GP15_BPT7
ID GP15_BPT7 Reviewed; 747 AA.
AC P03725;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 25-MAY-2022, entry version 71.
DE RecName: Full=Internal virion protein gp15 {ECO:0000255|HAMAP-Rule:MF_04122};
DE AltName: Full=Gene product 15;
DE Short=Gp15;
GN OrderedLocusNames=15;
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 VIRION, AND SUBUNIT.
RX PubMed=12614603; DOI=10.1016/s0022-2836(03)00117-7;
RA Cerritelli M.E., Trus B.L., Smith C.S., Cheng N., Conway J.F., Steven A.C.;
RT "A second symmetry mismatch at the portal vertex of bacteriophage T7: 8-
RT fold symmetry in the procapsid core.";
RL J. Mol. Biol. 327:1-6(2003).
RN [3]
RP FUNCTION.
RX PubMed=20036409; DOI=10.1016/j.virol.2009.12.002;
RA Chang C.Y., Kemp P., Molineux I.J.;
RT "Gp15 and gp16 cooperate in translocating bacteriophage T7 DNA into the
RT infected cell.";
RL Virology 398:176-186(2010).
RN [4]
RP INTERACTION WITH GP14 AND GP16.
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 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).
RN [6]
RP INTERACTION WITH GP16, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=26476287; DOI=10.1016/j.virol.2015.09.022;
RA Lupo D., Leptihn S., Nagler G., Haase M., Molineux I.J., Kuhn A.;
RT "The T7 ejection nanomachine components gp15-gp16 form a spiral ring
RT complex that binds DNA and a lipid membrane.";
RL Virology 486:263-271(2015).
CC -!- FUNCTION: Component of the cylindrical core that assembles on the inner
CC surface of the capsid during capsid formation and plays a role in viral
CC DNA ejection into the host cell. The inner core is composed of stacked
CC rings of gp14, gp15 and gp16 proteins. Following binding to the host
CC cell surface, the internal core is disassembled and gp15 is ejected
CC along with gp14 and gp16 into the infected cell. Gp15 probably remains
CC associated with gp16. The gp15-gp16 complex binds to both the viral DNA
CC and the host inner membrane, probably escorting the leading end of the
CC genome through the periplasm and controlling the extend of DNA
CC translocated into the host cell. {ECO:0000255|HAMAP-Rule:MF_04122,
CC ECO:0000269|PubMed:20036409, ECO:0000269|PubMed:26476287}.
CC -!- SUBUNIT: Homooctamer (PubMed:12614603). Interacts with gp16; after
CC ejection the gp15-gp16 complex composed of a gp15 octamer and a gp16
CC tetramer probably binds both the viral DNA and the host inner membrane
CC (PubMed:26476287). Interacts with gp14. {ECO:0000255|HAMAP-
CC Rule:MF_04122, ECO:0000269|PubMed:12614603,
CC ECO:0000269|PubMed:23580619, ECO:0000269|PubMed:26476287}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04122,
CC ECO:0000269|PubMed:23884409}. Host periplasm {ECO:0000255|HAMAP-
CC Rule:MF_04122, ECO:0000305|PubMed:26476287}. Note=The gp15-gp16 complex
CC spans the periplasm and the cytoplasmic membrane. {ECO:0000255|HAMAP-
CC Rule:MF_04122}.
CC -!- SIMILARITY: Belongs to the T7virus internal virion protein gp15 family.
CC {ECO:0000255|HAMAP-Rule:MF_04122}.
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DR EMBL; V01146; CAA24433.1; -; Genomic_DNA.
DR PIR; A04351; HIBPC7.
DR RefSeq; NP_042003.1; NC_001604.1.
DR PDB; 6YSZ; EM; 3.60 A; A/B/C/D/E/F=1-747.
DR PDB; 6YT5; EM; 3.00 A; A/B/C/D/E/F=1-747.
