PORTL_BPPH2
ID PORTL_BPPH2 Reviewed; 309 AA.
AC P04332; B3VMP6;
DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-1987, sequence version 1.
DT 23-FEB-2022, entry version 100.
DE RecName: Full=Portal protein {ECO:0000305};
DE AltName: Full=Connector protein {ECO:0000303|PubMed:6096227};
DE AltName: Full=Gene product 10 {ECO:0000305};
DE Short=gp10 {ECO:0000305};
DE AltName: Full=Gene product 19;
DE Short=gp19;
DE AltName: Full=Head-to-tail connector {ECO:0000303|PubMed:11562162};
DE AltName: Full=Probable portal protein;
DE AltName: Full=Protein p10 {ECO:0000305};
DE AltName: Full=Upper collar protein {ECO:0000305};
GN Name=10;
OS Bacillus phage phi29 (Bacteriophage phi-29).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Salasmaviridae; Picovirinae; Salasvirus.
OX NCBI_TaxID=10756;
OH NCBI_TaxID=1423; Bacillus subtilis.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3803926; DOI=10.1016/0378-1119(86)90406-3;
RA Vlcek C., Paces V.;
RT "Nucleotide sequence of the late region of Bacillus phage phi 29 completes
RT the 19,285-bp sequence of phi 29 genome. Comparison with the homologous
RT sequence of phage PZA.";
RL Gene 46:215-225(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6096227; DOI=10.1016/0378-1119(84)90108-2;
RA Garcia J.A., Mendez E., Salas M.;
RT "Cloning, nucleotide sequence and high level expression of the gene coding
RT for the connector protein of Bacillus subtilis phage phi 29.";
RL Gene 30:87-98(1984).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Villegas A.P., Lingohr E.J., Ceyssens P.-J., Kropinski A.M.;
RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION.
RX PubMed=10801350; DOI=10.1006/jmbi.2000.3712;
RA Ibarra B., Caston J.R., Llorca O., Valle M., Valpuesta J.M.,
RA Carrascosa J.L.;
RT "Topology of the components of the DNA packaging machinery in the phage
RT phi29 prohead.";
RL J. Mol. Biol. 298:807-815(2000).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=11562162; DOI=10.1006/jsbi.2001.4375;
RA Peterson C., Simon M., Hodges J., Mertens P., Higgins L., Egelman E.,
RA Anderson D.;
RT "Composition and mass of the bacteriophage phi29 prohead and virion.";
RL J. Struct. Biol. 135:18-25(2001).
RN [6]
RP INTERACTION WITH PACKAGING RNA.
RX PubMed=15886394; DOI=10.1093/nar/gki554;
RA Xiao F., Moll W.D., Guo S., Guo P.;
RT "Binding of pRNA to the N-terminal 14 amino acids of connector protein of
RT bacteriophage phi29.";
RL Nucleic Acids Res. 33:2640-2649(2005).
RN [7]
RP FUNCTION.
RX PubMed=19744688; DOI=10.1016/j.virol.2009.08.016;
RA Fu C.Y., Prevelige P.E. Jr.;
RT "In vitro incorporation of the phage Phi29 connector complex.";
RL Virology 394:149-153(2009).
RN [8]
RP FUNCTION.
RX PubMed=21570409; DOI=10.1016/j.jmb.2011.04.070;
RA Grimes S., Ma S., Gao J., Atz R., Jardine P.J.;
RT "Role of phi29 connector channel loops in late-stage DNA packaging.";
RL J. Mol. Biol. 410:50-59(2011).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS), SUBUNIT, AND FUNCTION.
RX PubMed=11130079; DOI=10.1038/35047129;
RA Simpson A.A., Tao Y., Leiman P.G., Badasso M.O., He Y., Jardine P.J.,
RA Olson N.H., Morais M.C., Grimes S., Anderson D.L., Baker T.S.,
RA Rossmann M.G.;
RT "Structure of the bacteriophage phi29 DNA packaging motor.";
RL Nature 408:745-750(2000).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS), AND SUBUNIT.
