ID W0FIP8_9RICK Unreviewed; 159 AA.
AC W0FIP8;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 03-MAY-2023, entry version 26.
DE RecName: Full=Cell division protein FtsZ {ECO:0000256|RuleBase:RU000631};
DE Flags: Fragment;
GN Name=ftsZ {ECO:0000313|EMBL:AHF21762.1};
OS Wolbachia endosymbiont of Drosophila simulans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Wolbachieae; Wolbachia.
OX NCBI_TaxID=77038 {ECO:0000313|EMBL:AHF21762.1};
RN [1] {ECO:0000313|EMBL:AHF21762.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=WCer2 {ECO:0000313|EMBL:AHF21762.1};
RX PubMed=24376534;
RA Schneider D.I., Riegler M., Arthofer W., Mercot H., Stauffer C.,
RA Miller W.J.;
RT "Uncovering Wolbachia Diversity upon Artificial Host Transfer.";
RL PLoS ONE 8:E82402-E82402(2013).
CC -!- FUNCTION: Essential cell division protein that forms a contractile ring
CC structure (Z ring) at the future cell division site. The regulation of
CC the ring assembly controls the timing and the location of cell
CC division. One of the functions of the FtsZ ring is to recruit other
CC cell division proteins to the septum to produce a new cell wall between
CC the dividing cells. Binds GTP and shows GTPase activity.
CC {ECO:0000256|RuleBase:RU000631}.
CC -!- SUBUNIT: Homodimer. Polymerizes to form a dynamic ring structure in a
CC strictly GTP-dependent manner. {ECO:0000256|RuleBase:RU000631}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU000631}.
CC -!- SIMILARITY: Belongs to the FtsZ family.
CC {ECO:0000256|RuleBase:RU000631}.
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DR EMBL; KF717545; AHF21762.1; -; Genomic_DNA.
DR AlphaFoldDB; W0FIP8; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0000917; P:division septum assembly; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1440; Tubulin/FtsZ, GTPase domain; 1.
DR InterPro; IPR020805; Cell_div_FtsZ_CS.
DR InterPro; IPR045061; FtsZ/CetZ.
DR InterPro; IPR008280; Tub_FtsZ_C.
DR InterPro; IPR036525; Tubulin/FtsZ_GTPase_sf.
DR InterPro; IPR003008; Tubulin_FtsZ_GTPase.
DR PANTHER; PTHR30314; CELL DIVISION PROTEIN FTSZ-RELATED; 1.
DR PANTHER; PTHR30314:SF3; MITOCHONDRIAL DIVISION PROTEIN FSZA; 1.
DR Pfam; PF00091; Tubulin; 1.
DR PRINTS; PR00423; CELLDVISFTSZ.
DR SMART; SM00864; Tubulin; 1.
DR SUPFAM; SSF55307; Tubulin C-terminal domain-like; 1.
DR SUPFAM; SSF52490; Tubulin nucleotide-binding domain-like; 1.
DR PROSITE; PS01135; FTSZ_2; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|RuleBase:RU000631};
KW Cell division {ECO:0000256|RuleBase:RU000631, ECO:0000313|EMBL:AHF21762.1};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|RuleBase:RU000631};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU000631}; Septation {ECO:0000256|RuleBase:RU000631}.
FT DOMAIN 1..122
FT /note="Tubulin/FtsZ GTPase"
FT /evidence="ECO:0000259|SMART:SM00864"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AHF21762.1"
FT NON_TER 159
FT /evidence="ECO:0000313|EMBL:AHF21762.1"
SQ SEQUENCE 159 AA; 16991 MW; A6CF4F65A926A344 CRC64;
SHMLFITAGM GGGTGTGAAP VIAKAAREAR AAVKDRAPKE KKILSVGVVT KPFGFEGVRR
MRIAELGLEE LQKYVDTLIV IPNQNLFRIA NEKTTFSDAF KLADNVLHIG IRGVTDLMVM
PGLINLDFAD IETVMSEMGK AMIGTGEAEG EDRAISAAE
//
