PHUZ_BPDPK
ID PHUZ_BPDPK Reviewed; 327 AA.
AC Q8SDC3;
DT 13-NOV-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Phage tubulin-like protein {ECO:0000250|UniProtKB:B3FK34};
DE Short=PhuZ {ECO:0000250|UniProtKB:B3FK34};
DE EC=3.6.5.- {ECO:0000250|UniProtKB:B3FK34};
DE AltName: Full=Phage tubulin/FtsZ {ECO:0000250|UniProtKB:B3FK34};
DE AltName: Full=Tubulin-like protein TubZ {ECO:0000250|UniProtKB:B3FK34};
GN OrderedLocusNames=PHIKZ039;
OS Pseudomonas phage phiKZ.
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Myoviridae; Phikzvirus.
OX NCBI_TaxID=169683;
OH NCBI_TaxID=287; Pseudomonas aeruginosa.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11916376; DOI=10.1006/jmbi.2001.5396;
RA Mesyanzhinov V.V., Robben J., Grymonprez B., Kostyuchenko V.A.,
RA Bourkaltseva M.V., Sykilinda N.N., Krylov V.N., Volckaert G.;
RT "The genome of bacteriophage phiKZ of Pseudomonas aeruginosa.";
RL J. Mol. Biol. 317:1-19(2002).
RN [2]
RP FUNCTION, AND SUBCELLULAR LOCATION.
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 [3] {ECO:0007744|PDB:3ZBP, ECO:0007744|PDB:3ZBQ}
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS), SUBUNIT, AND FUNCTION.
RX PubMed=23528827; DOI=10.1016/j.jmb.2013.03.019;
RA Aylett C.H., Izore T., Amos L.A., Lowe J.;
RT "Structure of the tubulin/FtsZ-like protein TubZ from Pseudomonas
RT bacteriophage KZ.";
RL J. Mol. Biol. 425:2164-2173(2013).
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. The motor component of a partition
CC system which pushes phage DNA (encased by protein gp105) to the center
CC of the bacterial host cell (PubMed:28813669). Also required for
CC movement of phage capsids to the vicinity of the viral DNA and rotation
CC of the encased viral DNA at midcell (PubMed:28813669). Forms filaments
CC during the lytic phase, which position phage DNA at the center of the
CC bacterial host cell (PubMed:28813669). Filaments have a three-stranded
CC intertwined architecture and form a spindle-like cytoskeleton within
CC the infected cell (PubMed:23528827). Has GTPase activity (Probable).
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 (By similarity). In infected host cells the
CC filament ends close to the cell pole are relatively stable, while the
CC other end near the phage DNA is highly dynamic. Both capsid movement
CC and DNA rotation probably require treadmilling (By similarity).
CC {ECO:0000250|UniProtKB:B3FK34, ECO:0000269|PubMed:23528827,
CC ECO:0000269|PubMed:28813669, ECO:0000305|PubMed:23528827}.
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:0000250|UniProtKB:B3FK34};
CC -!- ACTIVITY REGULATION: The non-hydrolyzable GTP analog GMPCPP stabilizes
CC filaments, which never disassemble. {ECO:0000250|UniProtKB:B3FK34}.
CC -!- SUBUNIT: Homomultimer (PubMed:23528827). Polymerizes in a strictly GTP-
CC dependent manner (By similarity). {ECO:0000250|UniProtKB:B3FK34,
CC ECO:0000269|PubMed:23528827}.
CC -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000250|UniProtKB:B3FK34}.
CC Note=In infected host cells forms a spindle-like structure emanating
CC from each cell pole. {ECO:0000250|UniProtKB:B3FK34}.
CC -!- DOMAIN: Consists of two domains: a nucleotide-binding N-terminus that
CC hydrolyzes GTP and a C-terminus domain necessary for polymerization.
CC The domains are bridged by a long, central helix. Interactions between
CC the C-terminus and the following monomer drive polymerization.
CC {ECO:0000250|UniProtKB:B3FK34}.
CC -!- SIMILARITY: Belongs to the FtsZ family. PhuZ subfamily. {ECO:0000305}.
