PORTL_BPT7
ID PORTL_BPT7 Reviewed; 536 AA.
AC P03728;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 25-MAY-2022, entry version 82.
DE RecName: Full=Portal protein {ECO:0000255|HAMAP-Rule:MF_04120, ECO:0000305};
DE AltName: Full=Gene product 8 {ECO:0000305};
DE Short=Gp8;
DE AltName: Full=Head-to-tail connector {ECO:0000255|HAMAP-Rule:MF_04120, ECO:0000305};
GN OrderedLocusNames=8;
OS Escherichia phage T7 (Bacteriophage T7).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Autographiviridae; Studiervirinae; Teseptimavirus.
OX NCBI_TaxID=10760;
OH NCBI_TaxID=562; Escherichia coli.
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=6864790; DOI=10.1016/s0022-2836(83)80282-4;
RA Dunn J.J., Studier F.W.;
RT "Complete nucleotide sequence of bacteriophage T7 DNA and the locations of
RT T7 genetic elements.";
RL J. Mol. Biol. 166:477-535(1983).
RN [2]
RP FUNCTION, INTERACTION WITH THE TAIL TUBE PROTEIN GP11, AND SUBUNIT.
RX PubMed=15784250; DOI=10.1016/j.jmb.2005.02.005;
RA Agirrezabala X., Martin-Benito J., Valle M., Gonzalez J.M., Valencia A.,
RA Valpuesta J.M., Carrascosa J.L.;
RT "Structure of the connector of bacteriophage T7 at 8A resolution:
RT structural homologies of a basic component of a DNA translocating
RT machinery.";
RL J. Mol. Biol. 347:895-902(2005).
RN [3]
RP INTERACTION WITH THE TERMINASE LARGE SUBUNIT.
RX PubMed=23632014; DOI=10.1074/jbc.m112.448951;
RA Dauden M.I., Martin-Benito J., Sanchez-Ferrero J.C., Pulido-Cid M.,
RA Valpuesta J.M., Carrascosa J.L.;
RT "Large terminase conformational change induced by connector binding in
RT bacteriophage T7.";
RL J. Biol. Chem. 288:16998-17007(2013).
RN [4]
RP INTERACTION WITH THE MAJOR CAPSID PROTEIN, AND INTERACTION WITH INTERNAL
RP VIRION PROTEIN GP14.
RX PubMed=23580619; DOI=10.1073/pnas.1215563110;
RA Guo F., Liu Z., Vago F., Ren Y., Wu W., Wright E.T., Serwer P., Jiang W.;
RT "Visualization of uncorrelated, tandem symmetry mismatches in the internal
RT genome packaging apparatus of bacteriophage T7.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6811-6816(2013).
RN [5]
RP STRUCTURE BY ELECTRON MICROSCOPY (12.0 ANGSTROMS) OF 1-497, FUNCTION,
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=23884409; DOI=10.1074/jbc.m113.491209;
RA Cuervo A., Pulido-Cid M., Chagoyen M., Arranz R., Gonzalez-Garcia V.A.,
RA Garcia-Doval C., Caston J.R., Valpuesta J.M., van Raaij M.J.,
RA Martin-Benito J., Carrascosa J.L.;
RT "Structural characterization of the bacteriophage T7 tail machinery.";
RL J. Biol. Chem. 288:26290-26299(2013).
CC -!- FUNCTION: Forms the portal vertex of the capsid. This portal plays
CC critical roles in head assembly, genome packaging, neck/tail
CC attachment, and genome ejection. The portal protein multimerizes as a
CC single ring-shaped homododecamer arranged around a central channel.
CC {ECO:0000255|HAMAP-Rule:MF_04120, ECO:0000305|PubMed:15784250,
CC ECO:0000305|PubMed:23884409}.
CC -!- SUBUNIT: Homododecamer. Interacts with major capsid protein. Interacts
CC with the tail tube protein gp11. Interacts with the terminase large
CC subunit. Interacts with the internal virion protein gp14.
CC {ECO:0000255|HAMAP-Rule:MF_04120, ECO:0000269|PubMed:15784250,
CC ECO:0000269|PubMed:23580619, ECO:0000269|PubMed:23632014,
CC ECO:0000269|PubMed:23884409}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04120,
CC ECO:0000269|PubMed:23884409}.