DR PDB; 7EYB; EM; 3.70 A; A/B/C/D/E/F/G/H=1-747.
DR PDB; 7K5C; EM; 2.70 A; A/C/E/H/I/K=1-747.
DR PDBsum; 6YSZ; -.
DR PDBsum; 6YT5; -.
DR PDBsum; 7EYB; -.
DR PDBsum; 7K5C; -.
DR SMR; P03725; -.
DR IntAct; P03725; 1.
DR MINT; P03725; -.
DR TCDB; 3.A.17.1.1; the phage t7 injectisome (t7 injectisome) family.
DR PRIDE; P03725; -.
DR GeneID; 1261034; -.
DR KEGG; vg:1261034; -.
DR Proteomes; UP000000840; Genome.
DR GO; GO:0044229; C:host cell periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0099002; P:viral genome ejection through host cell envelope, short tail mechanism; IEA:UniProtKB-UniRule.
DR HAMAP; MF_04122; GP15_T7; 1.
DR InterPro; IPR038993; Gp15.
PE 1: Evidence at protein level;
KW 3D-structure; Host periplasm; Reference proteome;
KW Viral genome ejection through host cell envelope;
KW Viral penetration into host cytoplasm; Viral short tail ejection system;
KW Virion; Virus entry into host cell.
FT CHAIN 1..747
FT /note="Internal virion protein gp15"
FT /id="PRO_0000106529"
FT HELIX 58..76
FT /evidence="ECO:0007829|PDB:7K5C"
FT HELIX 80..89
FT /evidence="ECO:0007829|PDB:7K5C"
FT TURN 93..96
FT /evidence="ECO:0007829|PDB:7K5C"
FT HELIX 98..126
FT /evidence="ECO:0007829|PDB:7K5C"
FT HELIX 132..151
FT /evidence="ECO:0007829|PDB:7K5C"
FT TURN 152..155
FT /evidence="ECO:0007829|PDB:7K5C"
FT HELIX 161..168
FT /evidence="ECO:0007829|PDB:7K5C"
FT HELIX 171..202
FT /evidence="ECO:0007829|PDB:7K5C"
FT TURN 203..205
FT /evidence="ECO:0007829|PDB:7K5C"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:7K5C"
FT HELIX 209..212
FT /evidence="ECO:0007829|PDB:7K5C"
FT HELIX 215..231
FT /evidence="ECO:0007829|PDB:7K5C"
FT STRAND 232..234
FT /evidence="ECO:0007829|PDB:7K5C"
FT HELIX 237..251
FT /evidence="ECO:0007829|PDB:7K5C"
FT HELIX 257..264
FT /evidence="ECO:0007829|PDB:7K5C"
FT STRAND 267..271
FT /evidence="ECO:0007829|PDB:7K5C"
FT STRAND 274..277
FT /evidence="ECO:0007829|PDB:7K5C"
FT HELIX 278..281
FT /evidence="ECO:0007829|PDB:7K5C"
FT HELIX 284..296
FT /evidence="ECO:0007829|PDB:7K5C"
FT HELIX 297..299
FT /evidence="ECO:0007829|PDB:7K5C"
FT HELIX 303..316
FT /evidence="ECO:0007829|PDB:7K5C"
FT HELIX 322..336
FT /evidence="ECO:0007829|PDB:7K5C"
FT TURN 337..339
FT /evidence="ECO:0007829|PDB:7K5C"
FT STRAND 342..344
FT /evidence="ECO:0007829|PDB:7K5C"
FT HELIX 347..395
FT /evidence="ECO:0007829|PDB:7K5C"
FT HELIX 404..406
FT /evidence="ECO:0007829|PDB:7K5C"
FT TURN 411..413
FT /evidence="ECO:0007829|PDB:7K5C"
FT HELIX 418..433
FT /evidence="ECO:0007829|PDB:7K5C"
FT STRAND 435..437
FT /evidence="ECO:0007829|PDB:7K5C"
FT HELIX 439..452
FT /evidence="ECO:0007829|PDB:7K5C"
FT HELIX 458..480
FT /evidence="ECO:0007829|PDB:7K5C"
FT HELIX 488..499
FT /evidence="ECO:0007829|PDB:7K5C"
FT HELIX 501..507
FT /evidence="ECO:0007829|PDB:7K5C"
FT HELIX 509..524
FT /evidence="ECO:0007829|PDB:7K5C"
FT HELIX 528..539
FT /evidence="ECO:0007829|PDB:7K5C"
FT HELIX 543..558
FT /evidence="ECO:0007829|PDB:7K5C"
FT HELIX 563..566
FT /evidence="ECO:0007829|PDB:7K5C"
FT HELIX 570..586
FT /evidence="ECO:0007829|PDB:7K5C"
FT HELIX 590..602
FT /evidence="ECO:0007829|PDB:7K5C"
FT STRAND 605..609
FT /evidence="ECO:0007829|PDB:7K5C"
FT STRAND 616..622
FT /evidence="ECO:0007829|PDB:7K5C"
FT HELIX 623..625
FT /evidence="ECO:0007829|PDB:7K5C"
FT STRAND 628..631
FT /evidence="ECO:0007829|PDB:7K5C"
FT HELIX 632..634
FT /evidence="ECO:0007829|PDB:7K5C"
FT HELIX 635..652
FT /evidence="ECO:0007829|PDB:7K5C"
FT STRAND 656..659
FT /evidence="ECO:0007829|PDB:7K5C"
FT STRAND 662..666
FT /evidence="ECO:0007829|PDB:7K5C"
FT STRAND 669..673
FT /evidence="ECO:0007829|PDB:7K5C"
FT STRAND 675..684
FT /evidence="ECO:0007829|PDB:7K5C"
FT HELIX 685..704
FT /evidence="ECO:0007829|PDB:7K5C"
SQ SEQUENCE 747 AA; 84341 MW; 959C572B7B42C2B8 CRC64;
MSKIESALQA AQPGLSRLRG GAGGMGYRAA TTQAEQPRSS LLDTIGRFAK AGADMYTAKE
QRARDLADER SNEIIRKLTP EQRREALNNG TLLYQDDPYA MEALRVKTGR NAAYLVDDDV
MQKIKEGVFR TREEMEEYRH SRLQEGAKVY AEQFGIDPED VDYQRGFNGD ITERNISLYG
AHDNFLSQQA QKGAIMNSRV ELNGVLQDPD MLRRPDSADF FEKYIDNGLV TGAIPSDAQA
TQLISQAFSD ASSRAGGADF LMRVGDKKVT LNGATTTYRE LIGEEQWNAL MVTAQRSQFE
TDAKLNEQYR LKINSALNQE DPRTAWEMLQ GIKAELDKVQ PDEQMTPQRE WLISAQEQVQ
NQMNAWTKAQ AKALDDSMKS MNKLDVIDKQ FQKRINGEWV STDFKDMPVN ENTGEFKHSD
MVNYANKKLA EIDSMDIPDG AKDAMKLKYL QADSKDGAFR TAIGTMVTDA GQEWSAAVIN
GKLPERTPAM DALRRIRNAD PQLIAALYPD QAELFLTMDM MDKQGIDPQV ILDADRLTVK
RSKEQRFEDD KAFESALNAS KAPEIARMPA SLRESARKIY DSVKYRSGNE SMAMEQMTKF
LKESTYTFTG DDVDGDTVGV IPKNMMQVNS DPKSWEQGRD ILEEARKGII ASNPWITNKQ
LTMYSQGDSI YLMDTTGQVR VRYDKELLSK VWSENQKKLE EKAREKALAD VNKRAPIVAA
TKAREAAAKR VREKRKQTPK FIYGRKE
