Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Baseplate central spike complex protein gp27 (Gene product 27) (gp27) (Hub protein 27)

 BP27_BPT4               Reviewed;         391 AA.
P17172; Q9T0T8;
01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
19-DEC-2001, sequence version 4.
28-FEB-2018, entry version 101.
RecName: Full=Baseplate central spike complex protein gp27 {ECO:0000303|PubMed:27193680};
AltName: Full=Gene product 27;
Short=gp27;
AltName: Full=Hub protein 27;
Name=27;
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=2349100; DOI=10.1093/nar/18.10.3046;
Bova R., Cascino A., Cipollaro M., Grau O., Micheli M.R., Santoro M.,
Storlazzi A., Scarlato V., Gargano S.;
"Bacteriophage T4 gene 27.";
Nucleic Acids Res. 18:3046-3046(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]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-53.
STRAIN=D;
PubMed=2763463; DOI=10.1016/0042-6822(89)90617-X;
Scarlato V., Storlazzi A., Gargano S., Cascino A.;
"Bacteriophage T4 late gene expression: overlapping promoters direct
divergent transcription of the base plate gene cluster.";
Virology 171:475-483(1989).
[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]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH GP5, AND SUBUNIT.
PubMed=12837775; DOI=10.1128/JB.185.14.4022-4030.2003;
Weigele P.R., Scanlon E., King J.;
"Homotrimeric, beta-stranded viral adhesins and tail proteins.";
J. Bacteriol. 185:4022-4030(2003).
[6]
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).
[7]
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).
[8]
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).
[9]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS), AND SUBUNIT.
PubMed=11823865; DOI=10.1038/415553a;
Kanamaru S., Leiman P.G., Kostyuchenko V.A., Chipman P.R.,
Mesyanzhinov V.V., Arisaka F., Rossmann M.G.;
"Structure of the cell-puncturing device of bacteriophage T4.";
Nature 415:553-557(2002).
[10]
STRUCTURE BY ELECTRON MICROSCOPY (12.0 ANGSTROMS).
PubMed=12923574; DOI=10.1038/nsb970;
Kostyuchenko V.A., Leiman P.G., Chipman P.R., Kanamaru S.,
van Raaij M.J., Arisaka F., Mesyanzhinov V.V., Rossmann M.G.;
"Three-dimensional structure of bacteriophage T4 baseplate.";
Nat. Struct. Biol. 10:688-693(2003).
[11]
STRUCTURE BY ELECTRON MICROSCOPY (17.0 ANGSTROMS) OF THE CONTRACTED
TAIL, SUBCELLULAR LOCATION, AND FUNCTION.
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).
[12]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
PubMed=15701513; DOI=10.1016/j.jmb.2004.12.042;
Kanamaru S., Ishiwata Y., Suzuki T., Rossmann M.G., Arisaka F.;
"Control of bacteriophage T4 tail lysozyme activity during the
infection process.";
J. Mol. Biol. 346:1013-1020(2005).
[13]
STRUCTURE BY ELECTRON MICROSCOPY (4.11 ANGSTROMS), SUBUNIT,
SUBCELLULAR LOCATION, FUNCTION, INTERACTION WITH GP5, AND INTERACTION
WITH GP5.4.
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: Baseplate central spike complex-associated protein
involved in the tail assembly. {ECO:0000269|PubMed:12837775,
ECO:0000269|PubMed:27193680, ECO:0000303|PubMed:21129200}.
-!- SUBUNIT: Homotrimer (PubMed:12837775, PubMed:19896486,
PubMed:11823865). Heteromultimer with gp5 trimer and gp5.4
monomer; this interaction forms the tail lysozyme complex that
creates an extension of the tail tube (PubMed:12837775,
PubMed:27193680). The T4 tail lysozyme complex is made up of three
copies of the proteolytically processed gp5 and three copies of
gp27.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) (PubMed:27193680). {ECO:0000269|PubMed:11823865,
ECO:0000269|PubMed:12837775, ECO:0000269|PubMed:19896486,
ECO:0000269|PubMed:27193680, ECO:0000303|PubMed:21129200}.
-!- INTERACTION:
P16009:5; NbExp=2; IntAct=EBI-1032762, EBI-1032754;
-!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:12837775,
ECO:0000269|PubMed:2403438, ECO:0000269|PubMed:27193680}.
Note=Present in 3 copies in the baseplate.
{ECO:0000303|PubMed:21129200}.
-!- INDUCTION: Expressed in the late phase of the viral replicative
cycle. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; X52236; CAA36481.1; -; Genomic_DNA.
EMBL; AF158101; AAD42435.2; -; Genomic_DNA.
EMBL; J04354; AAA88466.1; -; Genomic_DNA.
PIR; JU0285; GZBPT4.
RefSeq; NP_049803.1; NC_000866.4.
PDB; 1K28; X-ray; 2.90 A; D=1-391.
PDB; 1PDJ; EM; 12.00 A; D/E/F=1-391.
PDB; 1WTH; X-ray; 2.80 A; D=1-391.
PDB; 2Z6B; X-ray; 3.11 A; D=1-391.