CC -!- SIMILARITY: Belongs to the podoviridae portal protein family.
CC {ECO:0000255|HAMAP-Rule:MF_04120}.
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DR EMBL; V01146; CAA24425.1; -; Genomic_DNA.
DR PIR; A04354; JQBPT7.
DR RefSeq; NP_041995.1; NC_001604.1.
DR PDB; 3J4A; EM; 12.00 A; A/B/C/D/E/F/G/H/I/J/K/L=1-497.
DR PDB; 6QWP; X-ray; 3.40 A; A/B/C/D/E/F/G/H/I/J/K/L/M=1-536.
DR PDB; 6QX5; X-ray; 3.60 A; A/B/C/D/E/F/G/H/I/J/K/L=5-494.
DR PDB; 6QXM; EM; 4.10 A; A/B/C/D/E/F/G/H/I/J/K/L=1-536.
DR PDB; 6R21; EM; 3.33 A; A/B/C/D/E/F/G/H/I/J/K/L=1-536.
DR PDB; 6TJP; X-ray; 3.74 A; A/B/C/D/E/F/G/H/I/J/K/L/M=1-536.
DR PDB; 7BOU; EM; 3.60 A; A/B/C/D/E/F/G/H/I/J/K/L=1-536.
DR PDB; 7BP0; EM; 4.60 A; a/b/c/d/e/f/g/h/i/j/k/l=1-536.
DR PDB; 7EY6; EM; 4.30 A; A/B/C/D/E/F/G/H/I/J/K/L=1-536.
DR PDB; 7EY8; EM; 3.40 A; A/B/C/D/E/F/G/H/I/J/K/L=1-536.
DR PDBsum; 3J4A; -.
DR PDBsum; 6QWP; -.
DR PDBsum; 6QX5; -.
DR PDBsum; 6QXM; -.
DR PDBsum; 6R21; -.
DR PDBsum; 6TJP; -.
DR PDBsum; 7BOU; -.
DR PDBsum; 7BP0; -.
DR PDBsum; 7EY6; -.
DR PDBsum; 7EY8; -.
DR SMR; P03728; -.
DR MINT; P03728; -.
DR TCDB; 1.W.10.1.1; the (enterobacterial phage t7) portal protein 10 (ppp10) family.
DR GeneID; 1261033; -.
DR KEGG; vg:1261033; -.
DR Proteomes; UP000000840; Genome.
DR GO; GO:0046798; C:viral portal complex; IDA:UniProtKB.
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-UniRule.
DR HAMAP; MF_04120; PORTAL_PROTEIN_T7; 1.
DR InterPro; IPR020991; Connector_podovirus.
DR InterPro; IPR038995; Portal_prot_Caudovirale.
DR Pfam; PF12236; Head-tail_con; 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 penetration into host cytoplasm; Viral release from host cell;
KW Viral short tail ejection system; Virion; Virus entry into host cell.
