ID A0A1D3TZR2_9ACTN Unreviewed; 220 AA. AC A0A1D3TZR2; DT 30-NOV-2016, integrated into UniProtKB/TrEMBL. DT 30-NOV-2016, sequence version 1. DT 29-SEP-2021, entry version 12. DE RecName: Full=Cell division protein FtsZ {ECO:0000256|RuleBase:RU000631}; DE Flags: Fragment; GN Name=ftsZ {ECO:0000313|EMBL:SCQ05615.1}; OS Frankia sp. AgbBO.4. OC Bacteria; Actinobacteria; Frankiales; Frankiaceae; Frankia; OC unclassified Frankia. OX NCBI_TaxID=1903991 {ECO:0000313|EMBL:SCQ05615.1}; RN [1] {ECO:0000313|EMBL:SCQ05615.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=AgbBO.4 {ECO:0000313|EMBL:SCQ05615.1}; RA Dubost A.; RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:SCQ05615.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=AgbBO.4 {ECO:0000313|EMBL:SCQ05615.1}; RA Pozzi A., Bautista-Guerrero H.H., Schwob G., Abby S.S., RA Herrera-Belaroussi A., Fernandez M.; RT "A robust phylogeny for the symbiotic Actinobacteria Frankia sp based on RT Multi-Locus Sequence Analysis."; RL Submitted (SEP-2016) 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}. 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; LT617019; SCQ05615.1; -; Genomic_DNA. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0000917; P:division septum assembly; IEA:UniProtKB-KW. DR CDD; cd02201; FtsZ_type1; 1. DR Gene3D; 3.30.1330.20; -; 1. DR Gene3D; 3.40.50.1440; -; 1. DR InterPro; IPR000158; Cell_div_FtsZ. DR InterPro; IPR020805; Cell_div_FtsZ_CS. DR InterPro; IPR024757; FtsZ_C. DR InterPro; IPR008280; Tub_FtsZ_C. DR InterPro; IPR037103; Tubulin/FtsZ-like_C. DR InterPro; IPR018316; Tubulin/FtsZ_2-layer-sand-dom. DR InterPro; IPR036525; Tubulin/FtsZ_GTPase_sf. DR InterPro; IPR003008; Tubulin_FtsZ_GTPase. DR Pfam; PF12327; FtsZ_C; 1. DR Pfam; PF00091; Tubulin; 1. DR PRINTS; PR00423; CELLDVISFTSZ. DR SMART; SM00864; Tubulin; 1. DR SMART; SM00865; Tubulin_C; 1. DR SUPFAM; SSF52490; SSF52490; 1. DR SUPFAM; SSF55307; SSF55307; 1. DR TIGRFAMs; TIGR00065; ftsZ; 1. DR PROSITE; PS01135; FTSZ_2; 1. PE 3: Inferred from homology; KW Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|RuleBase:RU000631}; KW Cell division {ECO:0000256|ARBA:ARBA00022618, KW ECO:0000256|RuleBase:RU000631}; 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..154 FT /note="Tubulin" FT /evidence="ECO:0000259|SMART:SM00864" FT DOMAIN 156..220 FT /note="Tubulin_C" FT /evidence="ECO:0000259|SMART:SM00865" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:SCQ05615.1" FT NON_TER 220 FT /evidence="ECO:0000313|EMBL:SCQ05615.1" SQ SEQUENCE 220 AA; 22667 MW; B1849EB7E1AEA204 CRC64; MSDADVKLDV GRELTRGLGA GADPEVGRQA AEDHREEIEE VLKGADMVFV TAGEGGGTGT GGAPVVANVA RSLGALTIGV VTRPFTFEGR RRATQADTGI DTLRNEVDTL IVIPNDRLLA MTDRDISVLD AFRSADQVLL SGVQGITDLI TTPGLINLDF ADVKTVMSHA GSALMGIGRA RGDDRATVAA EQAIASPLLE ASMDGAQGVL LNISGGSDLG //