PHUZ_BP201
ID PHUZ_BP201 Reviewed; 315 AA.
AC B3FK34;
DT 07-NOV-2018, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=Phage tubulin-like protein {ECO:0000305};
DE Short=PhuZ {ECO:0000303|PubMed:22726436};
DE EC=3.6.5.- {ECO:0000269|PubMed:22726436};
DE AltName: Full=Phage tubulin/FtsZ {ECO:0000303|PubMed:22726436};
DE AltName: Full=Tubulin-like protein TubZ {ECO:0000305};
GN ORFNames=201phi2-1p059 {ECO:0000312|EMBL:ABY62892.1};
OS Pseudomonas phage 201phi2-1 (Pseudomonas chlororaphis phage 201phi2-1).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Myoviridae.
OX NCBI_TaxID=198110;
OH NCBI_TaxID=587753; Pseudomonas chlororaphis.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=18474389; DOI=10.1016/j.virol.2008.04.004;
RA Thomas J.A., Rolando M.R., Carroll C.A., Shen P.S., Belnap D.M.,
RA Weintraub S.T., Serwer P., Hardies S.C.;
RT "Characterization of Pseudomonas chlororaphis myovirus 201varphi2-1 via
RT genomic sequencing, mass spectrometry, and electron microscopy.";
RL Virology 376:330-338(2008).
RN [2]
RP FUNCTION, ACTIVITY REGULATION, SUBUNIT, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF ASP-190.
RX PubMed=25429514; DOI=10.7554/elife.03197;
RA Erb M.L., Kraemer J.A., Coker J.K., Chaikeeratisak V., Nonejuie P.,
RA Agard D.A., Pogliano J.;
RT "A bacteriophage tubulin harnesses dynamic instability to center DNA in
RT infected cells.";
RL Elife 3:0-0(2014).
RN [3]
RP FUNCTION IN BACTERIOPHAGE DNA POSITIONING, AND MUTAGENESIS OF ASP-190.
RX PubMed=28082593; DOI=10.1126/science.aal2130;
RA Chaikeeratisak V., Nguyen K., Khanna K., Brilot A.F., Erb M.L., Coker J.K.,
RA Vavilina A., Newton G.L., Buschauer R., Pogliano K., Villa E., Agard D.A.,
RA Pogliano J.;
RT "Assembly of a nucleus-like structure during viral replication in
RT bacteria.";
RL Science 355:194-197(2017).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=28813669; DOI=10.1016/j.celrep.2017.07.064;
RA Chaikeeratisak V., Nguyen K., Egan M.E., Erb M.L., Vavilina A.,
RA Pogliano J.;
RT "The Phage Nucleus and Tubulin Spindle Are Conserved among Large
RT Pseudomonas Phages.";
RL Cell Rep. 20:1563-1571(2017).
RN [5]
RP FUNCTION IN BACTERIOPHAGE CAPSID MOVEMENT, AND MUTAGENESIS OF ASP-190;
RP ASP-235; ASP-259 AND ASP-263.
RX PubMed=31199917; DOI=10.1016/j.cell.2019.05.032;
RA Chaikeeratisak V., Khanna K., Nguyen K.T., Sugie J., Egan M.E., Erb M.L.,
RA Vavilina A., Nonejuie P., Nieweglowska E., Pogliano K., Agard D.A.,
RA Villa E., Pogliano J.;
RT "Viral Capsid Trafficking along Treadmilling Tubulin Filaments in
RT Bacteria.";
RL Cell 177:1771-1780(2019).
RN [6] {ECO:0007744|PDB:3R4V, ECO:0007744|PDB:3RB8}
RP X-RAY CRYSTALLOGRAPHY (1.67 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP INDUCTION, DOMAIN, MUTAGENESIS OF ASP-187 AND ASP-190, SUBCELLULAR
RP LOCATION, AND SUBUNIT.
RX PubMed=22726436; DOI=10.1016/j.cell.2012.04.034;
RA Kraemer J.A., Erb M.L., Waddling C.A., Montabana E.A., Zehr E.A., Wang H.,
RA Nguyen K., Pham D.S., Agard D.A., Pogliano J.;
RT "A phage tubulin assembles dynamic filaments by an atypical mechanism to
RT center viral DNA within the host cell.";
RL Cell 149:1488-1499(2012).
RN [7] {ECO:0007744|PDB:3J5V}
RP STRUCTURE BY ELECTRON MICROSCOPY (7.10 ANGSTROMS) OF 2-315, FUNCTION, AND
RP MUTAGENESIS OF ARG-217; ASP-303 AND ASP-305.
RX PubMed=24631461; DOI=10.1016/j.str.2014.02.006;
RA Zehr E.A., Kraemer J.A., Erb M.L., Coker J.K., Montabana E.A., Pogliano J.,
RA Agard D.A.;
RT "The structure and assembly mechanism of a novel three-stranded tubulin
RT filament that centers phage DNA.";
RL Structure 22:539-548(2014).
