PORTL_BPSPP
ID PORTL_BPSPP Reviewed; 503 AA.
AC P54309;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 29-SEP-2021, entry version 90.
DE RecName: Full=Portal protein {ECO:0000305};
DE AltName: Full=Gene product 6 {ECO:0000305};
DE Short=gp6;
DE AltName: Full=Portal vertex protein {ECO:0000305};
GN Name=6; Synonyms=siz;
OS Bacillus phage SPP1 (Bacteriophage SPP1).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Siphoviridae.
OX NCBI_TaxID=10724;
OH NCBI_TaxID=1423; Bacillus subtilis.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION, AND MUTAGENESIS OF
RP GLU-251; ASN-365 AND GLU-424.
RX PubMed=1583695; DOI=10.1016/0022-2836(92)91027-m;
RA Tavares P., Santos M.A., Lurz R., Morelli G., de Lencastre H.,
RA Trautner T.A.;
RT "Identification of a gene in Bacillus subtilis bacteriophage SPP1
RT determining the amount of packaged DNA.";
RL J. Mol. Biol. 225:81-92(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=9434185; DOI=10.1016/s0378-1119(97)00547-7;
RA Alonso J.C., Luder G., Stiege A.C., Chai S., Weise F., Trautner T.A.;
RT "The complete nucleotide sequence and functional organization of Bacillus
RT subtilis bacteriophage SPP1.";
RL Gene 204:201-212(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-37.
RX PubMed=1548711; DOI=10.1016/0022-2836(92)90578-8;
RA Chai S., Bravo A., Lueder G., Nedlin A., Trautner T.A., Alonso J.C.;
RT "Molecular analysis of the Bacillus subtilis bacteriophage SPP1 region
RT encompassing genes 1 to 6. The products of gene 1 and gene 2 are required
RT for pac cleavage.";
RL J. Mol. Biol. 224:87-102(1992).
RN [4]
RP SUBUNIT.
RX PubMed=8890151;
RA van Heel M., Orlova E.V., Dube P., Tavares P.;
RT "Intrinsic versus imposed curvature in cyclical oligomers: the portal
RT protein of bacteriophage SPP1.";
RL EMBO J. 15:4785-4788(1996).
RN [5]
RP FUNCTION, AND INTERACTION WITH THE GP7 PROTEIN.
RX PubMed=10656821; DOI=10.1006/jmbi.1999.3450;
RA Droege A., Santos M.A., Stiege A.C., Alonso J.C., Lurz R., Trautner T.A.,
RA Tavares P.;
RT "Shape and DNA packaging activity of bacteriophage SPP1 procapsid: protein
RT components and interactions during assembly.";
RL J. Mol. Biol. 296:117-132(2000).
RN [6]
RP INTERACTION WITH THE GP7 PROTEIN.
RX PubMed=12940981; DOI=10.1046/j.1365-2958.2003.03631.x;
RA Stiege A.C., Isidro A., Droege A., Tavares P.;
RT "Specific targeting of a DNA-binding protein to the SPP1 procapsid by
RT interaction with the portal oligomer.";
RL Mol. Microbiol. 49:1201-1212(2003).
RN [7]
RP FUNCTION.
RX PubMed=14763972; DOI=10.1046/j.1365-2958.2003.03880.x;
RA Isidro A., Santos M.A., Henriques A.O., Tavares P.;
RT "The high-resolution functional map of bacteriophage SPP1 portal protein.";
RL Mol. Microbiol. 51:949-962(2004).
RN [8] {ECO:0007744|PDB:2JES}
RP X-RAY CRYSTALLOGRAPHY (3.40 ANGSTROMS), SUBUNIT, AND FUNCTION.
RX PubMed=17363899; DOI=10.1038/sj.emboj.7601643;
RA Lebedev A.A., Krause M.H., Isidro A.L., Vagin A.A., Orlova E.V., Turner J.,
RA Dodson E.J., Tavares P., Antson A.A.;
RT "Structural framework for DNA translocation via the viral portal protein.";
RL EMBO J. 26:1984-1994(2007).
