ID B8LF02_VIBAL Unreviewed; 171 AA.
AC B8LF02;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 03-MAY-2023, entry version 44.
DE RecName: Full=Cell division protein FtsZ {ECO:0000256|RuleBase:RU000631};
DE Flags: Fragment;
GN Name=ftsZ {ECO:0000313|EMBL:ABM66460.1};
OS Vibrio alginolyticus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=663 {ECO:0000313|EMBL:ABM66460.1};
RN [1] {ECO:0000313|EMBL:ABM66460.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=LMG 4409 {ECO:0000313|EMBL:ABM66460.1};
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; EF027344; ABM66460.1; -; Genomic_DNA.
DR AlphaFoldDB; B8LF02; -.
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:ABM66460.1};
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:ABM66460.1"
FT NON_TER 171
FT /evidence="ECO:0000313|EMBL:ABM66460.1"
SQ SEQUENCE 171 AA; 17681 MW; 7E85D261C1A89437 CRC64;
FISVNTDAQA LRKTSVGNVI QIGGDITKGL GAGANPQVGR DAALEDRDRI KDSLTGADMV
FIAAGMGGGT GTGAAPVIAE VAKELGILTV AVVTKPFSFE GKKRLAFAEQ GIDELSKHVD
SLITIPNEKL LKVLGRGVTL LEAFASANDV LKNAVQGIAE LITRPGMINV D
//
