CAPSD_BPP22
ID CAPSD_BPP22 Reviewed; 430 AA.
AC P26747; A8CGC7; Q77D91; Q7PCI5;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Major capsid protein {ECO:0000305};
DE AltName: Full=Gene product 5 {ECO:0000305};
DE Short=gp5;
DE AltName: Full=Major head protein {ECO:0000305};
GN Name=5;
OS Salmonella phage P22 (Bacteriophage P22).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Podoviridae; Lederbergvirus.
OX NCBI_TaxID=10754;
OH NCBI_TaxID=90371; Salmonella typhimurium.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-9.
RX PubMed=1853558; DOI=10.1016/0042-6822(91)90981-g;
RA Eppler K., Wyckoff E., Goates J., Parr R., Casjens S.;
RT "Nucleotide sequence of the bacteriophage P22 genes required for DNA
RT packaging.";
RL Virology 183:519-538(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11053393; DOI=10.1128/jb.182.22.6472-6481.2000;
RA Vander Byl C.S., Kropinski A.M.B.;
RT "Sequence of the genome of Salmonella bacteriophage P22.";
RL J. Bacteriol. 182:6472-6481(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12562822; DOI=10.1128/jb.185.4.1475-1477.2003;
RA Pedulla M.L., Ford M.E., Karthikeyan T., Houtz J.M., Hendrix R.W.,
RA Hatfull G.F., Poteete A.R., Gilcrease E.B., Winn-Stapley D.A.,
RA Casjens S.R.;
RT "Corrected sequence of the bacteriophage P22 genome.";
RL J. Bacteriol. 185:1475-1477(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19585-B1 {ECO:0000312|Proteomes:UP000002165}, and
RC MSU {ECO:0000312|EMBL:BAF80720.1, ECO:0000312|Proteomes:UP000001315};
RX PubMed=18621868; DOI=10.1128/aem.00352-08;
RA Masago Y., Shibata T., Rose J.B.;
RT "Bacteriophage P22 and Staphylococcus aureus attenuation on nonporous
RT fomites as determined by plate assay and quantitative PCR.";
RL Appl. Environ. Microbiol. 74:5838-5840(2008).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19585-B1 {ECO:0000312|EMBL:BAG12603.1};
RA Masago Y., Fong T.T., Rose J.B.;
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP INTERACTION WITH THE CAPSID ASSEMBLY SCAFFOLDING PROTEIN.
RX PubMed=9680476; DOI=10.1006/jmbi.1998.1917;
RA Parker M.H., Casjens S., Prevelige P.E. Jr.;
RT "Functional domains of bacteriophage P22 scaffolding protein.";
RL J. Mol. Biol. 281:69-79(1998).
RN [7]
RP DOMAIN.
RX PubMed=24126914; DOI=10.1074/jbc.m113.515312;
RA Suhanovsky M.M., Teschke C.M.;
RT "An intramolecular chaperone inserted in bacteriophage P22 coat protein
RT mediates its chaperonin-independent folding.";
RL J. Biol. Chem. 288:33772-33783(2013).
RN [8]
RP INTERACTION WITH THE CAPSID ASSEMBLY SCAFFOLDING PROTEIN, AND MUTAGENESIS
RP OF GLU-5; ASP-14; GLU-15; GLU-18; LYS-377 AND ASP-385.
RX PubMed=24600011; DOI=10.1128/jvi.00036-14;
RA Cortines J.R., Motwani T., Vyas A.A., Teschke C.M.;
RT "Highly specific salt bridges govern bacteriophage P22 icosahedral capsid
RT assembly: identification of the site in coat protein responsible for
RT interaction with scaffolding protein.";
RL J. Virol. 88:5287-5297(2014).
RN [9]
RP MUTAGENESIS OF TRP-241; GLN-242; LEU-243; ASP-244; ASN-245; ASP-246;
RP LYS-249 AND ASN-251.
RX PubMed=26269173; DOI=10.1128/jvi.01629-15;
RA D'Lima N.G., Teschke C.M.;
RT "A Molecular Staple: D-Loops in the I Domain of Bacteriophage P22 Coat
RT Protein Make Important Intercapsomer Contacts Required for Procapsid
RT Assembly.";
RL J. Virol. 89:10569-10579(2015).
RN [10]
RP MUTAGENESIS OF TRP-61, AND FUNCTION.
RX PubMed=31068429; DOI=10.1128/jvi.00727-19;
RA Asija K., Teschke C.M.;
RT "A Hydrophobic Network: Intersubunit and Intercapsomer Interactions
RT Stabilizing the Bacteriophage P22 Capsid.";
RL J. Virol. 93:0-0(2019).
RN [11] {ECO:0007744|PDB:3IYH, ECO:0007744|PDB:3IYI}
RP STRUCTURE BY ELECTRON MICROSCOPY (8.20 ANGSTROMS), AND SUBCELLULAR
RP LOCATION.
