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Baseplate hub protein gp44 (43 kDa tail protein) (Gene product 44) (gp44) (Gene product P) (gpP)

 BP44_BPMU               Reviewed;         379 AA.
P08558;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
01-AUG-1988, sequence version 1.
16-JAN-2019, entry version 86.
RecName: Full=Baseplate hub protein gp44;
AltName: Full=43 kDa tail protein;
AltName: Full=Gene product 44;
Short=gp44;
AltName: Full=Gene product P;
Short=gpP;
Name=P; OrderedLocusNames=Mup44;
Escherichia phage Mu (Bacteriophage Mu).
Viruses; dsDNA viruses, no RNA stage; Caudovirales; Myoviridae;
Muvirus.
NCBI_TaxID=10677;
NCBI_TaxID=543; Enterobacteriaceae.
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=MUCTS62PAP1;
PubMed=2968539; DOI=10.1093/nar/16.11.5211;
Chaconas G., Gloor G.;
"Sequence of bacteriophage Mu N and P genes.";
Nucleic Acids Res. 16:5211-5212(1988).
[2]
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).
[3]
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).
[4]
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).
[5]
CHARACTERIZATION, SUBUNIT, AND CLEAVAGE OF C-TERMINUS.
PubMed=15944413; DOI=10.1093/jb/mvi076;
Kitazawa D., Takeda S., Kageyama Y., Tomihara M., Fukada H.;
"Expression and characterization of a baseplate protein for
bacteriophage Mu, gp44.";
J. Biochem. 137:601-606(2005).
[6]
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).
[7]
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).
[8]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), SUBCELLULAR LOCATION, AND
SUBUNIT.
PubMed=16125724; DOI=10.1016/j.jmb.2005.07.044;
Kondou Y., Kitazawa D., Takeda S., Tsuchiya Y., Yamashita E.,
Mizuguchi M., Kawano K., Tsukihara T.;
"Structure of the central hub of bacteriophage Mu baseplate determined
by X-ray crystallography of gp44.";
J. Mol. Biol. 352:976-985(2005).
-!- FUNCTION: Forms the central cylindrical hub of the baseplate and
plays an important role in baseplate and tail assembly (Probable).
Core component of the initiator complex that triggers the tail
tube polymerization during tail assembly (Probable). Forms a
conduit that probably functions as an extension of the tail tube
allowing viral DNA release during ejection. Might facilitate the
interaction of the virus with the host cell surface through
electrostatic interactions during virus entry into host cell.
{ECO:0000305}.
-!- SUBUNIT: Heterotrimer of one uncleaved (42 kDa) and two cleaved
(40 kDa) forms. Forms a hub-like structure with an inner diameter
of 25 Angstroms through which DNA can presumably pass during
infection. 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:15944413, ECO:0000269|PubMed:16125724,
ECO:0000269|PubMed:27555589}.
-!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:16125724,
ECO:0000269|PubMed:27555589}. Host cytoplasm
{ECO:0000305|PubMed:16125724}. 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: C-terminal region forms a flexible domain. {ECO:0000305}.
-!- PTM: Cleavage of the C-terminus gives rise to a shorter 40 kDa
