PORTL_BPG20
ID PORTL_BPG20 Reviewed; 448 AA.
AC A0A1L4BKQ4;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 1.
DT 03-AUG-2022, entry version 23.
DE RecName: Full=Portal protein {ECO:0000303|PubMed:24192358};
DE AltName: Full=Gene product 81 {ECO:0000305};
DE Short=gp81 {ECO:0000305};
GN ORFNames=G20c_81 {ECO:0000312|EMBL:API81889.1};
OS Thermus phage G20c (Thermus thermophilus phage G20c).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Siphoviridae; Oshimavirus; unclassified Oshimavirus.
OX NCBI_TaxID=1406341;
OH NCBI_TaxID=274; Thermus thermophilus.
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=28100693; DOI=10.1093/nar/gkw1354;
RA Xu R.G., Jenkins H.T., Chechik M., Blagova E.V., Lopatina A., Klimuk E.,
RA Minakhin L., Severinov K., Greive S.J., Antson A.A.;
RT "Viral genome packaging terminase cleaves DNA using the canonical RuvC-like
RT two-metal catalysis mechanism.";
RL Nucleic Acids Res. 45:3580-3590(2017).
RN [2]
RP STRUCTURE BY ELECTRON MICROSCOPY (2.10 ANGSTROMS) OF 21-425, AND SUBUNIT.
RX PubMed=24192358; DOI=10.1107/s174430911302486x;
RA Williams L.S., Levdikov V.M., Minakhin L., Severinov K., Antson A.A.;
RT "12-Fold symmetry of the putative portal protein from the Thermus
RT thermophilus bacteriophage G20C determined by X-ray analysis.";
RL Acta Crystallogr. F 69:1239-1241(2013).
RN [3]
RP STRUCTURE BY ELECTRON MICROSCOPY (1.95 ANGSTROMS) OF 1-438, SUBUNIT,
RP INTERACTION WITH THE CAPSID PROTEIN, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=30737287; DOI=10.1073/pnas.1813204116;
RA Bayfield O.W., Klimuk E., Winkler D.C., Hesketh E.L., Chechik M., Cheng N.,
RA Dykeman E.C., Minakhin L., Ranson N.A., Severinov K., Steven A.C.,
RA Antson A.A.;
RT "Cryo-EM structure and in vitro DNA packaging of a thermophilic virus with
RT supersized T=7 capsids.";
RL Proc. Natl. Acad. Sci. U.S.A. 116:3556-3561(2019).
CC -!- FUNCTION: Forms the portal vertex of the capsid (PubMed:30737287). This
CC portal plays critical roles in head assembly, genome packaging,
CC neck/tail attachment, and genome ejection (PubMed:30737287). The portal
CC protein multimerizes as a single ring-shaped homododecamer arranged
CC around a central channel (PubMed:30737287). Forms the portal vertex of
CC the capsid. This portal plays critical roles in head assembly, genome
CC packaging, neck/tail attachment, and genome ejection (PubMed:30737287).
CC {ECO:0000269|PubMed:30737287}.
CC -!- SUBUNIT: Homododecamer (PubMed:30737287, PubMed:24192358). Interacts
CC with the capsid protein (Probable). Interacts with the terminase large
CC subunit; this interaction allows the packaging of viral DNA (By
CC similarity). {ECO:0000250|UniProtKB:P26744,
CC ECO:0000269|PubMed:24192358, ECO:0000269|PubMed:30737287,
CC ECO:0000305|PubMed:30737287}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:30737287}.
CC Note=Located at a unique vertex of the capsid.
CC {ECO:0000269|PubMed:30737287}.
CC -!- SIMILARITY: Belongs to the P23virus portal protein family.
CC {ECO:0000305}.
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DR EMBL; KX987127; API81889.1; -; Genomic_DNA.
DR PDB; 6IBG; X-ray; 1.95 A; A/B/C=1-438.
DR PDBsum; 6IBG; -.
DR SMR; A0A1L4BKQ4; -.
DR Proteomes; UP000223104; Genome.
DR GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW 3D-structure; Capsid protein; Reference proteome; Viral capsid assembly;
KW Viral genome packaging; Viral release from host cell; Virion.