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DR EMBL; AF399011; AAL82940.1; -; Genomic_DNA.
DR RefSeq; NP_803605.1; NC_004629.1.
DR PDB; 3ZBP; X-ray; 2.00 A; A=1-327.
DR PDB; 3ZBQ; X-ray; 1.70 A; A=1-327.
DR PDBsum; 3ZBP; -.
DR PDBsum; 3ZBQ; -.
DR SMR; Q8SDC3; -.
DR GeneID; 1258293; -.
DR KEGG; vg:1258293; -.
DR Proteomes; UP000002098; 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 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..327
FT /note="Phage tubulin-like protein"
FT /id="PRO_0000448589"
FT REGION 303..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 14..15
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q8KNP3"
FT BINDING 107..109
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q8KNP3"
FT SITE 201
FT /note="GTP hydrolysis"
FT /evidence="ECO:0000250|UniProtKB:B3FK34"
FT SITE 204
FT /note="GTP hydrolysis"
FT /evidence="ECO:0000250|UniProtKB:B3FK34"
FT STRAND 6..12
FT /evidence="ECO:0007829|PDB:3ZBQ"
FT HELIX 13..23
FT /evidence="ECO:0007829|PDB:3ZBQ"
FT STRAND 28..37
FT /evidence="ECO:0007829|PDB:3ZBQ"
FT TURN 46..48
FT /evidence="ECO:0007829|PDB:3ZBQ"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:3ZBQ"
FT HELIX 62..69
FT /evidence="ECO:0007829|PDB:3ZBP"
FT HELIX 74..81
FT /evidence="ECO:0007829|PDB:3ZBQ"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:3ZBQ"
FT HELIX 85..91
FT /evidence="ECO:0007829|PDB:3ZBQ"
FT STRAND 96..108
FT /evidence="ECO:0007829|PDB:3ZBQ"
FT HELIX 109..122
FT /evidence="ECO:0007829|PDB:3ZBQ"
FT STRAND 127..133
FT /evidence="ECO:0007829|PDB:3ZBQ"
FT HELIX 138..158
FT /evidence="ECO:0007829|PDB:3ZBQ"
FT STRAND 163..168
FT /evidence="ECO:0007829|PDB:3ZBQ"
FT HELIX 175..192
FT /evidence="ECO:0007829|PDB:3ZBQ"
FT HELIX 202..209
FT /evidence="ECO:0007829|PDB:3ZBQ"
FT HELIX 211..213
FT /evidence="ECO:0007829|PDB:3ZBQ"
FT STRAND 222..229
FT /evidence="ECO:0007829|PDB:3ZBQ"
FT HELIX 230..234
FT /evidence="ECO:0007829|PDB:3ZBQ"
FT STRAND 236..248
FT /evidence="ECO:0007829|PDB:3ZBQ"
FT HELIX 249..251
FT /evidence="ECO:0007829|PDB:3ZBQ"
FT STRAND 259..265
FT /evidence="ECO:0007829|PDB:3ZBQ"
FT TURN 268..270
FT /evidence="ECO:0007829|PDB:3ZBQ"
FT STRAND 274..282
FT /evidence="ECO:0007829|PDB:3ZBQ"
FT HELIX 284..304
FT /evidence="ECO:0007829|PDB:3ZBQ"
SQ SEQUENCE 327 AA; 36425 MW; 407F207D5A743276 CRC64;
MMSKVKTRIY FCGGAGFRIG ELFHGYHEDV CYIDTSVQNK HKHNTDDNTI IIEADTKLAD
QTARKRAIGM GKDRKAAAEL ISAHIPAIAH HFPAGDTNIV VYSMGGASGS TIGPSLVSHL
QQQGEVVVSV VIGSYDSDIS LRNSSGSLKT FEGVSSVSKV PMIINYHENV EGIPQSMVNQ
NILEVLNALV ILFNQEHQSL DLMDITNWAH FHKHHDVPVQ TVQLHVCFDR QEAQAILDPI
SIASLYTDPD RDVSISTVLT RTTGYADPEK YDFDQMHFVI NGLSIEDIRK RLEERREMMN
RAKANMRKRQ STLDVDDQAT SSGLVFD
