PORTL_BPT4
ID PORTL_BPT4 Reviewed; 524 AA.
AC P13334; Q9T0U2;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 19-DEC-2001, sequence version 2.
DT 23-FEB-2022, entry version 83.
DE RecName: Full=Portal protein {ECO:0000255|HAMAP-Rule:MF_04114};
DE AltName: Full=Gene product 20;
DE AltName: Full=gp20 {ECO:0000255|HAMAP-Rule:MF_04114};
GN Name=20;
OS Enterobacteria phage T4 (Bacteriophage T4).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Myoviridae; Tevenvirinae; Tequatrovirus.
OX NCBI_TaxID=10665;
OH NCBI_TaxID=562; Escherichia coli.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=D;
RX PubMed=2798102; DOI=10.1093/nar/17.18.7514;
RA Marusich E.I., Mesyanzhinov V.V.;
RT "Nucleotide and deduced amino acid sequences of bacteriophage T4 gene 20.";
RL Nucleic Acids Res. 17:7514-7514(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12626685; DOI=10.1128/mmbr.67.1.86-156.2003;
RA Miller E.S., Kutter E., Mosig G., Arisaka F., Kunisawa T., Ruger W.;
RT "Bacteriophage T4 genome.";
RL Microbiol. Mol. Biol. Rev. 67:86-156(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-27.
RX PubMed=2963141; DOI=10.1128/jvi.62.3.882-886.1988;
RA Arisaka F., Ishimoto L., Kassavetis G., Kumazaki T., Ishii S.;
RT "Nucleotide sequence of the tail tube structural gene of bacteriophage
RT T4.";
RL J. Virol. 62:882-886(1988).
RN [4]
RP INTERACTION WITH THE MAJOR CAPSID PROTEIN, AND INTERACTION WITH THE CAPSID
RP VERTEX PROTEIN.
RX PubMed=6406677; DOI=10.1016/s0022-2836(83)80089-8;
RA Driedonks R.A., Caldentey J.;
RT "Gene 20 product of bacteriophage T4. II. Its structural organization in
RT prehead and bacteriophage.";
RL J. Mol. Biol. 166:341-360(1983).
RN [5]
RP FUNCTION.
RX PubMed=2685327; DOI=10.1016/0022-2836(89)90599-8;
RA Michaud G., Zachary A., Rao V.B., Black L.W.;
RT "Membrane-associated assembly of a phage T4 DNA entrance vertex structure
RT studied with expression vectors.";
RL J. Mol. Biol. 209:667-681(1989).
RN [6]
RP INTERACTION WITH THE LARGE TERMINASE SUBUNIT, AND SUBUNIT.
RX PubMed=10366503; DOI=10.1006/jmbi.1999.2781;
RA Lin H., Rao V.B., Black L.W.;
RT "Analysis of capsid portal protein and terminase functional domains:
RT interaction sites required for DNA packaging in bacteriophage T4.";
RL J. Mol. Biol. 289:249-260(1999).
RN [7]
RP REVIEW.
RX PubMed=21129201; DOI=10.1186/1743-422x-7-356;
RA Rao V.B., Black L.W.;
RT "Structure and assembly of bacteriophage T4 head.";
RL Virol. J. 7:356-356(2010).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=22855489; DOI=10.1128/jvi.01284-12;
RA Quinten T.A., Kuhn A.;
RT "Membrane interaction of the portal protein gp20 of bacteriophage T4.";
RL J. Virol. 86:11107-11114(2012).
RN [9]
RP FUNCTION.
RX PubMed=24126213; DOI=10.1016/j.jmb.2013.10.011;
RA Padilla-Sanchez V., Gao S., Kim H.R., Kihara D., Sun L., Rossmann M.G.,
RA Rao V.B.;
RT "Structure-function analysis of the DNA translocating portal of the
RT bacteriophage T4 packaging machine.";
RL J. Mol. Biol. 426:1019-1038(2014).
RN [10]
RP STRUCTURE BY ELECTRON MICROSCOPY (15.0 ANGSTROMS), AND SUBCELLULAR
RP LOCATION.
RX PubMed=11162794; DOI=10.1006/viro.2000.0735;
RA Olson N.H., Gingery M., Eiserling F.A., Baker T.S.;
RT "The structure of isometric capsids of bacteriophage T4.";
RL Virology 279:385-391(2001).
RN [11]
RP STRUCTURE BY ELECTRON MICROSCOPY (22.0 ANGSTROMS), AND FUNCTION.
RX PubMed=15071181; DOI=10.1073/pnas.0400444101;
RA Fokine A., Chipman P.R., Leiman P.G., Mesyanzhinov V.V., Rao V.B.,
RA Rossmann M.G.;
RT "Molecular architecture of the prolate head of bacteriophage T4.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:6003-6008(2004).
RN [12]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.6 ANGSTROMS), AND INTERACTION WITH THE
RP LARGE TERMINASE SUBUNIT.
RX PubMed=26144253; DOI=10.1038/ncomms8548;
RA Sun L., Zhang X., Gao S., Rao P.A., Padilla-Sanchez V., Chen Z., Sun S.,
RA Xiang Y., Subramaniam S., Rao V.B., Rossmann M.G.;
RT "Cryo-EM structure of the bacteriophage T4 portal protein assembly at near-
RT atomic resolution.";
RL Nat. Commun. 6:7548-7548(2015).