FT CHAIN 1..448
FT /note="Portal protein"
FT /id="PRO_0000447193"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:6IBG"
FT HELIX 52..62
FT /evidence="ECO:0007829|PDB:6IBG"
FT HELIX 66..80
FT /evidence="ECO:0007829|PDB:6IBG"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:6IBG"
FT STRAND 89..92
FT /evidence="ECO:0007829|PDB:6IBG"
FT HELIX 93..106
FT /evidence="ECO:0007829|PDB:6IBG"
FT HELIX 116..131
FT /evidence="ECO:0007829|PDB:6IBG"
FT STRAND 132..142
FT /evidence="ECO:0007829|PDB:6IBG"
FT STRAND 148..156
FT /evidence="ECO:0007829|PDB:6IBG"
FT HELIX 158..160
FT /evidence="ECO:0007829|PDB:6IBG"
FT STRAND 161..166
FT /evidence="ECO:0007829|PDB:6IBG"
FT STRAND 172..180
FT /evidence="ECO:0007829|PDB:6IBG"
FT STRAND 187..194
FT /evidence="ECO:0007829|PDB:6IBG"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:6IBG"
FT STRAND 198..204
FT /evidence="ECO:0007829|PDB:6IBG"
FT STRAND 207..209
FT /evidence="ECO:0007829|PDB:6IBG"
FT HELIX 216..218
FT /evidence="ECO:0007829|PDB:6IBG"
FT HELIX 219..241
FT /evidence="ECO:0007829|PDB:6IBG"
FT STRAND 244..248
FT /evidence="ECO:0007829|PDB:6IBG"
FT HELIX 257..271
FT /evidence="ECO:0007829|PDB:6IBG"
FT HELIX 273..275
FT /evidence="ECO:0007829|PDB:6IBG"
FT STRAND 284..287
FT /evidence="ECO:0007829|PDB:6IBG"
FT HELIX 298..310
FT /evidence="ECO:0007829|PDB:6IBG"
FT TURN 311..313
FT /evidence="ECO:0007829|PDB:6IBG"
FT TURN 318..322
FT /evidence="ECO:0007829|PDB:6IBG"
FT STRAND 324..326
FT /evidence="ECO:0007829|PDB:6IBG"
FT HELIX 330..355
FT /evidence="ECO:0007829|PDB:6IBG"
FT HELIX 357..361
FT /evidence="ECO:0007829|PDB:6IBG"
FT TURN 362..364
FT /evidence="ECO:0007829|PDB:6IBG"
FT STRAND 373..375
FT /evidence="ECO:0007829|PDB:6IBG"
FT HELIX 384..397
FT /evidence="ECO:0007829|PDB:6IBG"
FT TURN 398..400
FT /evidence="ECO:0007829|PDB:6IBG"
FT HELIX 404..413
FT /evidence="ECO:0007829|PDB:6IBG"
FT HELIX 417..423
FT /evidence="ECO:0007829|PDB:6IBG"
FT HELIX 428..433
FT /evidence="ECO:0007829|PDB:6IBG"
SQ SEQUENCE 448 AA; 49671 MW; 2567B6B25613D214 CRC64;
MAKRGRKPKE LVPGPGSIDP SDVPKLEGAS VPVMSTSYDV VVDREFDELL QGKDGLLVYH
KMLSDGTVKN ALNYIFGRIR SAKWYVEPAS TDPEDIAIAA FIHAQLGIDD ASVGKYPFGR
LFAIYENAYI YGMAAGEIVL TLGADGKLIL DKIVPIHPFN IDEVLYDEEG GPKALKLSGE
VKGGSQFVSG LEIPIWKTVV FLHNDDGSFT GQSALRAAVP HWLAKRALIL LINHGLERFM
IGVPTLTIPK SVRQGTKQWE AAKEIVKNFV QKPRHGIILP DDWKFDTVDL KSAMPDAIPY
LTYHDAGIAR ALGIDFNTVQ LNMGVQAINI GEFVSLTQQT IISLQREFAS AVNLYLIPKL
VLPNWPSATR FPRLTFEMEE RNDFSAAANL MGMLINAVKD SEDIPTELKA LIDALPSKMR
RALGVVDEVR EAVRQPADSR YLYTRRRR
