ID Q9R3C4_9RICK Unreviewed; 319 AA.
AC Q9R3C4;
DT 01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2000, sequence version 1.
DT 13-SEP-2023, entry version 101.
DE RecName: Full=Cell division protein FtsZ {ECO:0000256|RuleBase:RU000631};
DE Flags: Fragment;
GN Name=ftsZ {ECO:0000313|EMBL:CAB63867.1};
OS Wolbachia sp. Abt.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Wolbachieae; Wolbachia.
OX NCBI_TaxID=108059 {ECO:0000313|EMBL:CAB63867.1};
RN [1] {ECO:0000313|EMBL:CAB63867.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Abt {ECO:0000313|EMBL:CAB63867.1};
RX PubMed=10652077; DOI=10.1046/j.1365-294x.2000.00836.x;
RA Malloch G., Fenton B., Butcher R.D.;
RT "Molecular evidence for multiple infections of a new subgroup of Wolbachia
RT in the European raspberry beetle Byturus tomentosus.";
RL Mol. Ecol. 9:77-90(2000).
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. {ECO:0000256|ARBA:ARBA00009690,
CC ECO:0000256|RuleBase:RU000631}.
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DR EMBL; AJ250964; CAB63866.1; -; Genomic_DNA.
DR EMBL; AJ250965; CAB63867.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9R3C4; -.
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 CDD; cd02201; FtsZ_type1; 1.
DR Gene3D; 3.30.1330.20; Tubulin/FtsZ, C-terminal domain; 1.
DR Gene3D; 3.40.50.1440; Tubulin/FtsZ, GTPase domain; 1.
DR HAMAP; MF_00909; FtsZ; 1.
DR InterPro; IPR000158; Cell_div_FtsZ.
DR InterPro; IPR020805; Cell_div_FtsZ_CS.
DR InterPro; IPR045061; FtsZ/CetZ.
DR InterPro; IPR024757; FtsZ_C.
DR InterPro; IPR008280; Tub_FtsZ_C.
DR InterPro; IPR037103; Tubulin/FtsZ-like_C.
DR InterPro; IPR018316; Tubulin/FtsZ_2-layer-sand-dom.
DR InterPro; IPR036525; Tubulin/FtsZ_GTPase_sf.
DR InterPro; IPR003008; Tubulin_FtsZ_GTPase.
DR NCBIfam; TIGR00065; ftsZ; 1.
DR PANTHER; PTHR30314; CELL DIVISION PROTEIN FTSZ-RELATED; 1.
DR PANTHER; PTHR30314:SF3; MITOCHONDRIAL DIVISION PROTEIN FSZA; 1.
DR Pfam; PF12327; FtsZ_C; 1.
DR Pfam; PF00091; Tubulin; 1.
DR PRINTS; PR00423; CELLDVISFTSZ.
DR SMART; SM00864; Tubulin; 1.
DR SMART; SM00865; Tubulin_C; 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};
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..164
FT /note="Tubulin/FtsZ GTPase"
FT /evidence="ECO:0000259|SMART:SM00864"
FT DOMAIN 166..284
FT /note="Tubulin/FtsZ 2-layer sandwich"
FT /evidence="ECO:0000259|SMART:SM00865"
FT REGION 276..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..319
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:CAB63867.1"
FT NON_TER 319
FT /evidence="ECO:0000313|EMBL:CAB63867.1"
SQ SEQUENCE 319 AA; 34216 MW; 8DF60E3A9D3CAEA2 CRC64;
LCDKKIQLGI NLTKGLGAGA LPDVGKGAAE ESIDEIMEHI KDSHMLFITA GMGGGTGTGA
APVIAKAARE ARAAVKDRAP KEKKILTVGV VTKPFGFEGV RRMRTAEFGL EELQKYVDTL
IVIPNQNLFR IANEKTTFSD AFKLADNVLH IGIRGVTDLM VMPGLINLDF ADIETIMSEM
GKAMIGTGEA EGEDRAISAA EAAISNPLLD NVSMKGAQGI LINITGGGDM TLFEVDAAAN
RVREEVDENA NIIFGATFDQ AMEGRVRVSV LATGIDGRNN KSETSPISQS EDSEKEKFKW
PYSHSESTQD KTLETKPTE
//