RX PubMed=11526317; DOI=10.1107/s0907444901010435;
RA Simpson A.A., Leiman P.G., Tao Y., He Y., Badasso M.O., Jardine P.J.,
RA Anderson D.L., Rossmann M.G.;
RT "Structure determination of the head-tail connector of bacteriophage
RT phi29.";
RL Acta Crystallogr. D 57:1260-1269(2001).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS), SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=11812138; DOI=10.1006/jmbi.2001.5278;
RA Guasch A., Pous J., Ibarra B., Gomis-Ruth F.X., Valpuesta J.M., Sousa N.,
RA Carrascosa J.L., Coll M.;
RT "Detailed architecture of a DNA translocating machine: the high-resolution
RT structure of the bacteriophage phi29 connector particle.";
RL J. Mol. Biol. 315:663-676(2002).
CC -!- FUNCTION: Forms the portal vertex of the capsid (PubMed:10801350)
CC (PubMed:19744688, PubMed:21570409). This portal plays critical roles in
CC head assembly, genome packaging, neck/tail attachment, and genome
CC ejection (By similarity). The portal protein multimerizes as a single
CC ring-shaped homododecamer arranged around a central channel
CC (PubMed:11812138, PubMed:21570409). Binds to the 6 packaging RNA
CC molecules (pRNA) forming a double-ring structure which in turn binds to
CC the ATPase gp16 hexamer, forming the active DNA-translocating motor
CC (PubMed:15886394, PubMed:11130079). This complex is essential for the
CC specificity of packaging from the left DNA end.
CC {ECO:0000250|UniProtKB:P13334, ECO:0000269|PubMed:11130079,
CC ECO:0000269|PubMed:11812138, ECO:0000269|PubMed:15886394,
CC ECO:0000269|PubMed:19744688, ECO:0000269|PubMed:21570409,
CC ECO:0000305|PubMed:10801350}.
CC -!- SUBUNIT: Homododecamer (PubMed:11130079, PubMed:11526317)
CC (PubMed:11812138). Interacts (via N-terminus) with the pRNA
CC (PubMed:15886394). {ECO:0000269|PubMed:11130079,
CC ECO:0000269|PubMed:11526317, ECO:0000269|PubMed:11812138,
CC ECO:0000269|PubMed:15886394}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:11562162}.
CC Note=Present in 12 copies in the virion. {ECO:0000269|PubMed:11562162,
CC ECO:0000269|PubMed:11812138}.
CC -!- SIMILARITY: Belongs to the phi29likevirus portal protein family.
CC {ECO:0000305}.
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DR EMBL; M14782; AAA32283.1; -; Genomic_DNA.
DR EMBL; M12456; AAA32292.1; -; Genomic_DNA.
DR EMBL; EU771092; ACE96033.1; -; Genomic_DNA.
DR PIR; E25816; WMBPC9.
DR RefSeq; YP_002004539.1; NC_011048.1.
DR PDB; 1FOU; X-ray; 3.20 A; A/B/C/D/E/F/G/H/I/J/K/L=1-309.
DR PDB; 1H5W; X-ray; 2.10 A; A/B/C=1-309.
DR PDB; 1IJG; X-ray; 2.90 A; A/B/C/D/E/F/G/H/I/J/K/L=1-309.
DR PDB; 1JNB; X-ray; 3.20 A; A/B/C/D/E/F/G/H/I/J/K/L=1-309.
DR PDB; 6QX7; EM; 3.80 A; 0a/0b/0c/0d/0e/0f/0g/0h/0i/0j/0k/0l=1-309.
DR PDB; 6QYJ; EM; 3.40 A; 0a/0b/0c/0d/0e/0f/0g/0h/0i/0j/0k/0l=1-309.
DR PDB; 6QYM; EM; 3.60 A; 0a/0b/0c/0d/0e/0f/0g/0h/0i/0j/0k/0l=1-309.
DR PDB; 6QZ9; EM; 3.30 A; 0a/0b/0c/0d/0e/0f/0g/0h/0i/0j/0k/0l=1-309.
DR PDB; 6QZF; EM; 3.80 A; 0a/0b/0c/0d/0e/0f/0g/0h/0i/0j/0k/0l=1-309.
DR PDBsum; 1FOU; -.
DR PDBsum; 1H5W; -.