RX PubMed=20223221; DOI=10.1016/j.str.2009.12.014;
RA Parent K.N., Khayat R., Tu L.H., Suhanovsky M.M., Cortines J.R.,
RA Teschke C.M., Johnson J.E., Baker T.S.;
RT "P22 coat protein structures reveal a novel mechanism for capsid
RT maturation: stability without auxiliary proteins or chemical crosslinks.";
RL Structure 18:390-401(2010).
RN [12] {ECO:0007744|PDB:2XYY, ECO:0007744|PDB:2XYZ}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.80 ANGSTROMS), AND FUNCTION.
RX PubMed=21220301; DOI=10.1073/pnas.1015739108;
RA Chen D.H., Baker M.L., Hryc C.F., DiMaio F., Jakana J., Wu W.,
RA Dougherty M., Haase-Pettingell C., Schmid M.F., Jiang W., Baker D.,
RA King J.A., Chiu W.;
RT "Structural basis for scaffolding-mediated assembly and maturation of a
RT dsDNA virus.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:1355-1360(2011).
RN [13] {ECO:0007744|PDB:2M5S}
RP STRUCTURE BY NMR OF 223-345, SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=24836025; DOI=10.1016/j.str.2014.04.003;
RA Rizzo A.A., Suhanovsky M.M., Baker M.L., Fraser L.C., Jones L.M.,
RA Rempel D.L., Gross M.L., Chiu W., Alexandrescu A.T., Teschke C.M.;
RT "Multiple functional roles of the accessory I-domain of bacteriophage P22
RT coat protein revealed by NMR structure and CryoEM modeling.";
RL Structure 22:830-841(2014).
RN [14] {ECO:0007744|PDB:5UU5}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.30 ANGSTROMS).
RX PubMed=28270620; DOI=10.1073/pnas.1621152114;
RA Hryc C.F., Chen D.H., Afonine P.V., Jakana J., Wang Z.,
RA Haase-Pettingell C., Jiang W., Adams P.D., King J.A., Schmid M.F., Chiu W.;
RT "Accurate model annotation of a near-atomic resolution cryo-EM map.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:3103-3108(2017).
CC -!- FUNCTION: Self-assembles to form an icosahedral capsid with a T=7
CC symmetry. {ECO:0000269|PubMed:21220301, ECO:0000305|PubMed:31068429}.
CC -!- SUBUNIT: Interacts (via N-terminus) with the capsid assembly
CC scaffolding protein (via C-terminus); capsid proteins and scaffolding
CC proteins form building blocks that assemble to form the procapsid.
CC {ECO:0000269|PubMed:24600011, ECO:0000269|PubMed:9680476}.
CC -!- INTERACTION:
CC P26747; P26747: 5; NbExp=2; IntAct=EBI-15582363, EBI-15582363;
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:20223221,
CC ECO:0000269|PubMed:24836025}. Note=Forms the capsid icosahedric shell.
CC {ECO:0000269|PubMed:20223221, ECO:0000269|PubMed:24836025}.
CC -!- DOMAIN: The insertion domain (I domain) plays an important role in the
CC folding of the capsid protein by acting as an intramolecular chaperone.
CC {ECO:0000269|PubMed:24126914, ECO:0000269|PubMed:24836025}.
CC -!- SIMILARITY: Belongs to the P22 phage major capsid protein family.
CC {ECO:0000305}.
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DR EMBL; M59749; AAA72963.1; -; Genomic_DNA.
DR EMBL; AF217253; AAF75047.1; -; Genomic_DNA.
DR EMBL; BK000583; DAA00987.1; -; Genomic_DNA.
DR EMBL; AF527608; AAM81389.1; -; Genomic_DNA.
DR EMBL; AB362338; BAF80720.1; -; Genomic_DNA.
DR EMBL; AB426868; BAG12603.1; -; Genomic_DNA.
DR PIR; E40474; Z5BP22.
DR RefSeq; NP_059630.1; NC_002371.2.
DR PDB; 2M5S; NMR; -; A=223-345.
DR PDB; 2XYY; EM; 3.80 A; A/B/C/D/E/F/G=1-430.
DR PDB; 2XYZ; EM; 4.00 A; A/B/C/D/E/F/G=1-430.
DR PDB; 3IYH; EM; -; A/B/C/D/E/F=1-430.
DR PDB; 3IYI; EM; -; A/B/C/D/E/F/G=1-430.
DR PDB; 5UU5; EM; 3.30 A; A/B/C/D/E/F/G=1-430.
DR PDBsum; 2M5S; -.
DR PDBsum; 2XYY; -.
DR PDBsum; 2XYZ; -.
DR PDBsum; 3IYH; -.
