PORTL_BPP22
ID PORTL_BPP22 Reviewed; 725 AA.
AC P26744; Q7PCI7;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 02-JUN-2021, entry version 82.
DE RecName: Full=Portal protein {ECO:0000305};
DE AltName: Full=Gene product 1 {ECO:0000305};
DE Short=Gp1;
DE AltName: Full=Head-to-tail connector {ECO:0000305};
GN Name=1;
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 2-6.
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 MUTAGENESIS OF VAL-64 AND VAL-303, AND FUNCTION.
RX PubMed=28242514; DOI=10.1016/j.virol.2017.02.019;
RA Bedwell G.J., Prevelige P.E. Jr.;
RT "Targeted mutagenesis of the P22 portal protein reveals the mechanism of
RT signal transmission during DNA packaging.";
RL Virology 505:127-138(2017).
RN [5]
RP FUNCTION.
RX PubMed=30787152; DOI=10.1128/jvi.00187-19;
RA Motwani T., Teschke C.M.;
RT "Architect of Virus Assembly: the Portal Protein Nucleates Procapsid
RT Assembly in Bacteriophage P22.";
RL J. Virol. 93:0-0(2019).
RN [6] {ECO:0007744|PDB:3LJ5, ECO:0007744|PDB:4V4K}
RP X-RAY CRYSTALLOGRAPHY (3.25 ANGSTROMS) OF 1-602, SUBUNIT, AND FUNCTION.
RX PubMed=21499245; DOI=10.1038/nsmb.2023;
RA Olia A.S., Prevelige P.E. Jr., Johnson J.E., Cingolani G.;
RT "Three-dimensional structure of a viral genome-delivery portal vertex.";
RL Nat. Struct. Mol. Biol. 18:597-603(2011).
RN [7] {ECO:0007744|PDB:5JJ1, ECO:0007744|PDB:5JJ3}
RP X-RAY CRYSTALLOGRAPHY (3.30 ANGSTROMS) OF 1-602, FUNCTION, INTERACTION WITH
RP THE TERMINASE LARGE SUBUNIT, AND INTERACTION WITH GP4.
RX PubMed=28134243; DOI=10.1038/ncomms14310;
RA Lokareddy R.K., Sankhala R.S., Roy A., Afonine P.V., Motwani T.,
RA Teschke C.M., Parent K.N., Cingolani G.;
RT "Portal protein functions akin to a DNA-sensor that couples genome-
RT packaging to icosahedral capsid maturation.";
RL Nat. Commun. 8:14310-14310(2017).
CC -!- FUNCTION: Forms the portal vertex of the capsid (PubMed:21499245). This
CC portal plays critical roles in head assembly, genome packaging,
CC neck/tail attachment, and genome ejection (PubMed:30787152). Procapsid
CC assembly may initiate with a nucleation complex composed of portal and
CC scaffolding proteins (PubMed:30787152). The portal protein multimerizes
CC as a single ring-shaped homododecamer arranged around a central channel
CC (PubMed:21499245, PubMed:28134243). Switches upon genome packaging from
CC an asymmetrical conformation in the procapsid (PC-portal) to a
CC symmetrical ring in the mature capsid (MV-portal). This change of
CC conformation may serve as a signal for headful packaging
CC (PubMed:28134243). {ECO:0000269|PubMed:21499245,
CC ECO:0000269|PubMed:28134243, ECO:0000269|PubMed:30787152}.
CC -!- SUBUNIT: Homododecamer (PubMed:21499245). Interacts with the terminase
CC large subunit; this interaction allows the packaging of viral DNA
CC (PubMed:28134243). Interacts with gp4; this interaction participates in
CC the head completion (PubMed:28134243). {ECO:0000269|PubMed:21499245,
CC ECO:0000269|PubMed:28134243}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the p22likevirus portal protein family.
CC {ECO:0000305}.
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DR EMBL; M59749; AAA72961.1; -; Genomic_DNA.
DR EMBL; AF217253; AAF75045.1; -; Genomic_DNA.
DR EMBL; BK000583; DAA00985.1; -; Genomic_DNA.
