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Baseplate puncturing device gp45 (Baseplate spike protein) (Gene product 45) (gp45) (Gene product Q) (gpQ)

 BP45_BPMU               Reviewed;         197 AA.
Q9T1V4;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
22-NOV-2017, entry version 62.
RecName: Full=Baseplate puncturing device gp45;
AltName: Full=Baseplate spike protein;
AltName: Full=Gene product 45;
Short=gp45;
AltName: Full=Gene product Q;
Short=gpQ;
OrderedLocusNames=Mup45;
Escherichia phage Mu (Bacteriophage Mu).
Viruses; dsDNA viruses, no RNA stage; Caudovirales; Myoviridae;
Muvirus.
NCBI_TaxID=10677;
NCBI_TaxID=543; Enterobacteriaceae.
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=11922669; DOI=10.1006/jmbi.2002.5437;
Morgan G.J., Hatfull G.F., Casjens S., Hendrix R.W.;
"Bacteriophage Mu genome sequence: analysis and comparison with Mu-
like prophages in Haemophilus, Neisseria and Deinococcus.";
J. Mol. Biol. 317:337-359(2002).
[2]
DISRUPTION PHENOTYPE.
PubMed=3904174; DOI=10.1016/0042-6822(85)90388-5;
Grundy F.J., Howe M.M.;
"Morphogenetic structures present in lysates of amber mutants of
bacteriophage Mu.";
Virology 143:485-504(1985).
[3]
INDUCTION.
PubMed=8293968;
Chiang L.W., Howe M.M.;
"Mutational analysis of a C-dependent late promoter of bacteriophage
Mu.";
Genetics 135:619-629(1993).
[4]
FUNCTION, AND SUBUNIT.
PubMed=20478417; DOI=10.1016/j.bbapap.2010.05.003;
Suzuki H., Yamada S., Toyama Y., Takeda S.;
"The C-terminal domain is sufficient for host-binding activity of the
Mu phage tail-spike protein.";
Biochim. Biophys. Acta 1804:1738-1742(2010).
[5]
REVIEW.
PubMed=22297511; DOI=10.1007/978-1-4614-0980-9_5;
Leiman P.G., Shneider M.M.;
"Contractile tail machines of bacteriophages.";
Adv. Exp. Med. Biol. 726:93-114(2012).
[6]
SUBUNIT, AND SUBCELLULAR LOCATION.
PubMed=27555589; DOI=10.1073/pnas.1607966113;
Buettner C.R., Wu Y., Maxwell K.L., Davidson A.R.;
"Baseplate assembly of phage Mu: Defining the conserved core
components of contractile-tailed phages and related bacterial
systems.";
Proc. Natl. Acad. Sci. U.S.A. 113:10174-10179(2016).
[7]
X-RAY CRYSTALLOGRAPHY (1.44 ANGSTROMS) OF 92-197, FUNCTION, SUBUNIT,
DOMAIN, COFACTOR, AND MUTAGENESIS OF ASP-188.
PubMed=22922659; DOI=10.1016/j.bbapap.2012.08.015;
Harada K., Yamashita E., Nakagawa A., Miyafusa T., Tsumoto K.,
Ueno T., Toyama Y., Takeda S.;
"Crystal structure of the C-terminal domain of Mu phage central spike
and functions of bound calcium ion.";
Biochim. Biophys. Acta 1834:284-291(2013).
-!- FUNCTION: Component of the baseplate that forms a central
needlelike spike used to puncture the host cell membrane for tube
insertion during virus entry. Probably involved in baseplate and
tail assembly. Serves as the distal plug of tail tube channel and
might regulate the process of the phage DNA and protein ejection
into the host cell. {ECO:0000269|PubMed:20478417,
ECO:0000269|PubMed:22922659}.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Evidence={ECO:0000269|PubMed:22922659};
Note=Binds 1 Ca(2+) cation per trimer. Ca(2+) plays an important
role in interaction with the host cell membrane.
{ECO:0000269|PubMed:22922659};
-!- COFACTOR:
Name=chloride; Xref=ChEBI:CHEBI:17996;
Evidence={ECO:0000269|PubMed:22922659};
Note=Binds 1 Cl(-) ion per trimer. {ECO:0000269|PubMed:22922659};
-!- COFACTOR:
Name=Fe cation; Xref=ChEBI:CHEBI:24875;
Evidence={ECO:0000269|PubMed:22922659};
Note=Binds 1 Fe cation per trimer. {ECO:0000269|PubMed:22922659};
-!- SUBUNIT: Homotrimer (PubMed:20478417, PubMed:22922659). Part of a
complex composed of three DNA circularization protein N, three
baseplate hub protein gp44 and three sub-complex wedge (made of
two copies of each baseplate protein gp46, gp47 and gp48) that
forms the baseplate (PubMed:27555589).
