ID D8VNR0_9GAMM Unreviewed; 185 AA.
AC D8VNR0;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, 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:ADJ67848.1};
OS Photobacterium jeanii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=858640 {ECO:0000313|EMBL:ADJ67848.1};
RN [1] {ECO:0000313|EMBL:ADJ67848.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=R-40903 {ECO:0000313|EMBL:ADJ67848.1};
RX PubMed=20081016; DOI=10.1099/ijs.0.019968-0;
RA Chimetto L.A., Cleenwerck I., Thompson C.C., Brocchi M., Willems A.,
RA de Vos P., Thompson F.L.;
RT "Photobacterium jeanii sp. nov., isolated from corals and zoanthids.";
RL Int. J. Syst. Evol. Microbiol. 60:2843-2848(2010).
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; GU065218; ADJ67848.1; -; Genomic_DNA.
DR AlphaFoldDB; D8VNR0; -.
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:ADJ67848.1};
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..151
FT /note="Tubulin/FtsZ GTPase"
FT /evidence="ECO:0000259|SMART:SM00864"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ADJ67848.1"
FT NON_TER 185
FT /evidence="ECO:0000313|EMBL:ADJ67848.1"
SQ SEQUENCE 185 AA; 19221 MW; EC5EE53FD12EA04F CRC64;
VSTVIQIGGD ITKGLGAGAN PQVGRDSALE DRESIKAELQ GSDMIFIAAG MGGGTGTGAA
PIIAEVAKEL GILTVAVVTK PFSFEGKKRM AFAEQGIEEL SKHVDSLITI PNEKLLKVLG
RGITLLDAFA KANDVLKNAV QGIAELITRP GMINVDFADV RTVMSEMGHA MMGSGVAIGD
DRAEE
//