DR PIR; C40474; Z1BP22.
DR RefSeq; YP_063735.1; NC_002371.2.
DR PDB; 3LJ5; X-ray; 7.50 A; A/B/C/D/E/F/G/H/I/J/K/L=1-725.
DR PDB; 4V4K; X-ray; 3.25 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=1-602.
DR PDB; 5GAI; EM; 10.50 A; A/B/C/D/E/F/G/H/I/J/W/X=5-721.
DR PDB; 5JJ1; X-ray; 3.30 A; A/B/C/D/E/F/G/H/I/J/K/L=1-602.
DR PDB; 5JJ3; X-ray; 7.00 A; A/B/C/D/E/F/G/H/I/J/K/L=1-725.
DR PDBsum; 3LJ5; -.
DR PDBsum; 4V4K; -.
DR PDBsum; 5GAI; -.
DR PDBsum; 5JJ1; -.
DR PDBsum; 5JJ3; -.
DR SMR; P26744; -.
DR DIP; DIP-59581N; -.
DR IntAct; P26744; 1.
DR TCDB; 1.W.1.1.1; the phage portal protein 1 (ppp1) family.
DR GeneID; 2944241; -.
DR KEGG; vg:2944241; -.
DR Proteomes; UP000001795; Genome.
DR Proteomes; UP000007960; Genome.
DR GO; GO:0046798; C:viral portal complex; IDA:UniProtKB.
DR GO; GO:0019073; P:viral DNA genome packaging; IMP:UniProtKB.
DR GO; GO:0098006; P:viral DNA genome packaging, headful; IMP:CACAO.
DR GO; GO:0099002; P:viral genome ejection through host cell envelope, short tail mechanism; IDA:UniProtKB.
DR GO; GO:0019068; P:virion assembly; IDA:UniProtKB.
DR InterPro; IPR032427; P22_portal.
DR Pfam; PF16510; P22_portal; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Capsid protein; Direct protein sequencing; Late protein;
KW Reference proteome; Viral capsid assembly;
KW Viral genome ejection through host cell envelope; Viral genome packaging;
KW Viral penetration into host cytoplasm; Viral release from host cell;
KW Viral short tail ejection system; Virion; Virus entry into host cell.
FT INIT_MET 1
FT /note="Removed; by host"
FT /evidence="ECO:0000269|PubMed:1853558"
FT CHAIN 2..725
FT /note="Portal protein"
FT /id="PRO_0000077747"
FT MUTAGEN 64
FT /note="V->A,T,M: Overpackaging."
FT /evidence="ECO:0000269|PubMed:28242514"
FT MUTAGEN 303
FT /note="V->A,T,M,Y: Overpackaging."
FT /evidence="ECO:0000269|PubMed:28242514"
FT TURN 15..17
FT /evidence="ECO:0007829|PDB:5JJ1"
FT HELIX 19..22
FT /evidence="ECO:0007829|PDB:5JJ1"
FT TURN 25..27
FT /evidence="ECO:0007829|PDB:5JJ1"
FT HELIX 28..30
FT /evidence="ECO:0007829|PDB:5JJ1"
FT TURN 31..39
FT /evidence="ECO:0007829|PDB:5JJ1"
FT HELIX 61..65
FT /evidence="ECO:0007829|PDB:5JJ1"
FT HELIX 67..71
FT /evidence="ECO:0007829|PDB:5JJ1"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:5JJ1"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:5JJ1"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:5JJ1"
FT HELIX 105..108
FT /evidence="ECO:0007829|PDB:5JJ1"
FT HELIX 110..114
FT /evidence="ECO:0007829|PDB:5JJ1"
