ID C9WMC2_VIBHA Unreviewed; 232 AA.
AC C9WMC2;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 13-SEP-2023, entry version 50.
DE RecName: Full=Cell division protein FtsZ {ECO:0000256|RuleBase:RU000631};
DE Flags: Fragment;
GN Name=ftsZ {ECO:0000313|EMBL:ACX35582.1};
OS Vibrio harveyi (Beneckea harveyi).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=669 {ECO:0000313|EMBL:ACX35582.1};
RN [1] {ECO:0000313|EMBL:ACX35582.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=T4 {ECO:0000313|EMBL:ACX35582.1};
RX PubMed=19486404; DOI=10.1111/j.1365-2672.2009.04304.x;
RA Sun K., Hu Y.H., Zhang X.H., Bai F.F., Sun L.;
RT "Identification of vhhP2, a novel genetic marker of Vibrio harveyi, and its
RT application in the quick detection of V. harveyi from animal specimens and
RT environmental samples.";
RL J. Appl. Microbiol. 107:1251-1257(2009).
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; FJ752689; ACX35582.1; -; Genomic_DNA.
DR AlphaFoldDB; C9WMC2; -.
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 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; 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 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:ACX35582.1};
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 2..180
FT /note="Tubulin/FtsZ GTPase"
FT /evidence="ECO:0000259|SMART:SM00864"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ACX35582.1"
FT NON_TER 232
FT /evidence="ECO:0000313|EMBL:ACX35582.1"
SQ SEQUENCE 232 AA; 24184 MW; 92305C0F75B56DDF CRC64;
VVEHMVRESI EGVEFISVNT DAQALRKTSV GNVIQIGGDI TKGLGAGANP QVGREAALED
RDRIKDSLTG ADMVFIAAGM GGGTGTGAAP VIAEVAKELG ILTVAVVTKP FSFEGKKRLA
FAEQGIDELS KHVDSLITIP NEKLLKVLGR GVTLLEAFAS ANDVLKNAVQ GIAELITRPG
MINVDFADVR TVMSEMGHAM MGSGIAKGED RAEEAAEMAI SSPLLEDIDL AG
//