DR PDBsum; 1IJG; -.
DR PDBsum; 1JNB; -.
DR PDBsum; 6QX7; -.
DR PDBsum; 6QYJ; -.
DR PDBsum; 6QYM; -.
DR PDBsum; 6QZ9; -.
DR PDBsum; 6QZF; -.
DR SMR; P04332; -.
DR TCDB; 1.W.6.1.1; the (bacillus phage phi29) portal protein 6 (ppp6) family.
DR GeneID; 6446518; -.
DR KEGG; vg:6446518; -.
DR EvolutionaryTrace; P04332; -.
DR Proteomes; UP000001207; Genome.
DR GO; GO:0046798; C:viral portal complex; IDA:UniProtKB.
DR GO; GO:0046729; C:viral procapsid; IDA:CACAO.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0019073; P:viral DNA genome packaging; IDA:UniProtKB.
DR GO; GO:0099002; P:viral genome ejection through host cell envelope, short tail mechanism; IEA:UniProtKB-KW.
DR InterPro; IPR008016; Gp10.
DR InterPro; IPR036199; Gp10_sf.
DR Pfam; PF05352; Phage_connector; 1.
DR SUPFAM; SSF56826; SSF56826; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Capsid protein; Late protein; Reference proteome;
KW RNA-binding; 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 CHAIN 1..309
FT /note="Portal protein"
FT /id="PRO_0000106586"
FT REGION 1..14
FT /note="Binding to the pRNA"
FT /evidence="ECO:0000269|PubMed:15886394"
FT HELIX 14..16
FT /evidence="ECO:0007829|PDB:1FOU"
FT HELIX 18..36
FT /evidence="ECO:0007829|PDB:1H5W"
FT STRAND 38..43
FT /evidence="ECO:0007829|PDB:1H5W"
FT HELIX 50..60
FT /evidence="ECO:0007829|PDB:1H5W"
FT STRAND 61..68
FT /evidence="ECO:0007829|PDB:1H5W"
FT TURN 69..71
FT /evidence="ECO:0007829|PDB:1H5W"
FT STRAND 72..76
FT /evidence="ECO:0007829|PDB:1H5W"
FT STRAND 78..82
FT /evidence="ECO:0007829|PDB:1H5W"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:1FOU"
FT STRAND 92..96
FT /evidence="ECO:0007829|PDB:1H5W"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:1FOU"
FT STRAND 101..106
FT /evidence="ECO:0007829|PDB:1H5W"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:1H5W"
FT STRAND 118..124
FT /evidence="ECO:0007829|PDB:1H5W"
FT HELIX 131..154
FT /evidence="ECO:0007829|PDB:1H5W"
FT STRAND 159..163
FT /evidence="ECO:0007829|PDB:1H5W"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:1H5W"
FT HELIX 171..176
FT /evidence="ECO:0007829|PDB:1H5W"
FT STRAND 180..183
FT /evidence="ECO:0007829|PDB:1H5W"
FT STRAND 195..200
FT /evidence="ECO:0007829|PDB:1H5W"
FT HELIX 207..224
FT /evidence="ECO:0007829|PDB:1H5W"
FT HELIX 247..272
FT /evidence="ECO:0007829|PDB:1H5W"
FT STRAND 277..281
FT /evidence="ECO:0007829|PDB:1H5W"
SQ SEQUENCE 309 AA; 35878 MW; F5B01C1BE17FDE60 CRC64;
MARKRSNTYR SINEIQRQKR NRWFIHYLNY LQSLAYQLFE WENLPPTINP SFLEKSIHQF
GYVGFYKDPV ISYIACNGAL SGQRDVYNQA TVFRAASPVY QKEFKLYNYR DMKEEDMGVV
IYNNDMAFPT TPTLELFAAE LAELKEIISV NQNAQKTPVL IRANDNNQLS LKQVYNQYEG
NAPVIFAHEA LDSDSIEVFK TDAPYVVDKL NAQKNAVWNE MMTFLGIKNA NLEKKERMVT
DEVSSNDEQI ESSGTVFLKS REEACEKINE LYGLNVKVKF RYDIVEQMRR ELQQIENVSR
GTSDGETNE
