ID A0A1V0JDB1_9LACO Unreviewed; 443 AA. AC A0A1V0JDB1; DT 07-JUN-2017, integrated into UniProtKB/TrEMBL. DT 07-JUN-2017, sequence version 1. DT 31-JUL-2019, entry version 12. DE RecName: Full=Cell division protein FtsZ {ECO:0000256|HAMAP-Rule:MF_00909, ECO:0000256|RuleBase:RU000631}; GN Name=ftsZ {ECO:0000256|HAMAP-Rule:MF_00909}; GN ORFNames=B1745_04070 {ECO:0000313|EMBL:ARD06860.1}; OS Lactobacillus amylolyticus. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=83683 {ECO:0000313|EMBL:ARD06860.1, ECO:0000313|Proteomes:UP000191936}; RN [1] {ECO:0000313|EMBL:ARD06860.1, ECO:0000313|Proteomes:UP000191936} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=L6 {ECO:0000313|EMBL:ARD06860.1, RC ECO:0000313|Proteomes:UP000191936}; RA Fei Y.; RT "Complete genome sequence of Lactobacillus amylolyticus isolated from RT naturally fermented tofu whey."; RL Submitted (MAR-2017) 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|HAMAP-Rule:MF_00909, CC ECO:0000256|RuleBase:RU000631}. CC -!- SUBUNIT: Homodimer. Polymerizes to form a dynamic ring structure CC in a strictly GTP-dependent manner. Interacts directly with CC several other division proteins. {ECO:0000256|HAMAP- CC Rule:MF_00909}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00909}. CC Note=Assembles at midcell at the inner surface of the cytoplasmic CC membrane. {ECO:0000256|HAMAP-Rule:MF_00909}. CC -!- SIMILARITY: Belongs to the FtsZ family. {ECO:0000256|HAMAP- CC Rule:MF_00909, 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; CP020457; ARD06860.1; -; Genomic_DNA. DR KEGG; lamy:B1745_04070; -. DR KO; K03531; -. DR Proteomes; UP000191936; Chromosome. DR GO; GO:0032153; C:cell division site; IEA:UniProtKB-UniRule. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule. DR GO; GO:0000917; P:division septum assembly; IEA:UniProtKB-KW. DR GO; GO:0043093; P:FtsZ-dependent cytokinesis; IEA:UniProtKB-UniRule. DR GO; GO:0051258; P:protein polymerization; IEA:UniProtKB-UniRule. DR CDD; cd02201; FtsZ_type1; 1. DR Gene3D; 3.30.1330.20; -; 1. DR Gene3D; 3.40.50.1440; -; 1. DR HAMAP; MF_00909; FtsZ; 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; IPR037103; Tubulin/FtsZ_C_sf. 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; PS01134; FTSZ_1; 1. DR PROSITE; PS01135; FTSZ_2; 1. PE 3: Inferred from homology; KW Cell cycle {ECO:0000256|HAMAP-Rule:MF_00909, KW ECO:0000256|RuleBase:RU000631}; KW Cell division {ECO:0000256|HAMAP-Rule:MF_00909, KW ECO:0000256|RuleBase:RU000631, ECO:0000313|EMBL:ARD06860.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000191936}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00909}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00909, KW ECO:0000256|RuleBase:RU000631}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00909, KW ECO:0000256|RuleBase:RU000631}; KW Septation {ECO:0000256|HAMAP-Rule:MF_00909, KW ECO:0000256|RuleBase:RU000631}. FT DOMAIN 14 206 Tubulin. {ECO:0000259|SMART:SM00864}. FT DOMAIN 208 325 Tubulin_C. {ECO:0000259|SMART:SM00865}. FT NP_BIND 22 26 GTP. {ECO:0000256|HAMAP-Rule:MF_00909}. FT NP_BIND 109 111 GTP. {ECO:0000256|HAMAP-Rule:MF_00909}. FT REGION 66 86 Disordered. {ECO:0000256|SAM:MobiDB- FT lite}. FT REGION 321 443 Disordered. {ECO:0000256|SAM:MobiDB- FT lite}. FT COMPBIAS 344 422 Polar. {ECO:0000256|SAM:MobiDB-lite}. FT BINDING 140 140 GTP. {ECO:0000256|HAMAP-Rule:MF_00909}. FT BINDING 144 144 GTP. {ECO:0000256|HAMAP-Rule:MF_00909}. FT BINDING 188 188 GTP. {ECO:0000256|HAMAP-Rule:MF_00909}. SQ SEQUENCE 443 AA; 46895 MW; EC1A7972267F22F1 CRC64; MDFTFDSDDN KNAVIKVIGV GGAGGNAVNR MIDDGVQGVS FIAANTDVQA LNSNKAEEKI QLGPKLTRGL GAGSHPEVGQ KAAEESEQTI EDALKGADMI FITAGMGGGT GTGAAPVVAK IARETGALTV GVVTRPFSFE GPKRSRNAAE GITQLKQYVD TLVIIANNRL LEMVDKKTPM MDAFKEADNV LKQGVQGISD LITSTDYVNL DFADVKTVME NQGAALMGIG RASGENRTVE ATKLAISSPL LEVSIDGAKQ VLLNITGGPD LTLFEAQDAS EIVSKAAGDD VNIIFGTSIN PNLGDEVVVT VIATGIDSAT EEAASKQLPG RSHQIKSQPK KTEEAQATKP TIGQTVQPTV NQSTNNTTAK HESMVDPTSV WGLNNDDQTT RRTTPTNTNA SQDDSFDYFS SEDQNSISQI ETSAQDDDDD NNDIPFFKHR GEN //