ID A0A1V0JDB1_9LACO Unreviewed; 443 AA. AC A0A1V0JDB1; DT 07-JUN-2017, integrated into UniProtKB/TrEMBL. DT 07-JUN-2017, sequence version 1. DT 24-JAN-2024, entry version 27. 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; Bacillota; 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 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|HAMAP-Rule:MF_00909, ECO:0000256|RuleBase:RU000631}. CC -!- SUBUNIT: Homodimer. Polymerizes to form a dynamic ring structure in a CC strictly GTP-dependent manner. Interacts directly with several other CC division proteins. {ECO:0000256|HAMAP-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|ARBA:ARBA00009690, CC ECO:0000256|HAMAP-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 AlphaFoldDB; A0A1V0JDB1; -. DR KEGG; lamy:B1745_04070; -. 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; Tubulin/FtsZ, C-terminal domain; 1. DR Gene3D; 3.40.50.1440; Tubulin/FtsZ, GTPase domain; 1. DR HAMAP; MF_00909; FtsZ; 1. DR InterPro; IPR000158; Cell_div_FtsZ. DR InterPro; IPR020805; Cell_div_FtsZ_CS. DR InterPro; IPR045061; FtsZ/CetZ. 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 NCBIfam; TIGR00065; ftsZ; 1. DR PANTHER; PTHR30314; CELL DIVISION PROTEIN FTSZ-RELATED; 1. DR PANTHER; PTHR30314:SF3; MITOCHONDRIAL DIVISION PROTEIN FSZA; 1. 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; SSF55307; Tubulin C-terminal domain-like; 1. DR SUPFAM; SSF52490; Tubulin nucleotide-binding domain-like; 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}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00909}; KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP- KW Rule:MF_00909}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_00909}; KW Septation {ECO:0000256|ARBA:ARBA00023210, ECO:0000256|HAMAP-Rule:MF_00909}. FT DOMAIN 14..206 FT /note="Tubulin/FtsZ GTPase" FT /evidence="ECO:0000259|SMART:SM00864" FT DOMAIN 208..325 FT /note="Tubulin/FtsZ 2-layer sandwich" FT /evidence="ECO:0000259|SMART:SM00865" FT REGION 66..86 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 321..443 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 344..422 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 22..26 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00909" FT BINDING 109..111 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00909" FT BINDING 140 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00909" FT BINDING 144 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00909" FT BINDING 188 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="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 //