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Database: UniProt
Entry: B8LF05_9VIBR
LinkDB: B8LF05_9VIBR
Original site: B8LF05_9VIBR 
ID   B8LF05_9VIBR            Unreviewed;       175 AA.
AC   B8LF05;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   03-MAY-2023, entry version 39.
DE   RecName: Full=Cell division protein FtsZ {ECO:0000256|RuleBase:RU000631};
DE   Flags: Fragment;
GN   Name=ftsZ {ECO:0000313|EMBL:ABM66463.1};
OS   Vibrio nigripulchritudo.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=28173 {ECO:0000313|EMBL:ABM66463.1};
RN   [1] {ECO:0000313|EMBL:ABM66463.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=LMG 3896 {ECO:0000313|EMBL:ABM66463.1};
RA   Sawabe T., Kita-Tsukamoto K.;
RT   "Evolution of Vibrio.";
RL   Submitted (SEP-2006) 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.
CC       {ECO:0000256|RuleBase:RU000631}.
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DR   EMBL; EF027347; ABM66463.1; -; Genomic_DNA.
DR   AlphaFoldDB; B8LF05; -.
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; 3.40.50.1440; Tubulin/FtsZ, GTPase domain; 1.
DR   InterPro; IPR000158; Cell_div_FtsZ.
DR   InterPro; IPR020805; Cell_div_FtsZ_CS.
DR   InterPro; IPR045061; FtsZ/CetZ.
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; 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:ABM66463.1};
KW   GTP-binding {ECO:0000256|RuleBase:RU000631};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU000631};
KW   Septation {ECO:0000256|RuleBase:RU000631}.
FT   DOMAIN          1..166
FT                   /note="Tubulin/FtsZ GTPase"
FT                   /evidence="ECO:0000259|SMART:SM00864"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ABM66463.1"
FT   NON_TER         175
FT                   /evidence="ECO:0000313|EMBL:ABM66463.1"
SQ   SEQUENCE   175 AA;  18155 MW;  262BCD77E7CDF197 CRC64;
     FISVNTDAQA LRKTSVSSVI QIGGDITKGL GAGANPQVGR EAALEDRDRL KEILTGADMV
     FIAAGMGGGT GTGAAPVIAE VAKELGILTV AVVTKPFGFE GKKRLAFAEQ GIEELSKHVD
     SLITIPNEKL LKVLGRGVTL LEAFASANDV LKNAVQGIAE LITRPGMINV DFADV
//
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