FT CHAIN 1..536
FT /note="Portal protein"
FT /id="PRO_0000106517"
FT HELIX 7..9
FT /evidence="ECO:0007829|PDB:6QWP"
FT HELIX 13..36
FT /evidence="ECO:0007829|PDB:6QWP"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:6QWP"
FT HELIX 61..77
FT /evidence="ECO:0007829|PDB:6QWP"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:6QWP"
FT HELIX 90..95
FT /evidence="ECO:0007829|PDB:6QWP"
FT TURN 96..98
FT /evidence="ECO:0007829|PDB:6QWP"
FT HELIX 100..103
FT /evidence="ECO:0007829|PDB:6QWP"
FT HELIX 106..123
FT /evidence="ECO:0007829|PDB:6QWP"
FT HELIX 126..139
FT /evidence="ECO:0007829|PDB:6QWP"
FT STRAND 140..146
FT /evidence="ECO:0007829|PDB:6QWP"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:6QWP"
FT STRAND 159..162
FT /evidence="ECO:0007829|PDB:6QWP"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:6QWP"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:6QWP"
FT STRAND 176..186
FT /evidence="ECO:0007829|PDB:6QWP"
FT HELIX 187..189
FT /evidence="ECO:0007829|PDB:6QWP"
FT HELIX 192..200
FT /evidence="ECO:0007829|PDB:6QWP"
FT STRAND 210..219
FT /evidence="ECO:0007829|PDB:6QWP"
FT STRAND 221..232
FT /evidence="ECO:0007829|PDB:6QWP"
FT STRAND 242..245
FT /evidence="ECO:0007829|PDB:6QWP"
FT HELIX 246..248
FT /evidence="ECO:0007829|PDB:6QWP"
FT STRAND 250..257
FT /evidence="ECO:0007829|PDB:6QWP"
FT HELIX 269..272
FT /evidence="ECO:0007829|PDB:6QWP"
FT HELIX 273..293
FT /evidence="ECO:0007829|PDB:6QWP"
FT STRAND 297..300
FT /evidence="ECO:0007829|PDB:6QWP"
FT HELIX 308..312
FT /evidence="ECO:0007829|PDB:6QWP"
FT STRAND 319..321
FT /evidence="ECO:0007829|PDB:6QWP"
FT TURN 324..326
FT /evidence="ECO:0007829|PDB:6QWP"
FT STRAND 327..329
FT /evidence="ECO:0007829|PDB:6QWP"
FT HELIX 335..355
FT /evidence="ECO:0007829|PDB:6QWP"
FT STRAND 356..358
FT /evidence="ECO:0007829|PDB:7EY8"
FT HELIX 359..361
FT /evidence="ECO:0007829|PDB:6QWP"
FT STRAND 365..367
FT /evidence="ECO:0007829|PDB:6QWP"
FT HELIX 371..395
FT /evidence="ECO:0007829|PDB:6QWP"
FT HELIX 397..410
FT /evidence="ECO:0007829|PDB:6QWP"
FT HELIX 419..421
FT /evidence="ECO:0007829|PDB:6QWP"
FT STRAND 425..427
FT /evidence="ECO:0007829|PDB:6QWP"
FT HELIX 430..433
FT /evidence="ECO:0007829|PDB:6QWP"
FT HELIX 437..449
FT /evidence="ECO:0007829|PDB:6QWP"
FT HELIX 450..452
FT /evidence="ECO:0007829|PDB:6QWP"
FT HELIX 454..457
FT /evidence="ECO:0007829|PDB:7EY8"
FT STRAND 459..461
FT /evidence="ECO:0007829|PDB:7EY8"
FT HELIX 463..474
FT /evidence="ECO:0007829|PDB:6QWP"
FT HELIX 485..493
FT /evidence="ECO:0007829|PDB:6QWP"
FT STRAND 517..519
FT /evidence="ECO:0007829|PDB:7EY8"
FT HELIX 520..530
FT /evidence="ECO:0007829|PDB:7EY8"
SQ SEQUENCE 536 AA; 59120 MW; CDE87B92DC4A6C65 CRC64;
MAEKRTGLAE DGAKSVYERL KNDRAPYETR AQNCAQYTIP SLFPKDSDNA STDYQTPWQA
VGARGLNNLA SKLMLALFPM QTWMRLTISE YEAKQLLSDP DGLAKVDEGL SMVERIIMNY
IESNSYRVTL FEALKQLVVA GNVLLYLPEP EGSNYNPMKL YRLSSYVVQR DAFGNVLQMV
TRDQIAFGAL PEDIRKAVEG QGGEKKADET IDVYTHIYLD EDSGEYLRYE EVEGMEVQGS
DGTYPKEACP YIPIRMVRLD GESYGRSYIE EYLGDLRSLE NLQEAIVKMS MISSKVIGLV
NPAGITQPRR LTKAQTGDFV TGRPEDISFL QLEKQADFTV AKAVSDAIEA RLSFAFMLNS
AVQRTGERVT AEEIRYVASE LEDTLGGVYS ILSQELQLPL VRVLLKQLQA TQQIPELPKE
AVEPTISTGL EAIGRGQDLD KLERCVTAWA ALAPMRDDPD INLAMIKLRI ANAIGIDTSG
ILLTEEQKQQ KMAQQSMQMG MDNGAAALAQ GMAAQATASP EAMAAAADSV GLQPGI
