PHUZ_BPPA3
ID PHUZ_BPPA3 Reviewed; 315 AA.
AC F8SJR0;
DT 13-NOV-2019, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 1.
DT 03-AUG-2022, entry version 32.
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 Name=028 {ECO:0000312|EMBL:AEH03455.1};
OS Pseudomonas phage PhiPA3 (Pseudomonas aeruginosa phage PhiPA3).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Myoviridae.
OX NCBI_TaxID=998086;
OH NCBI_TaxID=287; Pseudomonas aeruginosa.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=21163841; DOI=10.1099/mic.0.044701-0;
RA Monson R., Foulds I., Foweraker J., Welch M., Salmond G.P.;
RT "The Pseudomonas aeruginosa generalized transducing phage phiPA3 is a new
RT member of the phiKZ-like group of 'jumbo' phages, and infects model
RT laboratory strains and clinical isolates from cystic fibrosis patients.";
RL Microbiology 157:859-867(2011).
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]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASP-190.
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).
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:31199917). The motor
CC component of a partition system which pushes phage DNA (encased by
CC protein gp105) to the center of the bacterial host cell (By
CC similarity). Also required for movement of phage capsids to the
CC vicinity of the DNA and rotation of the encased viral DNA at midcell
CC (By similarity). Forms filaments during the lytic phase, which position
CC phage DNA at the center of the bacterial host cell (PubMed:31199917).
CC Filaments have a three-stranded intertwined architecture and form a
CC spindle-like cytoskeleton within the infected cell (By similarity). Has
CC GTPase activity (By similarity). Filaments grow at the plus end and
CC depolymerize at the minus end, a process called treadmilling, and
CC switch from growing in a polar manner to catastrophic depolymerization,
CC i.e. they display dynamic instability, like tubulin (By similarity). In
CC infected host cells the filament ends close to the cell pole are
CC relatively stable, while the other end near the phage DNA is highly
CC dynamic (By similarity). Both capsid movement and DNA rotation probably
CC require treadmilling (Probable). {ECO:0000250|UniProtKB:B3FK34,
CC ECO:0000269|PubMed:31199917, 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: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. Polymerizes in a strictly GTP-dependent manner.
CC {ECO:0000250|UniProtKB:B3FK34}.
CC -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000269|PubMed:31199917}.
CC Note=In infected host cells forms a spindle-like structure emanating
CC from each cell pole. {ECO:0000269|PubMed:31199917}.
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; HQ630627; AEH03455.1; -; Genomic_DNA.
DR RefSeq; YP_009217111.1; NC_028999.1.
DR SMR; F8SJR0; -.
DR DIP; DIP-60807N; -.
DR GeneID; 26643559; -.
DR KEGG; vg:26643559; -.
DR Proteomes; UP000008388; 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 GTP-binding; Host cytoplasm; Hydrolase; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..315
FT /note="Phage tubulin-like protein"
FT /id="PRO_0000448588"
FT BINDING 13..14
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 SITE 187
FT /note="GTP hydrolysis"
FT /evidence="ECO:0000250|UniProtKB:B3FK34"
FT SITE 190
FT /note="GTP hydrolysis"
FT /evidence="ECO:0000250|UniProtKB:B3FK34"
FT MUTAGEN 190
FT /note="D->A: Complete loss of ability to position viral DNA
FT and capsids in the middle of the host cell."
FT /evidence="ECO:0000269|PubMed:31199917"
SQ SEQUENCE 315 AA; 34453 MW; A0FCFAA0A373C3E5 CRC64;
MSKVKTRVYC CGGTGMDIGV NLQWHPDLVF IDTCDKNVTA DHDLERVFLT EGTRGAGKNR
RYMLPIIRPQ VPGFLERYPA GDFNIVVFGL GGGSGSTIGP VIVSELAKAG ESVAVVCMSG
IEATEVLQND IDTLKTLEGI AAATNTPVVI NHIENVNGVP YTELDKEAIF NIHALINLTS
QKHVRLDKLD IDNWINFTKK HNQIQPQLCQ LHISNNRQEA TSVPEPIAIA SLFADASREV
AFGTPFVRTV GISDVSDPDL LADQLHFVIN SIGVASLFGS LTKQKQELEA AQVRYQQRNA
IIDIDDNRTD DGFVV
