BP45_BPMU
ID BP45_BPMU Reviewed; 197 AA.
AC Q9T1V4;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Baseplate puncturing device gp45;
DE AltName: Full=Baseplate spike protein;
DE AltName: Full=Gene product 45;
DE Short=gp45;
DE AltName: Full=Gene product Q;
DE Short=gpQ;
GN OrderedLocusNames=Mup45;
OS Escherichia phage Mu (Bacteriophage Mu).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Myoviridae; Muvirus.
OX NCBI_TaxID=10677;
OH NCBI_TaxID=543; Enterobacteriaceae.
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11922669; DOI=10.1006/jmbi.2002.5437;
RA Morgan G.J., Hatfull G.F., Casjens S., Hendrix R.W.;
RT "Bacteriophage Mu genome sequence: analysis and comparison with Mu-like
RT prophages in Haemophilus, Neisseria and Deinococcus.";
RL J. Mol. Biol. 317:337-359(2002).
RN [2]
RP DISRUPTION PHENOTYPE.
RX PubMed=3904174; DOI=10.1016/0042-6822(85)90388-5;
RA Grundy F.J., Howe M.M.;
RT "Morphogenetic structures present in lysates of amber mutants of
RT bacteriophage Mu.";
RL Virology 143:485-504(1985).
RN [3]
RP INDUCTION.
RX PubMed=8293968; DOI=10.1093/genetics/135.3.619;
RA Chiang L.W., Howe M.M.;
RT "Mutational analysis of a C-dependent late promoter of bacteriophage Mu.";
RL Genetics 135:619-629(1993).
RN [4]
RP FUNCTION, AND SUBUNIT.
RX PubMed=20478417; DOI=10.1016/j.bbapap.2010.05.003;
RA Suzuki H., Yamada S., Toyama Y., Takeda S.;
RT "The C-terminal domain is sufficient for host-binding activity of the Mu
RT phage tail-spike protein.";
RL Biochim. Biophys. Acta 1804:1738-1742(2010).
RN [5]
RP REVIEW.
RX PubMed=22297511; DOI=10.1007/978-1-4614-0980-9_5;
RA Leiman P.G., Shneider M.M.;
RT "Contractile tail machines of bacteriophages.";
RL Adv. Exp. Med. Biol. 726:93-114(2012).
RN [6]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=27555589; DOI=10.1073/pnas.1607966113;
RA Buettner C.R., Wu Y., Maxwell K.L., Davidson A.R.;
RT "Baseplate assembly of phage Mu: Defining the conserved core components of
RT contractile-tailed phages and related bacterial systems.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:10174-10179(2016).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.44 ANGSTROMS) OF 92-197, FUNCTION, SUBUNIT,
RP DOMAIN, COFACTOR, AND MUTAGENESIS OF ASP-188.
RX PubMed=22922659; DOI=10.1016/j.bbapap.2012.08.015;
RA Harada K., Yamashita E., Nakagawa A., Miyafusa T., Tsumoto K., Ueno T.,
RA Toyama Y., Takeda S.;
RT "Crystal structure of the C-terminal domain of Mu phage central spike and
RT functions of bound calcium ion.";
RL Biochim. Biophys. Acta 1834:284-291(2013).
CC -!- FUNCTION: Component of the baseplate that forms a central needlelike
CC spike used to puncture the host cell membrane for tube insertion during
CC virus entry. Probably involved in baseplate and tail assembly. Serves
CC as the distal plug of tail tube channel and might regulate the process
CC of the phage DNA and protein ejection into the host cell.
CC {ECO:0000269|PubMed:20478417, ECO:0000269|PubMed:22922659}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:22922659};
CC Note=Binds 1 Ca(2+) cation per trimer. Ca(2+) plays an important role
CC in interaction with the host cell membrane.
CC {ECO:0000269|PubMed:22922659};
CC -!- COFACTOR:
CC Name=chloride; Xref=ChEBI:CHEBI:17996;
CC Evidence={ECO:0000269|PubMed:22922659};
CC Note=Binds 1 Cl(-) ion per trimer. {ECO:0000269|PubMed:22922659};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000269|PubMed:22922659};
CC Note=Binds 1 Fe cation per trimer. {ECO:0000269|PubMed:22922659};
CC -!- SUBUNIT: Homotrimer (PubMed:20478417, PubMed:22922659). Part of a
CC complex composed of three DNA circularization protein N, three
CC baseplate hub protein gp44 and three sub-complex wedge (made of two
CC copies of each baseplate protein gp46, gp47 and gp48) that forms the
CC baseplate (PubMed:27555589). {ECO:0000269|PubMed:20478417,
CC ECO:0000269|PubMed:22922659, ECO:0000269|PubMed:27555589}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:27555589}. Host
CC cytoplasm {ECO:0000305}. Note=Baseplate protein.
