GenomeNet

Database: UniProt
Entry: D8VNR0_9GAMM
LinkDB: D8VNR0_9GAMM
Original site: D8VNR0_9GAMM 
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
//
DBGET integrated database retrieval system