CC -!- FUNCTION: A tubulin-like GTPase that forms filaments, which are
CC required for positioning viral DNA and capsids in the middle of the
CC host cell for optimal replication (PubMed:28082593, PubMed:22726436,
CC PubMed:25429514, PubMed:31199917, PubMed:28813669). The motor component
CC of a partition system which pushes phage DNA (encased by protein gp105)
CC to the center of the bacterial host cell (PubMed:28082593,
CC PubMed:28813669). Also required for movement of phage capsids to the
CC vicinity of the viral DNA and rotation of the encased viral DNA at
CC midcell (PubMed:31199917). Forms filaments during the lytic phase,
CC which position phage DNA at the center of the bacterial host cell
CC (PubMed:22726436, PubMed:25429514, PubMed:31199917, PubMed:28082593,
CC PubMed:28813669). Filaments have a three-stranded intertwined
CC achitecture and form a spindle-like cytoskeleton within the infected
CC cell (PubMed:24631461). Has GTPase activity (PubMed:22726436).
CC Filaments grow at the plus end and depolymerize at the minus end, a
CC process called treadmilling, and switch from growing in a polar manner
CC to catastrophic depolymerization, i.e. they display dynamic
CC instability, like tubulin. In infected host cells the filament ends
CC close to the cell pole are relatively stable, while the other end near
CC the phage DNA is highly dynamic (PubMed:25429514). Both capsid movement
CC and DNA rotation probably require treadmilling (Probable).
CC {ECO:0000269|PubMed:22726436, ECO:0000269|PubMed:24631461,
CC ECO:0000269|PubMed:25429514, ECO:0000269|PubMed:28082593,
CC ECO:0000269|PubMed:28813669, ECO:0000269|PubMed:31199917,
CC ECO:0000305|PubMed:31199917}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC Evidence={ECO:0000269|PubMed:22726436};
CC -!- ACTIVITY REGULATION: The non-hydrolyzable GTP analog GMPCPP stabilizes
CC filaments, which never disassemble. {ECO:0000269|PubMed:25429514}.
CC -!- SUBUNIT: Homomultimer (PubMed:22726436, PubMed:25429514). Polymerizes
CC in a strictly GTP-dependent manner (PubMed:22726436, PubMed:25429514).
CC {ECO:0000269|PubMed:22726436, ECO:0000269|PubMed:25429514}.
CC -!- INTERACTION:
CC B3FK34; B3FK34: 201phi2-1p059; NbExp=4; IntAct=EBI-16096260, EBI-16096260;
CC -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000269|PubMed:22726436,
CC ECO:0000269|PubMed:25429514}. Note=In infected host cells forms a
CC spindle-like structure emanating from each cell pole.
CC {ECO:0000269|PubMed:24631461, ECO:0000269|PubMed:25429514,
CC ECO:0000269|PubMed:28813669}.
CC -!- INDUCTION: Expressed by 1 hour post-infection (at protein level).
CC {ECO:0000269|PubMed:22726436, ECO:0000269|PubMed:28813669}.
CC -!- DOMAIN: Consists of two domains: a nucleotide-binding N-terminus that
CC hydrolyzes GTP and a C-terminus domain necessary for polymerization
CC (PubMed:22726436). The domains are bridged by a long, central helix
CC (PubMed:22726436). Interactions between the C-terminus and the
CC following monomer drive polymerization (PubMed:22726436).
CC {ECO:0000269|PubMed:22726436}.
CC -!- SIMILARITY: Belongs to the FtsZ family. PhuZ subfamily. {ECO:0000305}.
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DR EMBL; EU197055; ABY62892.1; -; Genomic_DNA.
DR RefSeq; YP_001956784.1; NC_010821.1.
DR PDB; 3J5V; EM; 7.10 A; a=2-315.
DR PDB; 3R4V; X-ray; 1.67 A; A=1-315.
DR PDB; 3RB8; X-ray; 2.60 A; A=2-315.
DR PDBsum; 3J5V; -.
DR PDBsum; 3R4V; -.
DR PDBsum; 3RB8; -.
DR SMR; B3FK34; -.
DR DIP; DIP-60806N; -.
DR GeneID; 6372455; -.
DR KEGG; vg:6372455; -.
DR Proteomes; UP000002421; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:RHEA.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0051649; P:establishment of localization in cell; IDA:CACAO.
DR Gene3D; 3.40.50.1440; -; 1.
DR InterPro; IPR036525; Tubulin/FtsZ_GTPase_sf.
DR SUPFAM; SSF52490; SSF52490; 1.
PE 1: Evidence at protein level;
KW 3D-structure; GTP-binding; Host cytoplasm; Hydrolase; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..315
FT /note="Phage tubulin-like protein"
FT /id="PRO_0000445603"
FT BINDING 12..13
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q8KNP3"
FT BINDING 93..95
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q8KNP3"
FT BINDING 165
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q8KNP3"
FT SITE 187
FT /note="GTP hydrolysis"
FT /evidence="ECO:0000269|PubMed:22726436"
FT SITE 190
FT /note="GTP hydrolysis"
FT /evidence="ECO:0000269|PubMed:22726436"
FT MUTAGEN 187
FT /note="D->A: Impaired GTP hydrolysis and polymerization
FT dynamics."
