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Database: UniProt
Entry: D4NZH5_9RICK
LinkDB: D4NZH5_9RICK
Original site: D4NZH5_9RICK 
ID   D4NZH5_9RICK            Unreviewed;       347 AA.
AC   D4NZH5;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   13-SEP-2023, entry version 43.
DE   RecName: Full=Cell division protein FtsZ {ECO:0000256|RuleBase:RU000631};
DE   Flags: Fragment;
GN   Name=ftsZ {ECO:0000313|EMBL:ADD65356.1};
OS   Wolbachia endosymbiont of Diaphorina citri.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Wolbachieae; Wolbachia.
OX   NCBI_TaxID=116598 {ECO:0000313|EMBL:ADD65356.1};
RN   [1] {ECO:0000313|EMBL:ADD65356.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Tian C.S.H., Wang K.Z., Yin P.Y.;
RT   "Detection and phylogenetic analysis of Wolbachia in Diaphorina citri.";
RL   Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases.
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; GU480077; ADD65356.1; -; Genomic_DNA.
DR   AlphaFoldDB; D4NZH5; -.
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; PS01134; FTSZ_1; 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:ADD65356.1};
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..177
FT                   /note="Tubulin/FtsZ GTPase"
FT                   /evidence="ECO:0000259|SMART:SM00864"
FT   DOMAIN          179..297
FT                   /note="Tubulin/FtsZ 2-layer sandwich"
FT                   /evidence="ECO:0000259|SMART:SM00865"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ADD65356.1"
FT   NON_TER         347
FT                   /evidence="ECO:0000313|EMBL:ADD65356.1"
SQ   SEQUENCE   347 AA;  37147 MW;  272174EF12B65FD4 CRC64;
     VVANTDAQAL EKSLCDKKIQ LGINLTKGLG AGALPDVGKG AAEESIDEIM EHIKDSHMLF
     ITAGMGGGTG TGAAPVIAKA ARETRAVVKD KGAKEKKILT VGVVTKPFGF EGVRRMRIAE
     LGLEELQKYV DTLIVIPNQN LFRIANEKTT FADAFQLADN VLHIGIRGVT DLMIMPGLIN
     LDFADIETVM SEMGKAMIGT GEAEGEDRAI SAAEAAISNP LLDNVSMKGA QGILINITGG
     GDMTLFEVDA AANRVREEVD ENANIIFGAT FDQAMEGRVR VSVLATGIDS CNDNSSVNQN
     KIPAEEKNFK WPYNQVPISE TKEYASTGQT NERVKWGGNV YDIPAYL
//
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