{ECO:0000269|PubMed:20478417, ECO:0000269|PubMed:22922659,
ECO:0000269|PubMed:27555589}.
-!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:27555589}. Host
cytoplasm {ECO:0000305}. Note=Baseplate protein.
{ECO:0000269|PubMed:27555589}.
-!- INDUCTION: Expressed in the late phase of the viral replicative
cycle. Expression of late genes is activated by the viral late
transcription activator C. {ECO:0000269|PubMed:8293968}.
-!- DOMAIN: The C-terminus is a needlelike shaped homotrimer
consisting of an intertwined beta-sheet, a triple beta-helix and a
metal-binding region. {ECO:0000269|PubMed:22922659}.
-!- DISRUPTION PHENOTYPE: No tail is synthesized.
{ECO:0000269|PubMed:3904174}.
-!- CAUTION: Translation initiates from a non-canonical start codon
(GUG). {ECO:0000305}.
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EMBL; AF083977; AAF01123.1; -; Genomic_DNA.
RefSeq; NP_050649.1; NC_000929.1.
PDB; 3VTN; X-ray; 1.75 A; A=100-197.
PDB; 3VTO; X-ray; 1.44 A; A/B/C/P/Q/R=92-197.
PDBsum; 3VTN; -.
PDBsum; 3VTO; -.
SMR; Q9T1V4; -.
GeneID; 2636280; -.
KEGG; vg:2636280; -.
OrthoDB; VOG090000U1; -.
Proteomes; UP000002611; Genome.
GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0098025; C:virus tail, baseplate; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0099000; P:viral genome ejection through host cell envelope, contractile tail mechanism; IEA:UniProtKB-KW.
GO; GO:0098003; P:viral tail assembly; IEA:UniProtKB-KW.
InterPro; IPR013046; GpV/Gp45.
InterPro; IPR014462; Phage_Mu_Gp45.
Pfam; PF06890; Phage_Mu_Gp45; 1.
PIRSF; PIRSF012337; gp45; 1.
TIGRFAMs; TIGR01644; phage_P2_V; 1.
1: Evidence at protein level;
3D-structure; Calcium; Chloride; Complete proteome; Host cytoplasm;
Iron; Late protein; Metal-binding; Reference proteome;
Viral baseplate protein; Viral contractile tail ejection system;
Viral genome ejection through host cell envelope;
Viral penetration into host cytoplasm; Viral release from host cell;
Viral tail assembly; Viral tail protein; Virion;
Virus entry into host cell.
CHAIN 1 197 Baseplate puncturing device gp45.
/FTId=PRO_0000077838.
REGION 177 197 Ions binding.
METAL 183 183 Iron; via tele nitrogen; shared with
trimeric partners.
METAL 185 185 Iron; via tele nitrogen; shared with
trimeric partners.
METAL 188 188 Calcium; shared with trimeric partners.
METAL 189 189 Calcium; shared with trimeric partners.
BINDING 188 188 Chloride; via amide nitrogen; shared with
trimeric partners.
MUTAGEN 188 188 D->A: Loss of membrane-binding ability.
{ECO:0000269|PubMed:22922659}.
STRAND 104 107 {ECO:0000244|PDB:3VTO}.
STRAND 113 117 {ECO:0000244|PDB:3VTO}.
TURN 118 120 {ECO:0000244|PDB:3VTO}.
STRAND 121 140 {ECO:0000244|PDB:3VTO}.
STRAND 142 154 {ECO:0000244|PDB:3VTO}.
STRAND 156 160 {ECO:0000244|PDB:3VTO}.
STRAND 162 166 {ECO:0000244|PDB:3VTO}.
STRAND 168 171 {ECO:0000244|PDB:3VTO}.
STRAND 173 175 {ECO:0000244|PDB:3VTO}.
TURN 180 182 {ECO:0000244|PDB:3VTO}.
STRAND 190 192 {ECO:0000244|PDB:3VTO}.
SEQUENCE 197 AA; 21689 MW; 448C7A7ADCADD5C9 CRC64;
MERVNDSALN RLLTPLMRRV RLMLARAVVN VINDGRKVQN LQVGLLDDEE SDEVERLQNY
GHFSVPLPGA EALIACVGAQ RDQGIAVVVE DRRYRPTNLE PGDAGIYHHE GHRIRLTKDG
RCIITCKTVE VYADESMTVD TPRTTFTGDV EIQKGLGVKG KSQFDSNITA PDAIINGKST
DKHIHRGDSG GTTGPMQ


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