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 10-JUN-2026, entry version 109. 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 Caudoviricetes incertae sedis; Salasmaviridae; Picovirinae; Salasvirus; OC Salasvirus phi29. OX NCBI_TaxID=2884424; 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:11130079, PubMed:15886394). 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 EMDB; EMD-4662; -. DR EMDB; EMD-4678; -. DR EMDB; EMD-4679; -. DR EMDB; EMD-4684; -. DR EMDB; EMD-4685; -. 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; Segment. 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:0099002; P:symbiont genome ejection through host cell envelope, short tail mechanism; IEA:UniProtKB-KW. DR GO; GO:0019073; P:viral DNA genome packaging; IDA:UniProtKB. DR Gene3D; 1.10.246.30; -; 1. DR Gene3D; 3.30.1350.20; Bacteriophage PHI-29 conector. Domain 3; 1. DR Gene3D; 2.40.500.10; Upper collar protein gp10 (connector protein); 1. DR InterPro; IPR008016; Gp10. DR InterPro; IPR036199; Gp10_sf. DR Pfam; PF05352; Phage_connector; 1. DR SUPFAM; SSF56826; Upper collar protein gp10 (connector protein); 1. 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; -. 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 202..204 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 //