CC {ECO:0000269|PubMed:27555589}.
CC -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC Expression of late genes is activated by the viral late transcription
CC activator C. {ECO:0000269|PubMed:8293968}.
CC -!- DOMAIN: The C-terminus is a needlelike shaped homotrimer consisting of
CC an intertwined beta-sheet, a triple beta-helix and a metal-binding
CC region. {ECO:0000269|PubMed:22922659}.
CC -!- DISRUPTION PHENOTYPE: No tail is synthesized.
CC {ECO:0000269|PubMed:3904174}.
CC -!- CAUTION: Translation initiates from a non-canonical start codon (GUG).
CC {ECO:0000305}.
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DR EMBL; AF083977; AAF01123.1; -; Genomic_DNA.
DR RefSeq; NP_050649.1; NC_000929.1.
DR PDB; 3VTN; X-ray; 1.75 A; A=100-197.
DR PDB; 3VTO; X-ray; 1.44 A; A/B/C/P/Q/R=92-197.
DR PDBsum; 3VTN; -.
DR PDBsum; 3VTO; -.
DR SMR; Q9T1V4; -.
DR GeneID; 2636280; -.
DR KEGG; vg:2636280; -.
DR Proteomes; UP000002611; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0098025; C:virus tail, baseplate; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0099000; P:viral genome ejection through host cell envelope, contractile tail mechanism; IEA:UniProtKB-KW.
DR GO; GO:0098003; P:viral tail assembly; IEA:UniProtKB-KW.
DR InterPro; IPR013046; GpV/Gp45.
DR InterPro; IPR014462; Phage_Mu_Gp45.
DR InterPro; IPR040629; Phage_spike.
DR Pfam; PF06890; Phage_Mu_Gp45; 1.
DR Pfam; PF18715; Phage_spike; 1.
DR PIRSF; PIRSF012337; gp45; 1.
DR TIGRFAMs; TIGR01644; phage_P2_V; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Chloride; Host cytoplasm; Iron; Late protein;
KW Metal-binding; Reference proteome; Viral baseplate protein;
KW Viral contractile tail ejection system;
KW Viral genome ejection through host cell envelope;
KW Viral penetration into host cytoplasm; Viral release from host cell;
KW Viral tail assembly; Viral tail protein; Virion;
KW Virus entry into host cell.
FT CHAIN 1..197
FT /note="Baseplate puncturing device gp45"
FT /id="PRO_0000077838"
FT REGION 172..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 183
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="ligand shared between trimeric partners"
FT BINDING 185
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="ligand shared between trimeric partners"
FT BINDING 188
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_note="ligand shared between trimeric partners"
FT BINDING 188
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /ligand_note="ligand shared between trimeric partners"
FT BINDING 189
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_note="ligand shared between trimeric partners"
FT MUTAGEN 188
FT /note="D->A: Loss of membrane-binding ability."
FT /evidence="ECO:0000269|PubMed:22922659"
FT STRAND 104..107
FT /evidence="ECO:0007829|PDB:3VTO"
FT STRAND 113..117
FT /evidence="ECO:0007829|PDB:3VTO"
FT TURN 118..120
FT /evidence="ECO:0007829|PDB:3VTO"
FT STRAND 121..140
FT /evidence="ECO:0007829|PDB:3VTO"
FT STRAND 142..154
FT /evidence="ECO:0007829|PDB:3VTO"
FT STRAND 156..160
FT /evidence="ECO:0007829|PDB:3VTO"
FT STRAND 162..166
FT /evidence="ECO:0007829|PDB:3VTO"
FT STRAND 168..171
FT /evidence="ECO:0007829|PDB:3VTO"
FT STRAND 173..175
FT /evidence="ECO:0007829|PDB:3VTO"
FT TURN 180..182
FT /evidence="ECO:0007829|PDB:3VTO"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:3VTO"
SQ 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
