20 ANGSTROMS), AND FUNCTION.
RX PubMed=21276801; DOI=10.1016/j.jmb.2011.01.016;
RA Huang R.K., Khayat R., Lee K.K., Gertsman I., Duda R.L., Hendrix R.W.,
RA Johnson J.E.;
RT "The Prohead-I structure of bacteriophage HK97: implications for scaffold-
RT mediated control of particle assembly and maturation.";
RL J. Mol. Biol. 408:541-554(2011).
RN [12] {ECO:0007744|PDB:3J1A}
RP STRUCTURE BY ELECTRON MICROSCOPY (16.00 ANGSTROMS) OF 182-380, AND
RP FUNCTION.
RX PubMed=22593163; DOI=10.1128/jvi.00407-12;
RA Shen P.S., Domek M.J., Sanz-Garcia E., Makaju A., Taylor R.M., Hoggan R.,
RA Culumber M.D., Oberg C.J., Breakwell D.P., Prince J.T., Belnap D.M.;
RT "Sequence and structural characterization of great salt lake bacteriophage
RT CW02, a member of the T7-like supergroup.";
RL J. Virol. 86:7907-7917(2012).
CC -!- FUNCTION: Assembles to form an icosahedral capsid of 66 nm, with a T=7
CC laevo symmetry (PubMed:11000116, PubMed:21276801). Responsible for its
CC self-assembly into a procapsid. The phage does not need to encode a
CC separate scaffolfing protein because its capsid protein contains the
CC delta domain that carries that function. {ECO:0000269|PubMed:11000116,
CC ECO:0000269|PubMed:21276801, ECO:0000269|PubMed:7669350,
CC ECO:0000269|PubMed:7723020}.
CC -!- SUBUNIT: Homopentamer and homohexamer; isoaspartyl lysine isopeptide-
CC linked. {ECO:0000269|PubMed:11000116}.
CC -!- INTERACTION:
CC P49861; P49860: 4; NbExp=3; IntAct=EBI-15611310, EBI-16087766;
CC P49861; P49861: 5; NbExp=9; IntAct=EBI-15611310, EBI-15611310;
CC -!- SUBCELLULAR LOCATION: Virion. Note=Forms the icosahedral capsid shell
CC which contains 420 major capsid proteins.
CC {ECO:0000269|PubMed:11000116}.
CC -!- DOMAIN: The scaffolding domain delta has a role of scaffold allowing
CC the self-assembly of the capsid protein.
CC {ECO:0000250|UniProtKB:Q6QGD8}.
CC -!- PTM: The scaffolding domain delta is cleaved by the viral protease and
CC lost after assembly. {ECO:0000269|PubMed:7723020}.
CC -!- PTM: The major capsid proteins are covalently cross-linked.
CC {ECO:0000269|PubMed:11000116}.
CC -!- SIMILARITY: Belongs to the HK97 phage major capsid protein family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC structure of expansion Intermediate IV;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=2fte";
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC structure of head II;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=2ft1";
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC structure of head I mutant K169Y;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=2fs3";
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC structure of pepsin-treated Expansion Intermediate IV;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=2fsy";
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC structure of expansion Intermediate IV;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=2frp";
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral empty
CC mature capsid structure;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1ohg";
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DR EMBL; U18319; AAA80204.1; -; Genomic_DNA.
DR EMBL; AF069529; AAF31090.1; -; Genomic_DNA.
DR PIR; S54392; S54392.
DR RefSeq; NP_037701.1; NC_002167.1.
DR PDB; 1IF0; EM; 12.00 A; A/B/C/D/E/F/G=128-383.
DR PDB; 1OHG; X-ray; 3.45 A; A/B/C/D/E/F/G=104-385.
DR PDB; 2FRP; X-ray; 7.50 A; A/B/C/D/E/F/G=104-385.
DR PDB; 2FS3; X-ray; 4.20 A; A/B/C/D/E/F/G=104-385.
DR PDB; 2FSY; X-ray; 3.80 A; A/B/C/D/E/F/G=104-385.
DR PDB; 2FT1; X-ray; 3.90 A; A/B/C/D/E/F/G=104-385.
DR PDB; 2FTE; EM; -; A/B/C/D/E/F/G=104-385.
DR PDB; 2GP1; X-ray; 5.20 A; A/B/C/D/E/F/G=104-385.
DR PDB; 3DDX; EM; -; A/B/C/D/E/F/G=104-385.
DR PDB; 3E8K; X-ray; 3.65 A; A/B/C/D/E/F/G=104-158, A/B/C/D/E/F/G=172-385.
DR PDB; 3J1A; EM; 16.00 A; A/B/C/D/E/F/G=182-380.
DR PDB; 3QPR; X-ray; 5.20 A; A/B/C/D/E/F/G=1-385.
DR PDBsum; 1IF0; -.
DR PDBsum; 1OHG; -.
DR PDBsum; 2FRP; -.
DR PDBsum; 2FS3; -.
DR PDBsum; 2FSY; -.
DR PDBsum; 2FT1; -.
DR PDBsum; 2FTE; -.
DR PDBsum; 2GP1; -.
DR PDBsum; 3DDX; -.
DR PDBsum; 3E8K; -.
DR PDBsum; 3J1A; -.
DR PDBsum; 3QPR; -.
DR SMR; P49861; -.
DR DIP; DIP-29163N; -.
DR IntAct; P49861; 1.