PDB; 5IV5; EM; 4.11 A; YD/YE/YF=1-391.
PDBsum; 1K28; -.
PDBsum; 1PDJ; -.
PDBsum; 1WTH; -.
PDBsum; 2Z6B; -.
PDBsum; 5IV5; -.
ProteinModelPortal; P17172; -.
SMR; P17172; -.
IntAct; P17172; 1.
MINT; P17172; -.
TCDB; 1.K.1.1.1; the gp27/5 t4-baseplate (t4-bp) family.
GeneID; 1258643; -.
KEGG; vg:1258643; -.
OrthoDB; VOG090000AR; -.
EvolutionaryTrace; P17172; -.
Proteomes; UP000009087; Genome.
GO; GO:0019012; C:virion; IDA:CACAO.
GO; GO:0098015; C:virus tail; IDA:CAFA.
GO; GO:0098025; C:virus tail, baseplate; IDA:UniProtKB.
GO; GO:0098003; P:viral tail assembly; IEA:UniProtKB-KW.
InterPro; IPR015180; Phage_T4_Gp27_C.
InterPro; IPR015181; Phage_T4_Gp27_N.
Pfam; PF09097; Phage-tail_1; 1.
Pfam; PF09096; Phage-tail_2; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Late protein; Reference proteome;
Viral baseplate protein; Viral release from host cell;
Viral tail assembly; Viral tail protein; Virion.
CHAIN 1 391 Baseplate central spike complex protein
gp27.
/FTId=PRO_0000165015.
CONFLICT 168 168 N -> T (in Ref. 1; CAA36481).
{ECO:0000305}.
CONFLICT 262 262 S -> E (in Ref. 1). {ECO:0000305}.
CONFLICT 308 308 A -> L (in Ref. 1; CAA36481).
{ECO:0000305}.
STRAND 13 20 {ECO:0000244|PDB:1WTH}.
HELIX 21 24 {ECO:0000244|PDB:1WTH}.
STRAND 32 43 {ECO:0000244|PDB:1WTH}.
STRAND 48 54 {ECO:0000244|PDB:1WTH}.
HELIX 60 62 {ECO:0000244|PDB:1WTH}.
STRAND 69 74 {ECO:0000244|PDB:1WTH}.
STRAND 76 78 {ECO:0000244|PDB:1WTH}.
STRAND 84 93 {ECO:0000244|PDB:1WTH}.
STRAND 99 101 {ECO:0000244|PDB:2Z6B}.
STRAND 105 110 {ECO:0000244|PDB:1WTH}.
HELIX 112 115 {ECO:0000244|PDB:1WTH}.
HELIX 128 139 {ECO:0000244|PDB:1WTH}.
TURN 140 146 {ECO:0000244|PDB:1WTH}.
STRAND 149 151 {ECO:0000244|PDB:1K28}.
HELIX 166 176 {ECO:0000244|PDB:1WTH}.
TURN 180 183 {ECO:0000244|PDB:1WTH}.
STRAND 184 190 {ECO:0000244|PDB:1WTH}.
STRAND 195 199 {ECO:0000244|PDB:1WTH}.
HELIX 200 204 {ECO:0000244|PDB:1WTH}.
STRAND 209 213 {ECO:0000244|PDB:1WTH}.
STRAND 230 239 {ECO:0000244|PDB:1WTH}.
HELIX 242 244 {ECO:0000244|PDB:1WTH}.
HELIX 247 250 {ECO:0000244|PDB:1WTH}.
STRAND 251 256 {ECO:0000244|PDB:1WTH}.
STRAND 258 261 {ECO:0000244|PDB:1WTH}.
STRAND 265 268 {ECO:0000244|PDB:1WTH}.
STRAND 273 278 {ECO:0000244|PDB:1WTH}.
HELIX 281 285 {ECO:0000244|PDB:1WTH}.
STRAND 286 291 {ECO:0000244|PDB:1WTH}.
HELIX 292 301 {ECO:0000244|PDB:1WTH}.
STRAND 306 313 {ECO:0000244|PDB:1WTH}.
STRAND 323 327 {ECO:0000244|PDB:1WTH}.
STRAND 335 346 {ECO:0000244|PDB:1WTH}.
STRAND 351 359 {ECO:0000244|PDB:1WTH}.