DR PDBsum; 3IYI; -.
DR PDBsum; 5UU5; -.
DR SMR; P26747; -.
DR DIP; DIP-29111N; -.
DR IntAct; P26747; 1.
DR PRIDE; P26747; -.
DR GeneID; 1262831; -.
DR KEGG; vg:1262831; -.
DR EvolutionaryTrace; P26747; -.
DR Proteomes; UP000001315; Genome.
DR Proteomes; UP000001795; Genome.
DR Proteomes; UP000001796; Genome.
DR Proteomes; UP000002165; Genome.
DR Proteomes; UP000007960; Genome.
DR GO; GO:0039620; C:T=7 icosahedral viral capsid; IDA:UniProtKB.
DR GO; GO:0019028; C:viral capsid; IDA:CAFA.
DR GO; GO:0046729; C:viral procapsid; IDA:CAFA.
DR GO; GO:0042802; F:identical protein binding; IDA:CAFA.
DR GO; GO:0046797; P:viral procapsid maturation; IDA:CAFA.
DR InterPro; IPR024659; Phage_coat_Gp5.
DR Pfam; PF11651; P22_CoatProtein; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Capsid protein; Direct protein sequencing; Late protein;
KW Reference proteome; T=7 icosahedral capsid protein; Virion.
FT INIT_MET 1
FT /note="Removed; by host"
FT /evidence="ECO:0000269|PubMed:1853558"
FT CHAIN 2..430
FT /note="Major capsid protein"
FT /id="PRO_0000077752"
FT REGION 2..56
FT /note="Binding to the capsid assembly scaffolding protein"
FT /evidence="ECO:0000269|PubMed:24600011"
FT REGION 223..345
FT /note="I domain"
FT /evidence="ECO:0000269|PubMed:24126914"
FT SITE 14
FT /note="Essential for binding to the capsid assembly
FT scaffolding protein"
FT /evidence="ECO:0000269|PubMed:24600011"
FT SITE 61
FT /note="Involved in capsid stabilization and maturation"
FT /evidence="ECO:0000269|PubMed:31068429"
FT MUTAGEN 5
FT /note="E->A: Impaired phage growth; probable capsid protein
FT misfolding."
FT /evidence="ECO:0000269|PubMed:24600011"
FT MUTAGEN 14
FT /note="D->A: Impaired phage growth; inability of the mutant
FT capsid protein to interact properly with scaffolding
FT protein."
FT /evidence="ECO:0000269|PubMed:24600011"
FT MUTAGEN 15
FT /note="E->A: Decreased phage growth."
FT /evidence="ECO:0000269|PubMed:24600011"
FT MUTAGEN 18
FT /note="E->A: Decreased phage growth."
FT /evidence="ECO:0000269|PubMed:24600011"
FT MUTAGEN 61
FT /note="W->N,V: Drastically decreases capsid stability."
FT /evidence="ECO:0000269|PubMed:31068429"
FT MUTAGEN 241
FT /note="W->A: Cold-sensitive phenotype probably due to an
FT assembly defect."
FT /evidence="ECO:0000269|PubMed:26269173"
FT MUTAGEN 242
FT /note="Q->A: Cold-sensitive phenotype probably due to an
FT assembly defect."
FT /evidence="ECO:0000269|PubMed:26269173"
FT MUTAGEN 243
FT /note="L->A: No effect on phage production."
FT /evidence="ECO:0000269|PubMed:26269173"
FT MUTAGEN 244
FT /note="D->A: Lethal. Complete loss of procapsids assembly."
FT /evidence="ECO:0000269|PubMed:26269173"
FT MUTAGEN 245
FT /note="N->A: Slight decrease in phage production."
FT /evidence="ECO:0000269|PubMed:26269173"
FT MUTAGEN 246
FT /note="D->A: Lethal. Complete loss of procapsids assembly,
FT assembles as tubes instead."
FT /evidence="ECO:0000269|PubMed:26269173"
FT MUTAGEN 249
FT /note="K->A: No effect on phage production."
FT /evidence="ECO:0000269|PubMed:26269173"
FT MUTAGEN 251
FT /note="N->A: Cold-sensitive phenotype probably due to an
FT assembly defect."
FT /evidence="ECO:0000269|PubMed:26269173"
FT MUTAGEN 377
FT /note="K->A: No effect on phage growth."
FT /evidence="ECO:0000269|PubMed:24600011"
FT MUTAGEN 385
FT /note="D->A: No effect on phage growth."
