ID   FTSZ_WOLPI              Reviewed;         315 AA.
AC   P50907;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Cell division protein FtsZ {ECO:0000255|HAMAP-Rule:MF_00909};
DE   Flags: Fragment;
GN   Name=ftsZ {ECO:0000255|HAMAP-Rule:MF_00909};
OS   Wolbachia pipientis.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Wolbachieae; Wolbachia.
OX   NCBI_TaxID=955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Group B;
RX   PubMed=7644549; DOI=10.1098/rspb.1995.0117;
RA   Werren J.H., Zhang W., Guo L.R.;
RT   "Evolution and phylogeny of Wolbachia: reproductive parasites of
RT   arthropods.";
RL   Proc. R. Soc. B 261:55-63(1995).
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:0000255|HAMAP-Rule:MF_00909}.
CC   -!- SUBUNIT: Homodimer. Polymerizes to form a dynamic ring structure in a
CC       strictly GTP-dependent manner. Interacts directly with several other
CC       division proteins. {ECO:0000255|HAMAP-Rule:MF_00909}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00909}.
CC       Note=Assembles at midcell at the inner surface of the cytoplasmic
CC       membrane. {ECO:0000255|HAMAP-Rule:MF_00909}.
CC   -!- SIMILARITY: Belongs to the FtsZ family. {ECO:0000255|HAMAP-
CC       Rule:MF_00909}.
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DR   EMBL; U28209; AAA70116.1; -; Genomic_DNA.
DR   AlphaFoldDB; P50907; -.
DR   SMR; P50907; -.
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; -; 1.
DR   Gene3D; 3.40.50.1440; -; 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   PANTHER; PTHR30314; PTHR30314; 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; SSF52490; SSF52490; 1.
DR   SUPFAM; SSF55307; SSF55307; 1.
DR   TIGRFAMs; TIGR00065; ftsZ; 1.
DR   PROSITE; PS01135; FTSZ_2; 1.
PE   3: Inferred from homology;
KW   Cell cycle; Cell division; Cytoplasm; GTP-binding; Nucleotide-binding;
KW   Septation.
FT   CHAIN           <1..>315
FT                   /note="Cell division protein FtsZ"
FT                   /id="PRO_0000114394"
FT   BINDING         55..57
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT   BINDING         98
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT   BINDING         102
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT   BINDING         146
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00909"
FT   NON_TER         1
FT   NON_TER         315
SQ   SEQUENCE   315 AA;  33713 MW;  F8948D463474B0F3 CRC64;
     LCDKKIQLGI NLTKGLGAGA LPDVGKGAAE ESIDEIMEHI KDSHMLFITA GMGGGTGTGA
     APVIAKAARE ARAVVKDKGA KEKKILTVGV VTKPFGFEGV RRMRIAELGL EELQKYVDTL
     IVIPNQNLFR IANEKTTFAD AFQLADNVLH IGIRGVTDLM IMPGLINLDF ADIETVMSEM
     GKAMIGTGEA EGEDRAISAA EAAISNPLLD NVSMKGAQGI LINITGGGDM TLFEVDSAAN
     RVREEVDENA NIIFGATFDQ AMEGRVRVSV LATGIDSCND NSSVNQNKIP AEEKNFKWPY
     NQIPILETKE YASTE