ID V5UWE1_9GAMM Unreviewed; 182 AA.
AC V5UWE1;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 03-MAY-2023, entry version 26.
DE RecName: Full=Cell division protein FtsZ {ECO:0000256|RuleBase:RU000631};
DE Flags: Fragment;
GN Name=ftsZ {ECO:0000313|EMBL:AHB81829.1};
OS Aliivibrio finisterrensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Aliivibrio.
OX NCBI_TaxID=511998 {ECO:0000313|EMBL:AHB81829.1};
RN [1] {ECO:0000313|EMBL:AHB81829.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CAIM 1821 {ECO:0000313|EMBL:AHB81829.1};
RA Gomez-Gil B., Sawabe T.;
RT "MLSA update of the Vibrionaceae.";
RL Submitted (SEP-2013) 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; KF666640; AHB81829.1; -; Genomic_DNA.
DR AlphaFoldDB; V5UWE1; -.
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; IPR008280; Tub_FtsZ_C.
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; 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, ECO:0000313|EMBL:AHB81829.1};
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..140
FT /note="Tubulin/FtsZ GTPase"
FT /evidence="ECO:0000259|SMART:SM00864"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AHB81829.1"
FT NON_TER 182
FT /evidence="ECO:0000313|EMBL:AHB81829.1"
SQ SEQUENCE 182 AA; 19027 MW; 66520EA216CEC9BB CRC64;
TKGFCWGANP VVGRHDLVGD RDRIKDSLTG ADMVFIAAGM GGGTGTGAAP VIAEVAKELG
ILTVAVVTKP FSFEGKKRLA FAEQGIDELS KHVDSLITIP NEKLLKVLGR GVTLLEAFAS
ANDVLKNAVQ GIAELITRPG MINVDFADVR TVMSEMGHAM MGSGIAKGED RAEEAAEMAI
SS
//