SEQUENCE 391 AA; 44389 MW; 0DABEFE1D890B1FA CRC64;
MSMLQRPGYP NLSVKLFDSY DAWSNNRFVE LAATITTLTM RDSLYGRNEG MLQFYDSKNI
HTKMDGNEII QISVANANDI NNVKTRIYGC KHFSVSVDSK GDNIIAIELG TIHSIENLKF
GRPFFPDAGE SIKEMLGVIY QDRTLLTPAI NAINAYVPDI PWTSTFENYL SYVREVALAV
GSDKFVFVWQ DIMGVNMMDY DMMINQEPYP MIVGEPSLIG QFIQELKYPL AYDFVWLTKS
NPHKRDPMKN ATIYAHSFLD SSIPMITTGK GENSIVVSRS GAYSEMTYRN GYEEAIRLQT
MAQYDGYAKC STIGNFNLTP GVKIIFNDSK NQFKTEFYVD EVIHELSNNN SVTHLYMFTN
ATKLETIDPV KVKNEFKSDT TTEESSSSNK Q


Related products :

Catalog number Product name Quantity
03-GP27 Polyclonal antibody Anti-NPRAP_Neurojungin (delta-Catenin) 25 μl
EIAAB40693 Central element synaptonemal complex protein 1,CESC1,Homo sapiens,Human,SYCE2,Synaptonemal complex central element protein 2
OBT1901 RECOMBINANT SARS SPIKE PROTEIN, Product Type Recombinant Protein, Specificity SARS SPIKE PROTEIN, Target Species Viral, Host N_A, Format Rec. Protein, Isotypes , Applications E, Clone 0.1 mg
SCH-OBT1901 RECOMBINANT SARS SPIKE PROTEIN, Product Type Recombinant Protein, Specificity SARS SPIKE PROTEIN, Target Species Viral, Host N_A, Format Rec. Protein, Isotypes , Applications E, Clone 0.1 mg
SCH-OBT1901X RECOMBINANT SARS SPIKE PROTEIN, Product Type Recombinant Protein, Specificity SARS SPIKE PROTEIN, Target Species Viral, Host N_A, Format Rec. Protein, Isotypes , Applications E, WB, Clone 1 mg
OBT1901X RECOMBINANT SARS SPIKE PROTEIN, Product Type Recombinant Protein, Specificity SARS SPIKE PROTEIN, Target Species Viral, Host N_A, Format Rec. Protein, Isotypes , Applications E, WB, Clone 1 mg
SYCE1_RAT ELISA Kit FOR Synaptonemal complex central element protein 1; organism: Rat; gene name: Syce1 96T
20-783-71068 MOUSE ANTI HUMAN CD151 - Platelet-endothelial tetraspan antigen 3; PETA-3; GP27; Membrane glycoprotein SFA-1; Tetraspanin-24; Tspan-24 Monoclonal 0.2 mg
20-783-71070 MOUSE ANTI HUMAN CD151 - Platelet-endothelial tetraspan antigen 3; PETA-3; GP27; Membrane glycoprotein SFA-1; Tetraspanin-24; Tspan-24 Monoclonal 0.1 mg
20-783-71071 MOUSE ANTI HUMAN CD151 RPE - Platelet-endothelial tetraspan antigen 3; PETA-3; GP27; Membrane glycoprotein SFA-1; Tetraspanin-24; Tspan-24 Monoclonal 100 TESTS
20-783-71069 MOUSE ANTI HUMAN CD151 FITC - Platelet-endothelial tetraspan antigen 3; PETA-3; GP27; Membrane glycoprotein SFA-1; Tetraspanin-24; Tspan-24 Monoclonal 0.1 mg
SYCE1_MOUSE ELISA Kit FOR Synaptonemal complex central element protein 1; organism: Mouse; gene name: Syce1 96T
SYC1L_MOUSE ELISA Kit FOR Synaptonemal complex central element protein 1-like; organism: Mouse; gene name: Syce1l 96T
SYCE2_MOUSE ELISA Kit FOR Synaptonemal complex central element protein 2; organism: Mouse; gene name: Syce2 96T
101-M289 CD151 Anti-Human Host: Mouse CD151; GP27; MER2; RAPH; SFA1; PETA-3; TSPAN24 100
101-M289 CD151, Host: Mouse, Species: Anti-Human, Synonyms: CD151; GP27; MER2; RAPH; SFA1; PETA-3; TSPAN24 100 ug
SYCE2 SYCE2 Gene synaptonemal complex central element protein 2
SYCE1L SYCE1L Gene synaptonemal complex central element protein 1-like
SYCE1 SYCE1 Gene synaptonemal complex central element protein 1
EIAAB06269 Cd151,CD151 antigen,GP27,Membrane glycoprotein SFA-1,Mouse,Mus musculus,Peta3,PETA-3,Platelet-endothelial tetraspan antigen 3
EIAAB06271 CD151,CD151 antigen,GP27,Homo sapiens,Human,Membrane glycoprotein SFA-1,PETA-3,Platelet-endothelial tetraspan antigen 3,Tetraspanin-24,TSPAN24,Tspan-24
EIAAB40683 Meiosis-related protein,Mmrp2,Mouse,Mus musculus,Syce1l,Synaptonemal complex central element protein 1-like
EIAAB40684 Homo sapiens,Human,Meiosis-related protein,SYCE1L,Synaptonemal complex central element protein 1-like
62-015 anti_yeast Taf10p antibody, rabbit serum The basal transcription factor TFIID plays a central role in the regulation of gene expression in Eukaryota and is a large protein complex composed of TATA box 50 ul
62-016 anti_yeast Taf10p antibody, rabbit serum The basal transcription factor TFIID plays a central role in the regulation of gene expression in Eukaryota and is a large protein complex composed of TATA box 250 ul


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur