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Baseplate wedge protein gp7 (Gene product 7) (gp7)

 BP07_BPT4               Reviewed;        1032 AA.
P19061;
01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
01-NOV-1990, sequence version 1.
22-NOV-2017, entry version 90.
RecName: Full=Baseplate wedge protein gp7 {ECO:0000255|HAMAP-Rule:MF_04103};
AltName: Full=Gene product 7;
Short=gp7;
Name=7;
Enterobacteria phage T4 (Bacteriophage T4).
Viruses; dsDNA viruses, no RNA stage; Caudovirales; Myoviridae;
Tevenvirinae; T4virus.
NCBI_TaxID=10665;
NCBI_TaxID=562; Escherichia coli.
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=D;
PubMed=2402473; DOI=10.1093/nar/18.17.5313;
Efimov V.P., Prilipov A.G., Mesyanzhinov V.V.;
"Nucleotide sequences of bacteriophage T4 genes 6, 7 and 8.";
Nucleic Acids Res. 18:5313-5313(1990).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12626685; DOI=10.1128/MMBR.67.1.86-156.2003;
Miller E.S., Kutter E., Mosig G., Arisaka F., Kunisawa T., Ruger W.;
"Bacteriophage T4 genome.";
Microbiol. Mol. Biol. Rev. 67:86-156(2003).
[3]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=2254933; DOI=10.1016/S0022-2836(05)80323-7;
Watts N.R., Hainfeld J., Coombs D.H.;
"Localization of the proteins gp7, gp8 and gp10 in the bacteriophage
T4 baseplate with colloidal gold: F(ab)2 and undecagold: Fab'
conjugates.";
J. Mol. Biol. 216:315-325(1990).
[4]
SUBCELLULAR LOCATION.
PubMed=2403438;
Watts N.R., Coombs D.H.;
"Structure of the bacteriophage T4 baseplate as determined by chemical
cross-linking.";
J. Virol. 64:143-154(1990).
[5]
REVIEW.
PubMed=14625682; DOI=10.1007/s00018-003-3072-1;
Leiman P.G., Kanamaru S., Mesyanzhinov V.V., Arisaka F.,
Rossmann M.G.;
"Structure and morphogenesis of bacteriophage T4.";
Cell. Mol. Life Sci. 60:2356-2370(2003).
[6]
REVIEW ON FUNCTION.
PubMed=21129200; DOI=10.1186/1743-422X-7-355;
Leiman P.G., Arisaka F., van Raaij M.J., Kostyuchenko V.A.,
Aksyuk A.A., Kanamaru S., Rossmann M.G.;
"Morphogenesis of the T4 tail and tail fibers.";
Virol. J. 7:355-355(2010).
[7]
SUBUNIT.
PubMed=19896486; DOI=10.1016/j.jmb.2009.10.071;
Yap M.L., Mio K., Leiman P.G., Kanamaru S., Arisaka F.;
"The baseplate wedges of bacteriophage T4 spontaneously assemble into
hubless baseplate-like structure in vitro.";
J. Mol. Biol. 395:349-360(2010).
[8]
STRUCTURE BY ELECTRON MICROSCOPY (17.0 ANGSTROMS) OF THE CONTRACTED
TAIL, AND SUBCELLULAR LOCATION.
PubMed=15315755; DOI=10.1016/j.cell.2004.07.022;
Leiman P.G., Chipman P.R., Kostyuchenko V.A., Mesyanzhinov V.V.,
Rossmann M.G.;
"Three-dimensional rearrangement of proteins in the tail of
bacteriophage T4 on infection of its host.";
Cell 118:419-429(2004).
[9]
STRUCTURE BY ELECTRON MICROSCOPY (4.11 ANGSTROMS), SUBUNIT,
SUBCELLULAR LOCATION, FUNCTION, INTERACTION WITH GP6, INTERACTION WITH
GP8, DISULFIDE BOND, AND INTERACTION WITH GP10.
PubMed=27193680; DOI=10.1038/nature17971;
Taylor N.M., Prokhorov N.S., Guerrero-Ferreira R.C., Shneider M.M.,
Browning C., Goldie K.N., Stahlberg H., Leiman P.G.;
"Structure of the T4 baseplate and its function in triggering sheath
contraction.";
Nature 533:346-352(2016).
-!- FUNCTION: Intermediate/inner baseplate protein (PubMed:27193680,
PubMed:15315755). The gp25-(gp6)2-gp7 module is involved in sheath
contraction (PubMed:27193680). Involved in the tail assembly
(PubMed:21129200). {ECO:0000269|PubMed:15315755,
ECO:0000269|PubMed:27193680, ECO:0000303|PubMed:21129200}.
-!- SUBUNIT: Heterotrimer with gp6; assembles as a (gp6)2-gp7
heterotrimeric molecule. The (gp6)2-gp7 heterotrimeric molecule
further interacts with gp25 and gp53. The gp25-(gp6)2-gp7 module
is involved in sheath contraction. Interacts with gp8. Binds to
gp10 homotrimer; disulfide-linked. Heteromultimer with gp10; a
gp10 molecule is disulfide-linked to gp7 and the other two
remaining gp10 molecules form a disulfide bond. Part of the
baseplate macromolecular complex which consists of gp5, gp5.4,
gp27 (central spike complex); gp6, gp25, gp53 (inner baseplate);
gp7, gp8 (intermediate baseplate); gp9, gp10, gp11, gp12
(peripheral); gp48 and gp54 (proximal region of the tail tube).
{ECO:0000255|HAMAP-Rule:MF_04103, ECO:0000269|PubMed:27193680}.
-!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04103,
ECO:0000269|PubMed:15315755, ECO:0000269|PubMed:2254933,
ECO:0000269|PubMed:2403438, ECO:0000269|PubMed:27193680}.
Note=Present in 6 copies in the baseplate.
{ECO:0000303|PubMed:21129200}.
-!- SIMILARITY: Belongs to the T4likevirus baseplate wedge protein gp7
family. {ECO:0000255|HAMAP-Rule:MF_04103}.
-----------------------------------------------------------------------
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EMBL; X15907; CAA34022.1; -; Genomic_DNA.
EMBL; AF158101; AAD42518.1; -; Genomic_DNA.
PIR; JQ0657; G7BPT4.
RefSeq; NP_049765.1; NC_000866.4.
PDB; 5HX2; EM; 3.80 A; A=1-1032.
PDB; 5IV5; EM; 4.11 A; BJ/C/EC/GF/Z/w=1-1032.
PDB; 5IV7; EM; 6.77 A; C/CA/EC/S/i/y=1-1032.
PDBsum; 5HX2; -.
PDBsum; 5IV5; -.
PDBsum; 5IV7; -.
SMR; P19061; -.
TCDB; 1.K.1.1.1; the gp27/5 t4-baseplate (t4-bp) family.
PRIDE; P19061; -.
GeneID; 1258549; -.
KEGG; vg:1258549; -.
OrthoDB; VOG09000012; -.
Proteomes; UP000009087; Genome.
GO; GO:0019012; C:virion; IDA:CACAO.
GO; GO:0098025; C:virus tail, baseplate; IDA:UniProtKB.
GO; GO:0098003; P:viral tail assembly; IEA:UniProtKB-KW.
CDD; cd00063; FN3; 1.
Gene3D; 2.130.10.10; -; 1.
Gene3D; 2.60.40.10; -; 1.
HAMAP; MF_04103; BP07_T4; 1.
InterPro; IPR003961; FN3_dom.
InterPro; IPR036116; FN3_sf.
InterPro; IPR034697; GP7_T4.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
SUPFAM; SSF49265; SSF49265; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Disulfide bond; Late protein;
Reference proteome; Viral baseplate protein;
Viral release from host cell; Viral tail assembly; Viral tail protein;
Virion.
CHAIN 1 1032 Baseplate wedge protein gp7.
/FTId=PRO_0000164997.
DISULFID 184 184 Interchain (with C-555 in GP10).
{ECO:0000269|PubMed:27193680}.
SEQUENCE 1032 AA; 119215 MW; 03B04E574620FA44 CRC64;
MTVKAPSVTS LRISKLSANQ VQVRWDDVGA NFYYFVEIAE TKTNSGENLP SNQYRWINLG
YTANNSFFFD DADPLTTYII RVATAAQDFE QSDWIYTEEF ETFATNAYTF QNMIEMQLAN
KFIQEKFTLN NSDYVNFNND TIMAALMNES FQFSPSYVDV SSISNFIIGE NEYHEIQGSI
QQVCKDINRV YLMESEGILY LFERYQPVVK VSNDKGQTWK AVKLFNDRVG YPLSKTVYYQ
SANTTYVLGY DKIFYGRKST DVRWSADDVR FSSQDITFAK LGDQLHLGFD VEIFATYATL
PANVYRIAEA ITCTDDYIYV VARDKVRYIK TSNALIDFDP LSPTYSERLF EPDTMTITGN
PKAVCYKMDS ICDKVFALII GEVETLNANP RTSKIIDSAD KGIYVLNHDE KTWKRVFGNT
EEERRRIQPG YANMSTDGKL VSLSSSNFKF LSDNVVNDPE TAAKYQLIGA VKYEFPREWL
ADKHYHMMAF IADETSDWET FTPQPMKYYA EPFFNWSKKS NTRCWINNSD RAVVVYADLK
YTKVIENIPE TSPDRLVHEY WDDGDCTIVM PNVKFTGFKK YASGMLFYKA SGEIISYYDF
NYRVRDTVEI IWKPTEVFLK AFLQNQEHET PWSPEEERGL ADPDLRPLIG TMMPDSYLLQ
DSNFEAFCEA YIQYLSDGYG TQYNNLRNLI RNQYPREEHA WEYLWSEIYK RNIYLNADKR
DAVARFFESR SYDFYSTKGI EASYKFLFKV LYNEEVEIEI ESGAGTEYDI IVQSDSLTED
LVGQTIYTAT GRCNVTYIER SYSNGKLQWT VTIHNLLGRL IAGQEVKAER LPSFEGEIIR
GVKGKDLLQN NIDYINRSRS YYVMKIKSNL PSSRWKSDVI RFVHPVGFGF IAITLLTMFI
NVGLTLKHTE TIINKYKNYK WDSGLPTEYA DRIAKLTPTG EIEHDSVTGE AIYEPGPMAG
VKYPLPDDYN AENNNSIFQG QLPSERRKLM SPLFDASGTT FAQFRDLVNK RLKDNIGNPR
DPENPTQVKI DE


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