RN [9] {ECO:0007744|PDB:5A20, ECO:0007744|PDB:5A21}
RP STRUCTURE BY ELECTRON MICROSCOPY (7.20 ANGSTROMS), AND INTERACTION WITH THE
RP CONNECTOR PROTEIN GP15.
RX PubMed=25991862; DOI=10.1073/pnas.1504039112;
RA Chaban Y., Lurz R., Brasiles S., Cornilleau C., Karreman M.,
RA Zinn-Justin S., Tavares P., Orlova E.V.;
RT "Structural rearrangements in the phage head-to-tail interface during
RT assembly and infection.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:7009-7014(2015).
CC -!- FUNCTION: Forms the portal vertex of the capsid (PubMed:17363899). This
CC portal plays critical roles in head assembly, genome packaging,
CC neck/tail attachment, and genome ejection. The portal protein
CC multimerizes as a single ring-shaped homododecamer arranged around a
CC central channel. Binds to the terminase subunits to form the packaging
CC machine. Necessary to ensure correct procapsid size during capsid
CC assembly. Once the capsid is packaged with the DNA, the terminase
CC complex is substituted by the connector proteins gp15.
CC {ECO:0000269|PubMed:17363899, ECO:0000305|PubMed:14763972}.
CC -!- SUBUNIT: Homododecamer (PubMed:8890151, PubMed:17363899). Has been seen
CC as 13-mer and 14-mer multimer in experiments, but assembles as
CC homododecamer in vivo (PubMed:8890151, PubMed:17363899). Interacts with
CC the gp7 protein (PubMed:10656821, PubMed:12940981). Interacts with the
CC connector proteins gp15; this interaction occurs at the end of the
CC packaging when the terminase complex is replaced by the connector
CC (PubMed:25991862). {ECO:0000269|PubMed:10656821,
CC ECO:0000269|PubMed:12940981, ECO:0000269|PubMed:17363899,
CC ECO:0000269|PubMed:25991862, ECO:0000269|PubMed:8890151}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000250|UniProtKB:P03710}.
CC -!- SIMILARITY: Belongs to the SPP1-like portal protein family.
CC {ECO:0000305}.
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DR EMBL; X56064; CAA39541.1; -; Genomic_DNA.
DR EMBL; X97918; CAA66580.1; -; Genomic_DNA.
DR PIR; S21805; S21805.
DR RefSeq; NP_690661.1; NC_004166.2.
DR PDB; 2JES; X-ray; 3.40 A; A/C/E/G/I/K/M/O/Q/S/U/W/Y=1-503.
DR PDB; 5A20; EM; 7.60 A; A/B=1-503.
DR PDB; 5A21; EM; 7.20 A; A/B=1-503.
DR PDBsum; 2JES; -.
DR PDBsum; 5A20; -.
DR PDBsum; 5A21; -.
DR SMR; P54309; -.
DR TCDB; 1.W.7.1.1; the (bacillus phage spp1) portal protein 7 (ppp7) family.
DR GeneID; 955279; -.
DR KEGG; vg:955279; -.
DR EvolutionaryTrace; P54309; -.
DR Proteomes; UP000002559; Genome.
DR GO; GO:0046798; C:viral portal complex; IDA:UniProtKB.
DR GO; GO:0046729; C:viral procapsid; IDA:CACAO.
DR GO; GO:0098006; P:viral DNA genome packaging, headful; IMP:CACAO.
DR GO; GO:0099001; P:viral genome ejection through host cell envelope, long flexible tail mechanism; IEA:UniProtKB-KW.
DR InterPro; IPR021145; Portal_protein.
DR InterPro; IPR006428; Portal_SPP1-type.
DR Pfam; PF05133; Phage_prot_Gp6; 1.
DR TIGRFAMs; TIGR01538; portal_SPP1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Capsid protein; Reference proteome; Viral capsid assembly;
KW Viral genome ejection through host cell envelope; Viral genome packaging;
KW Viral long flexible tail ejection system;
KW Viral penetration into host cytoplasm; Viral release from host cell;
KW Virion; Virus entry into host cell.