form.
-!- DISRUPTION PHENOTYPE: No tail is synthesized.
{ECO:0000269|PubMed:3904174}.
-----------------------------------------------------------------------
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EMBL; X06796; CAA29956.1; -; Genomic_DNA.
EMBL; AF083977; AAF01122.1; -; Genomic_DNA.
PIR; S01891; ZPBPMU.
RefSeq; NP_050648.1; NC_000929.1.
PDB; 1WRU; X-ray; 2.10 A; A=1-379.
PDBsum; 1WRU; -.
ProteinModelPortal; P08558; -.
SMR; P08558; -.
GeneID; 2636285; -.
KEGG; vg:2636285; -.
EvolutionaryTrace; P08558; -.
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: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.
Gene3D; 3.30.1920.10; -; 1.
InterPro; IPR023399; Baseplate-like_2-layer_sand.
InterPro; IPR026276; Baseplate_GpP.
PIRSF; PIRSF004440; GpP; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Host cytoplasm; Late protein;
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 1 379 Baseplate hub protein gp44.
/FTId=PRO_0000077692.
DNA_BIND 209 228 H-T-H motif. {ECO:0000255}.
REGION 216 224 Disordered. {ECO:0000255}.
REGION 345 379 Disordered. {ECO:0000255}.
STRAND 5 9 {ECO:0000244|PDB:1WRU}.
STRAND 12 15 {ECO:0000244|PDB:1WRU}.
STRAND 18 25 {ECO:0000244|PDB:1WRU}.
STRAND 32 39 {ECO:0000244|PDB:1WRU}.
HELIX 46 48 {ECO:0000244|PDB:1WRU}.
STRAND 53 58 {ECO:0000244|PDB:1WRU}.
STRAND 61 75 {ECO:0000244|PDB:1WRU}.
STRAND 80 88 {ECO:0000244|PDB:1WRU}.
HELIX 91 95 {ECO:0000244|PDB:1WRU}.
STRAND 101 108 {ECO:0000244|PDB:1WRU}.
HELIX 110 118 {ECO:0000244|PDB:1WRU}.
HELIX 119 121 {ECO:0000244|PDB:1WRU}.
STRAND 125 127 {ECO:0000244|PDB:1WRU}.
HELIX 132 135 {ECO:0000244|PDB:1WRU}.
STRAND 138 142 {ECO:0000244|PDB:1WRU}.
HELIX 149 158 {ECO:0000244|PDB:1WRU}.
TURN 159 161 {ECO:0000244|PDB:1WRU}.
STRAND 163 166 {ECO:0000244|PDB:1WRU}.
HELIX 168 170 {ECO:0000244|PDB:1WRU}.
STRAND 172 175 {ECO:0000244|PDB:1WRU}.
STRAND 180 187 {ECO:0000244|PDB:1WRU}.
TURN 188 190 {ECO:0000244|PDB:1WRU}.
STRAND 191 198 {ECO:0000244|PDB:1WRU}.
STRAND 205 209 {ECO:0000244|PDB:1WRU}.
STRAND 233 236 {ECO:0000244|PDB:1WRU}.
STRAND 245 248 {ECO:0000244|PDB:1WRU}.
HELIX 256 274 {ECO:0000244|PDB:1WRU}.
STRAND 275 285 {ECO:0000244|PDB:1WRU}.
STRAND 297 302 {ECO:0000244|PDB:1WRU}.
HELIX 303 305 {ECO:0000244|PDB:1WRU}.
STRAND 312 322 {ECO:0000244|PDB:1WRU}.
TURN 323 325 {ECO:0000244|PDB:1WRU}.
STRAND 326 335 {ECO:0000244|PDB:1WRU}.
HELIX 336 339 {ECO:0000244|PDB:1WRU}.
SEQUENCE 379 AA; 41785 MW; E09AED2158D13CA1 CRC64;
MSNTVTLRAD GRLFTGWTSV SVTRSIESVA GYFELGVNVP PGTDLSGLAP GKKFTLEIGG
QIVCTGYIDS RRRQMTADSM KITVAGRDKT ADLIDCAAVY SGGQWKNRTL EQIARDLCAP
YGVTVRWELS DKESSAAFPG FTLDHSETVY EALVRASRAR GVLMTSNAAG ELVFSRAAST
ATDELVLGEN LLTLDFEEDF RDRFSEYTVK GYARANGAEG DDIDAKSIVS RKGTATDSDV
TRYRPMIIIA DSKITAKDAQ ARALREQRRR LAKSITFEAE IDGWTRKDGQ LWMPNLLVTI
DASKYAIKTT ELLVSKVTLI LNDQDGLKTR VSLAPREGFL VPVESDRKNR KGGDSNGGID
ALVEDYYRRH PEKTPPWKE


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Kits Elisa; taq POLYMERASE

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