CC -!- FUNCTION: Forms the portal vertex of the capsid (PubMed:2685327,
CC PubMed:24126213). This portal plays critical roles in head assembly,
CC genome packaging, neck/tail attachment, and genome ejection. The portal
CC protein multimerizes as a single ring-shaped homododecamer arranged
CC around a central channel. Binds to the terminase subunits to form the
CC packaging machine. Attaches to the host inner membrane most likely
CC through interaction with host yidC and forms together with chaperone
CC gp40 an initiator complex to form the prohead. {ECO:0000255|HAMAP-
CC Rule:MF_04114, ECO:0000269|PubMed:15071181,
CC ECO:0000269|PubMed:22855489, ECO:0000269|PubMed:24126213,
CC ECO:0000269|PubMed:2685327}.
CC -!- SUBUNIT: Homododecamer. Interacts with the large terminase subunit.
CC Interacts with the major capsid protein. Interacts with the capsid
CC vertex protein. {ECO:0000255|HAMAP-Rule:MF_04114,
CC ECO:0000269|PubMed:10366503, ECO:0000269|PubMed:26144253,
CC ECO:0000269|PubMed:6406677}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04114,
CC ECO:0000269|PubMed:11162794}. Host cell inner membrane
CC {ECO:0000269|PubMed:22855489}. Note=Located at a unique 5-fold vertex
CC of the icosahedral capsid. Localization at the inner host membrane is
CC likely due to interactions with host membrane proteins such as yidC.
CC {ECO:0000255|HAMAP-Rule:MF_04114, ECO:0000269|PubMed:22855489}.
CC -!- SIMILARITY: Belongs to the Tevenvirinae portal protein family.
CC {ECO:0000255|HAMAP-Rule:MF_04114, ECO:0000305}.
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DR EMBL; X16055; CAA34190.1; -; Genomic_DNA.
DR EMBL; AF158101; AAD42425.1; -; Genomic_DNA.
DR EMBL; M19085; AAA32543.1; -; Genomic_DNA.
DR PIR; JU0161; VHBP20.
DR RefSeq; NP_049782.1; NC_000866.4.
DR PDB; 3JA7; EM; 3.63 A; A/B/C/D/E/F/G/H/I/J/K/L=74-524.
DR PDB; 6UZC; EM; 4.50 A; E/F/G/H/I/J/K/L/M/N/O/P=1-524.
DR PDBsum; 3JA7; -.
DR PDBsum; 6UZC; -.
DR SMR; P13334; -.
DR TCDB; 1.W.8.1.1; the (enterobacterial phage t4) portal protein 8 (ppp8) family.
DR GeneID; 1258582; -.
DR KEGG; vg:1258582; -.
DR Proteomes; UP000009087; Genome.
DR GO; GO:0020002; C:host cell plasma membrane; IDA:CACAO.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0046798; C:viral portal complex; IDA:CACAO.
DR GO; GO:0099000; P:viral genome ejection through host cell envelope, contractile tail mechanism; IEA:UniProtKB-UniRule.
DR GO; GO:0019072; P:viral genome packaging; IEA:UniProtKB-UniRule.
DR GO; GO:0019076; P:viral release from host cell; IEA:UniProtKB-UniRule.
DR HAMAP; MF_04114; PORTAL_T4; 1.
DR InterPro; IPR010823; Portal_Gp20.
DR Pfam; PF07230; Portal_Gp20; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Capsid protein; Coiled coil; Host cell inner membrane;
KW Host cell membrane; Host membrane; Membrane; Reference proteome;
KW Viral capsid assembly; Viral contractile tail ejection system;
KW Viral genome ejection through host cell envelope; Viral genome packaging;
KW Viral penetration into host cytoplasm; Viral release from host cell;
KW Virion; Virus entry into host cell.
FT CHAIN 1..524
FT /note="Portal protein"
FT /id="PRO_0000165010"
FT REGION 500..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 486..516
FT /evidence="ECO:0000255"
FT COMPBIAS 500..517
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 125
FT /note="M -> I (in Ref. 1; CAA34190)"
FT /evidence="ECO:0000305"
FT CONFLICT 141
FT /note="R -> Q (in Ref. 1; CAA34190)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 524 AA; 61032 MW; 1AF808425CBA84E4 CRC64;
MKFNVLSLFA PWAKMDERNF KDQEKEDLVS ITAPKLDDGA REFEVSSNEA ASPYNAAFQT
IFGSYEPGMK TTRELIDTYR NLMNNYEVDN AVSEIVSDAI VYEDDTEVVA LNLDKSKFSP
KIKNMMLDEF SDVLNHLSFQ RKGSDHFRRW YVDSRIFFHK IIDPKRPKEG IKELRRLDPR
QVQYVREIIT ETEAGTKIVK GYKEYFIYDT AHESYACDGR MYEAGTKIKI PKAAVVYAHS
GLVDCCGKNI IGYLHRAVKP ANQLKLLEDA VVIYRITRAP DRRVWYVDTG NMPARKAAEH
MQHVMNTMKN RVVYDASTGK IKNQQHNMSM TEDYWLQRRD GKAVTEVDTL PGADNTGNME
DIRWFRQALY MALRVPLSRI PQDQQGGVMF DSGTSITRDE LTFAKFIREL QHKFEEVFLD
PLKTNLLLKG IITEDEWNDE INNIKIEFHR DSYFAELKEA EILERRINML TMAEPFIGKY
ISHRTAMKDI LQMTDEEIEQ EAKQIEEESK EARFQDPDQE QEDF