FT CHAIN 1..503
FT /note="Portal protein"
FT /id="PRO_0000077792"
FT REGION 463..503
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..490
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 251
FT /note="E->K: In siz S; 4% reduction in DNA packaging."
FT MUTAGEN 365
FT /note="N->K: In siz A; 6% reduction in DNA packaging."
FT MUTAGEN 424
FT /note="E->K: In siz X; 6% reduction in DNA packaging."
FT HELIX 31..40
FT /evidence="ECO:0007829|PDB:2JES"
FT HELIX 44..53
FT /evidence="ECO:0007829|PDB:2JES"
FT HELIX 58..61
FT /evidence="ECO:0007829|PDB:2JES"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:2JES"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:2JES"
FT HELIX 88..100
FT /evidence="ECO:0007829|PDB:2JES"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:2JES"
FT HELIX 112..121
FT /evidence="ECO:0007829|PDB:2JES"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:2JES"
FT HELIX 125..140
FT /evidence="ECO:0007829|PDB:2JES"
FT STRAND 141..149
FT /evidence="ECO:0007829|PDB:2JES"
FT STRAND 155..160
FT /evidence="ECO:0007829|PDB:2JES"
FT TURN 162..164
FT /evidence="ECO:0007829|PDB:2JES"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:2JES"
FT STRAND 245..252
FT /evidence="ECO:0007829|PDB:2JES"
FT HELIX 256..259
FT /evidence="ECO:0007829|PDB:2JES"
FT HELIX 261..280
FT /evidence="ECO:0007829|PDB:2JES"
FT STRAND 285..292
FT /evidence="ECO:0007829|PDB:2JES"
FT HELIX 296..305
FT /evidence="ECO:0007829|PDB:2JES"
FT STRAND 306..320
FT /evidence="ECO:0007829|PDB:2JES"
FT HELIX 326..343
FT /evidence="ECO:0007829|PDB:2JES"
FT TURN 355..358
FT /evidence="ECO:0007829|PDB:2JES"
FT HELIX 360..398
FT /evidence="ECO:0007829|PDB:2JES"
FT HELIX 406..409
FT /evidence="ECO:0007829|PDB:2JES"
FT STRAND 411..413
FT /evidence="ECO:0007829|PDB:2JES"
FT HELIX 422..435
FT /evidence="ECO:0007829|PDB:2JES"
FT HELIX 440..446
FT /evidence="ECO:0007829|PDB:2JES"
FT HELIX 453..464
FT /evidence="ECO:0007829|PDB:2JES"
SQ SEQUENCE 503 AA; 57333 MW; A06405F7D88E9D52 CRC64;
MADIYPLGKT HTEELNEIIV ESAKEIAEPD TTMIQKLIDE HNPEPLLKGV RYYMCENDIE
KKRRTYYDAA GQQLVDDTKT NNRTSHAWHK LFVDQKTQYL VGEPVTFTSD NKTLLEYVNE
LADDDFDDIL NETVKNMSNK GIEYWHPFVD EEGEFDYVIF PAEEMIVVYK DNTRRDILFA
LRYYSYKGIM GEETQKAELY TDTHVYYYEK IDGVYQMDYS YGENNPRPHM TKGGQAIGWG
RVPIIPFKNN EEMVSDLKFY KDLIDNYDSI TSSTMDSFSD FQQIVYVLKN YDGENPKEFT
ANLRYHSVIK VSGDGGVDTL RAEIPVDSAA KELERIQDEL YKSAQAVDNS PETIGGGATG
PALENLYALL DLKANMAERK IRAGLRLFFW FFAEYLRNTG KGDFNPDKEL TMTFTRTRIQ
NDSEIVQSLV QGVTGGIMSK ETAVARNPFV QDPEEELARI EEEMNQYAEM QGNLLDDEGG
DDDLEEDDPN AGAAESGGAG QVS