FT /evidence="ECO:0000269|PubMed:24600011"
FT HELIX 26..29
FT /evidence="ECO:0007829|PDB:5UU5"
FT STRAND 30..33
FT /evidence="ECO:0007829|PDB:5UU5"
FT HELIX 37..42
FT /evidence="ECO:0007829|PDB:5UU5"
FT STRAND 45..50
FT /evidence="ECO:0007829|PDB:5UU5"
FT STRAND 74..78
FT /evidence="ECO:0007829|PDB:5UU5"
FT STRAND 83..90
FT /evidence="ECO:0007829|PDB:5UU5"
FT HELIX 91..94
FT /evidence="ECO:0007829|PDB:5UU5"
FT HELIX 99..125
FT /evidence="ECO:0007829|PDB:5UU5"
FT STRAND 128..135
FT /evidence="ECO:0007829|PDB:5UU5"
FT TURN 140..142
FT /evidence="ECO:0007829|PDB:5UU5"
FT HELIX 143..157
FT /evidence="ECO:0007829|PDB:5UU5"
FT STRAND 166..170
FT /evidence="ECO:0007829|PDB:5UU5"
FT HELIX 172..182
FT /evidence="ECO:0007829|PDB:5UU5"
FT HELIX 183..185
FT /evidence="ECO:0007829|PDB:5UU5"
FT HELIX 193..196
FT /evidence="ECO:0007829|PDB:5UU5"
FT TURN 197..199
FT /evidence="ECO:0007829|PDB:5UU5"
FT STRAND 200..204
FT /evidence="ECO:0007829|PDB:5UU5"
FT HELIX 205..207
FT /evidence="ECO:0007829|PDB:5UU5"
FT STRAND 210..213
FT /evidence="ECO:0007829|PDB:5UU5"
FT STRAND 228..232
FT /evidence="ECO:0007829|PDB:2M5S"
FT STRAND 240..243
FT /evidence="ECO:0007829|PDB:5UU5"
FT STRAND 249..251
FT /evidence="ECO:0007829|PDB:5UU5"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:2M5S"
FT STRAND 257..262
FT /evidence="ECO:0007829|PDB:5UU5"
FT STRAND 272..281
FT /evidence="ECO:0007829|PDB:5UU5"
FT STRAND 283..285
FT /evidence="ECO:0007829|PDB:5UU5"
FT STRAND 288..297
FT /evidence="ECO:0007829|PDB:5UU5"
FT STRAND 302..310
FT /evidence="ECO:0007829|PDB:5UU5"
FT STRAND 313..316
FT /evidence="ECO:0007829|PDB:5UU5"
FT TURN 322..324
FT /evidence="ECO:0007829|PDB:5UU5"
FT HELIX 325..327
FT /evidence="ECO:0007829|PDB:5UU5"
FT STRAND 330..332
FT /evidence="ECO:0007829|PDB:5UU5"
FT STRAND 336..342
FT /evidence="ECO:0007829|PDB:5UU5"
FT STRAND 351..355
FT /evidence="ECO:0007829|PDB:5UU5"
FT STRAND 359..363
FT /evidence="ECO:0007829|PDB:5UU5"
FT HELIX 371..373
FT /evidence="ECO:0007829|PDB:5UU5"
FT STRAND 376..382
FT /evidence="ECO:0007829|PDB:5UU5"
FT TURN 384..386
FT /evidence="ECO:0007829|PDB:5UU5"
FT STRAND 389..397
FT /evidence="ECO:0007829|PDB:5UU5"
FT TURN 398..401
FT /evidence="ECO:0007829|PDB:5UU5"
FT STRAND 402..409
FT /evidence="ECO:0007829|PDB:5UU5"
FT STRAND 411..416
FT /evidence="ECO:0007829|PDB:5UU5"
FT TURN 418..420
FT /evidence="ECO:0007829|PDB:5UU5"
FT STRAND 421..426
FT /evidence="ECO:0007829|PDB:5UU5"
SQ SEQUENCE 430 AA; 46752 MW; BBDF63575C4B3899 CRC64;
MALNEGQIVT LAVDEIIETI SAITPMAQKA KKYTPPAASM QRSSNTIWMP VEQESPTQEG
WDLTDKATGL LELNVAVNMG EPDNDFFQLR ADDLRDETAY RRRIQSAARK LANNVELKVA
NMAAEMGSLV ITSPDAIGTN TADAWNFVAD AEEIMFSREL NRDMGTSYFF NPQDYKKAGY
DLTKRDIFGR IPEEAYRDGT IQRQVAGFDD VLRSPKLPVL TKSTATGITV SGAQSFKPVA
WQLDNDGNKV NVDNRFATVT LSATTGMKRG DKISFAGVKF LGQMAKNVLA QDATFSVVRV
VDGTHVEITP KPVALDDVSL SPEQRAYANV NTSLADAMAV NILNVKDART NVFWADDAIR
IVSQPIPANH ELFAGMKTTS FSIPDVGLNG IFATQGDIST LSGLCRIALW YGVNATRPEA
IGVGLPGQTA