DR GeneID; 1262530; -.
DR KEGG; vg:1262530; -.
DR EvolutionaryTrace; P49861; -.
DR Proteomes; UP000002576; Genome.
DR GO; GO:0039620; C:T=7 icosahedral viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0019028; C:viral capsid; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046797; P:viral procapsid maturation; IMP:CACAO.
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; Direct protein sequencing;
KW Isopeptide bond; Late protein; Reference proteome;
KW T=7 icosahedral capsid protein; Viral capsid assembly;
KW Viral release from host cell; Virion.
FT CHAIN 1..103
FT /note="Scaffolding domain delta"
FT /id="PRO_0000020965"
FT CHAIN 104..385
FT /note="Major capsid protein"
FT /id="PRO_0000020966"
FT COILED 1..57
FT /evidence="ECO:0000255"
FT CROSSLNK 169
FT /note="Isoaspartyl lysine isopeptide (Lys-Asn) (interchain
FT with N-356)"
FT /evidence="ECO:0000269|PubMed:11000116"
FT CROSSLNK 356
FT /note="Isoaspartyl lysine isopeptide (Asn-Lys) (interchain
FT with K-169)"
FT /evidence="ECO:0000269|PubMed:11000116"
FT MUTAGEN 103
FT /note="K->L: Reduced cleavage efficiency."
FT /evidence="ECO:0000269|PubMed:7723020"
FT MUTAGEN 169
FT /note="K->Y: Loss of ability to form cross-links between
FT subunits."
FT /evidence="ECO:0000269|PubMed:7723020"
FT MUTAGEN 356
FT /note="N->D: Loss of cleavage and cross-linking."
FT /evidence="ECO:0000269|PubMed:7723020"
FT MUTAGEN 362
FT /note="C->S: No loss in the ability to form cross-links."
FT /evidence="ECO:0000269|PubMed:7723020"
FT TURN 109..112
FT /evidence="ECO:0007829|PDB:1OHG"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:1OHG"
FT STRAND 119..125
FT /evidence="ECO:0007829|PDB:1OHG"
FT HELIX 135..137
FT /evidence="ECO:0007829|PDB:1OHG"
FT STRAND 138..142
FT /evidence="ECO:0007829|PDB:1OHG"
FT STRAND 145..157
FT /evidence="ECO:0007829|PDB:1OHG"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:1OHG"
FT STRAND 173..182
FT /evidence="ECO:0007829|PDB:1OHG"
FT STRAND 184..193
FT /evidence="ECO:0007829|PDB:1OHG"
FT HELIX 194..199
FT /evidence="ECO:0007829|PDB:1OHG"
FT HELIX 203..224
FT /evidence="ECO:0007829|PDB:1OHG"
FT HELIX 236..239
FT /evidence="ECO:0007829|PDB:1OHG"
FT STRAND 240..242
FT /evidence="ECO:0007829|PDB:2FTE"
FT HELIX 245..247
FT /evidence="ECO:0007829|PDB:1OHG"
FT HELIX 254..264
FT /evidence="ECO:0007829|PDB:1OHG"
FT HELIX 266..268
FT /evidence="ECO:0007829|PDB:1OHG"
FT STRAND 274..277
FT /evidence="ECO:0007829|PDB:1OHG"
FT HELIX 279..286
FT /evidence="ECO:0007829|PDB:1OHG"
FT TURN 296..301
FT /evidence="ECO:0007829|PDB:1OHG"
FT STRAND 306..308
FT /evidence="ECO:0007829|PDB:1OHG"
FT STRAND 311..315
FT /evidence="ECO:0007829|PDB:1OHG"
FT STRAND 323..327
FT /evidence="ECO:0007829|PDB:1OHG"
FT HELIX 329..332
FT /evidence="ECO:0007829|PDB:1OHG"
FT STRAND 333..349
FT /evidence="ECO:0007829|PDB:1OHG"
FT TURN 353..355
FT /evidence="ECO:0007829|PDB:1OHG"
FT STRAND 357..366
FT /evidence="ECO:0007829|PDB:1OHG"
FT STRAND 368..371
FT /evidence="ECO:0007829|PDB:1OHG"
FT HELIX 373..375
FT /evidence="ECO:0007829|PDB:1OHG"
FT STRAND 376..380
FT /evidence="ECO:0007829|PDB:1OHG"
SQ SEQUENCE 385 AA; 42243 MW; E083A4D30E3313D6 CRC64;
MSELALIQKA IEESQQKMTQ LFDAQKAEIE STGQVSKQLQ SDLMKVQEEL TKSGTRLFDL
EQKLASGAEN PGEKKSFSER AAEELIKSWD GKQGTFGAKT FNKSLGSDAD SAGSLIQPMQ
IPGIIMPGLR RLTIRDLLAQ GRTSSNALEY VREEVFTNNA DVVAEKALKP ESDITFSKQT
ANVKTIAHWV QASRQVMDDA PMLQSYINNR LMYGLALKEE GQLLNGDGTG DNLEGLNKVA
TAYDTSLNAT GDTRADIIAH AIYQVTESEF SASGIVLNPR DWHNIALLKD NEGRYIFGGP
QAFTSNIMWG LPVVPTKAQA AGTFTVGGFD MASQVWDRMD ATVEVSREDR DNFVKNMLTI
LCEERLALAH YRPTAIIKGT FSSGS