FT STRAND 117..121
FT /evidence="ECO:0007829|PDB:5JJ1"
FT STRAND 131..135
FT /evidence="ECO:0007829|PDB:5JJ1"
FT TURN 181..184
FT /evidence="ECO:0007829|PDB:5JJ1"
FT HELIX 185..189
FT /evidence="ECO:0007829|PDB:5JJ1"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:5JJ1"
FT HELIX 239..241
FT /evidence="ECO:0007829|PDB:5JJ1"
FT HELIX 259..261
FT /evidence="ECO:0007829|PDB:5JJ1"
FT STRAND 294..296
FT /evidence="ECO:0007829|PDB:5JJ1"
FT STRAND 310..313
FT /evidence="ECO:0007829|PDB:5JJ1"
FT HELIX 320..323
FT /evidence="ECO:0007829|PDB:5JJ1"
FT TURN 324..328
FT /evidence="ECO:0007829|PDB:5JJ1"
FT HELIX 329..331
FT /evidence="ECO:0007829|PDB:5JJ1"
FT HELIX 332..343
FT /evidence="ECO:0007829|PDB:5JJ1"
FT HELIX 361..364
FT /evidence="ECO:0007829|PDB:5JJ1"
FT HELIX 401..415
FT /evidence="ECO:0007829|PDB:5JJ1"
FT HELIX 424..426
FT /evidence="ECO:0007829|PDB:5JJ1"
FT HELIX 431..434
FT /evidence="ECO:0007829|PDB:5JJ1"
FT TURN 435..437
FT /evidence="ECO:0007829|PDB:5JJ1"
FT TURN 439..441
FT /evidence="ECO:0007829|PDB:5JJ1"
FT HELIX 442..449
FT /evidence="ECO:0007829|PDB:5JJ1"
FT TURN 460..464
FT /evidence="ECO:0007829|PDB:5JJ1"
FT HELIX 466..469
FT /evidence="ECO:0007829|PDB:5JJ1"
FT STRAND 474..476
FT /evidence="ECO:0007829|PDB:5JJ1"
FT STRAND 526..529
FT /evidence="ECO:0007829|PDB:5JJ1"
FT TURN 530..532
FT /evidence="ECO:0007829|PDB:5JJ1"
FT HELIX 548..553
FT /evidence="ECO:0007829|PDB:5JJ1"
FT TURN 554..557
FT /evidence="ECO:0007829|PDB:5JJ1"
FT STRAND 560..563
FT /evidence="ECO:0007829|PDB:5JJ1"
FT HELIX 565..570
FT /evidence="ECO:0007829|PDB:5JJ1"
FT HELIX 575..578
FT /evidence="ECO:0007829|PDB:5JJ1"
SQ SEQUENCE 725 AA; 82743 MW; 264E03CAC14AB156 CRC64;
MADNENRLES ILSRFDADWT ASDEARREAK NDLFFSRVSQ WDDWLSQYTT LQYRGQFDVV
RPVVRKLVSE MRQNPIDVLY RPKDGARPDA ADVLMGMYRT DMRHNTAKIA VNIAVREQIE
AGVGAWRLVT DYEDQSPTSN NQVIRREPIH SACSHVIWDS NSKLMDKSDA RHCTVIHSMS
QNGWEDFAEK YDLDADDIPS FQNPNDWVFP WLTQDTIQIA EFYEVVEKKE TAFIYQDPVT
GEPVSYFKRD IKDVIDDLAD SGFIKIAERQ IKRRRVYKSI ITCTAVLKDK QLIAGEHIPI
VPVFGEWGFV EDKEVYEGVV RLTKDGQRLR NMIMSFNADI VARTPKKKPF FWPEQIAGFE
HMYDGNDDYP YYLLNRTDEN SGDLPTQPLA YYENPEVPQA NAYMLEAATS AVKEVATLGV
DTEAVNGGQV AFDTVNQLNM RADLETYVFQ DNLATAMRRD GEIYQSIVND IYDVPRNVTI
TLEDGSEKDV QLMAEVVDLA TGEKQVLNDI RGRYECYTDV GPSFQSMKQQ NRAEILELLG
KTPQGTPEYQ LLLLQYFTLL DGKGVEMMRD YANKQLIQMG VKKPETPEEQ QWLVEAQQAK
QGQQDPAMVQ AQGVLLQGQA ELAKAQNQTL SLQIDAAKVE AQNQLNAARI AEIFNNMDLS
KQSEFREFLK TVASFQQDRS EDARANAELL LKGDEQTHKQ RMDIANILQS QRQNQPSGSV
AETPQ