FT /evidence="ECO:0000269|PubMed:22726436"
FT MUTAGEN 190
FT /note="D->A: Impaired GTP hydrolysis and polymerization
FT dynamics. Reduces critical concentration for
FT polymerization, filaments no longer depolymerize. Encased
FT viral DNA stays at cell poles. Empty phage capsids are
FT immobile, probably on PhuZ filaments."
FT /evidence="ECO:0000269|PubMed:22726436,
FT ECO:0000269|PubMed:25429514, ECO:0000269|PubMed:28082593,
FT ECO:0000269|PubMed:31199917"
FT MUTAGEN 217
FT /note="R->A,D: Complete loss of ability to form filaments."
FT /evidence="ECO:0000269|PubMed:24631461"
FT MUTAGEN 235
FT /note="D->A: Blocks filament assembly."
FT /evidence="ECO:0000269|PubMed:31199917"
FT MUTAGEN 259
FT /note="D->A: No visible effect on filament formation, viral
FT capsid movement capsid filling or phage DNA rotation."
FT /evidence="ECO:0000269|PubMed:31199917"
FT MUTAGEN 263
FT /note="D->A: No visible effect on filament formation, viral
FT capsid movement capsid filling or phage DNA rotation."
FT /evidence="ECO:0000269|PubMed:31199917"
FT MUTAGEN 303
FT /note="D->A: 60% loss of ability to form filaments."
FT /evidence="ECO:0000269|PubMed:24631461"
FT MUTAGEN 305
FT /note="D->A: Almost complete loss of ability to form
FT filaments."
FT /evidence="ECO:0000269|PubMed:24631461"
FT MUTAGEN 305
FT /note="D->R: Complete loss of ability to form filaments."
FT /evidence="ECO:0000269|PubMed:24631461"
FT STRAND 6..10
FT /evidence="ECO:0007829|PDB:3R4V"
FT HELIX 11..18
FT /evidence="ECO:0007829|PDB:3R4V"
FT HELIX 19..27
FT /evidence="ECO:0007829|PDB:3R4V"
FT STRAND 28..35
FT /evidence="ECO:0007829|PDB:3R4V"
FT HELIX 40..44
FT /evidence="ECO:0007829|PDB:3R4V"
FT STRAND 45..49
FT /evidence="ECO:0007829|PDB:3R4V"
FT TURN 51..53
FT /evidence="ECO:0007829|PDB:3RB8"
FT HELIX 60..67
FT /evidence="ECO:0007829|PDB:3R4V"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:3R4V"
FT HELIX 71..76
FT /evidence="ECO:0007829|PDB:3R4V"
FT STRAND 84..94
FT /evidence="ECO:0007829|PDB:3R4V"
FT HELIX 95..108
FT /evidence="ECO:0007829|PDB:3R4V"
FT STRAND 113..119
FT /evidence="ECO:0007829|PDB:3R4V"
FT HELIX 124..144
FT /evidence="ECO:0007829|PDB:3R4V"
FT STRAND 148..154
FT /evidence="ECO:0007829|PDB:3R4V"
FT HELIX 161..178
FT /evidence="ECO:0007829|PDB:3R4V"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:3RB8"
FT HELIX 188..195
FT /evidence="ECO:0007829|PDB:3R4V"
FT HELIX 197..199
FT /evidence="ECO:0007829|PDB:3R4V"
FT STRAND 208..216
FT /evidence="ECO:0007829|PDB:3R4V"
FT HELIX 217..221
FT /evidence="ECO:0007829|PDB:3R4V"
FT STRAND 228..235
FT /evidence="ECO:0007829|PDB:3R4V"
FT HELIX 236..238
FT /evidence="ECO:0007829|PDB:3R4V"
FT STRAND 246..252
FT /evidence="ECO:0007829|PDB:3R4V"
FT STRAND 262..270
FT /evidence="ECO:0007829|PDB:3R4V"
FT HELIX 274..294
FT /evidence="ECO:0007829|PDB:3R4V"
SQ SEQUENCE 315 AA; 34621 MW; 9668891E0D2FE20F CRC64;
MPVKVCLIFA GGTGMNVATK LVDLGEAVHC FDTCDKNVVD VHRSVNVTLT KGTRGAGGNR
KVILPLVRPQ IPALMDTIPE ADFYIVCYSL GGGSGSVLGP LITGQLADRK ASFVSFVVGA
MESTDNLGND IDTMKTLEAI AVNKHLPIVV NYVPNTQGRS YESINDEIAE KIRKVVLLVN
QNHGRLDVHD VANWVRFTDK HNYLIPQVCE LHIETTRKDA ENVPEAISQL SLYLDPSKEV
AFGTPIYRKV GIMKVDDLDV TDDQIHFVIN SVGVVEIMKT ITDSKLEMTR QQSKFTQRNP
IIDADDNVDE DGMVV
