ID A0A1D3TZR2_9ACTN Unreviewed; 220 AA. AC A0A1D3TZR2; DT 30-NOV-2016, integrated into UniProtKB/TrEMBL. DT 30-NOV-2016, sequence version 1. DT 13-NOV-2019, entry version 8. 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 RT on Multi-Locus Sequence Analysis."; RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Essential cell division protein that forms a contractile CC ring structure (Z ring) at the future cell division site. The CC regulation of the ring assembly controls the timing and the CC location of cell division. One of the functions of the FtsZ ring CC is to recruit other cell division proteins to the septum to CC produce a new cell wall between the dividing cells. Binds GTP and CC shows GTPase activity. {ECO:0000256|RuleBase:RU000631}. CC -!- SUBUNIT: Homodimer. Polymerizes to form a dynamic ring structure CC in a strictly GTP-dependent manner. CC {ECO:0000256|RuleBase:RU000631}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU000631}. CC -!- SIMILARITY: Belongs to the FtsZ family. 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: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; -; 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; 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|RuleBase:RU000631}; KW Cell division {ECO:0000256|RuleBase:RU000631, KW ECO:0000313|EMBL:SCQ05615.1}; KW GTP-binding {ECO:0000256|RuleBase:RU000631}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU000631}; KW Septation {ECO:0000256|RuleBase:RU000631}. FT DOMAIN 1 154 Tubulin. {ECO:0000259|SMART:SM00864}. FT DOMAIN 156 220 Tubulin_C. {ECO:0000259|SMART:SM00865}. FT NON_TER 1 1 {ECO:0000313|EMBL:SCQ05615.1}. FT NON_TER 220 220 {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 //