ID FTSZ_ECOLI Reviewed; 383 AA. AC P0A9A6; P06138; P77857; P78047; DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2005, sequence version 1. DT 24-JAN-2024, entry version 153. DE RecName: Full=Cell division protein FtsZ {ECO:0000255|HAMAP-Rule:MF_00909}; GN Name=ftsZ {ECO:0000255|HAMAP-Rule:MF_00909}; Synonyms=sfiB, sulB; GN OrderedLocusNames=b0095, JW0093; OS Escherichia coli (strain K12). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=K12; RX PubMed=3000876; DOI=10.1016/0378-1119(85)90179-9; RA Yi Q.-M., Lutkenhaus J.; RT "The nucleotide sequence of the essential cell-division gene ftsZ of RT Escherichia coli."; RL Gene 36:241-247(1985). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12; RX PubMed=1630901; DOI=10.1093/nar/20.13.3305; RA Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K., RA Mizobuchi K., Nakata A.; RT "Systematic sequencing of the Escherichia coli genome: analysis of the RT 0-2.4 min region."; RL Nucleic Acids Res. 20:3305-3308(1992). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., RA Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1462(1997). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION TO 158 RP AND 222. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 RT and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-39. RX PubMed=6094474; DOI=10.1128/jb.160.2.546-555.1984; RA Robinson A.C., Kenan D.J., Hatfull G.F., Sullivan N.F., Spiegelberg R., RA Donachie W.D.; RT "DNA sequence and transcriptional organization of essential cell division RT genes ftsQ and ftsA of Escherichia coli: evidence for overlapping RT transcriptional units."; RL J. Bacteriol. 160:546-555(1984). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-39. RC STRAIN=K12; RX PubMed=2995680; DOI=10.1016/0022-2836(85)90290-6; RA Yi Q.-M., Rockenbach S., Ward J.E. Jr., Lutkenhaus J.; RT "Structure and expression of the cell division genes ftsQ, ftsA and ftsZ."; RL J. Mol. Biol. 184:399-412(1985). RN [7] RP PROTEIN SEQUENCE OF 1-12. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RA Frutiger S., Hughes G.J., Pasquali C., Hochstrasser D.F.; RL Submitted (FEB-1996) to UniProtKB. RN [8] RP PROTEIN SEQUENCE OF 1-12. RC STRAIN=K12 / EMG2; RX PubMed=9298646; DOI=10.1002/elps.1150180807; RA Link A.J., Robison K., Church G.M.; RT "Comparing the predicted and observed properties of proteins encoded in the RT genome of Escherichia coli K-12."; RL Electrophoresis 18:1259-1313(1997). RN [9] RP PROTEIN SEQUENCE OF 1-5 AND 175-180, SUBUNIT, SUBCELLULAR LOCATION, AND RP MUTAGENESIS OF ARG-174. RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574; RX PubMed=14731269; DOI=10.1046/j.1365-2958.2003.03876.x; RA Koppelman C.M., Aarsman M.E., Postmus J., Pas E., Muijsers A.O., RA Scheffers D.J., Nanninga N., den Blaauwen T.; RT "R174 of Escherichia coli FtsZ is involved in membrane interaction and RT protofilament bundling, and is essential for cell division."; RL Mol. Microbiol. 51:645-657(2004). RN [10] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 377-383. RC STRAIN=K12; RX PubMed=2824434; DOI=10.1128/jb.169.12.5408-5415.1987; RA Beall B., Lutkenhaus J.; RT "Sequence analysis, transcriptional organization, and insertional RT mutagenesis of the envA gene of Escherichia coli."; RL J. Bacteriol. 169:5408-5415(1987). RN [11] RP SUBCELLULAR LOCATION, AND RING-LIKE STRUCTURE. RX PubMed=1944597; DOI=10.1038/354161a0; RA Bi E., Lutkenhaus J.; RT "FtsZ ring structure associated with division in Escherichia coli."; RL Nature 354:161-164(1991). RN [12] RP GTPASE ACTIVITY. RX PubMed=1528267; DOI=10.1038/359251a0; RA Raychaudhuri D., Park J.T.; RT "Escherichia coli cell-division gene ftsZ encodes a novel GTP-binding RT protein."; RL Nature 359:251-254(1992). RN [13] RP GTPASE ACTIVITY. RX PubMed=1528268; DOI=10.1038/359254a0; RA de Boer P., Crossley R., Rothfield L.; RT "The essential bacterial cell-division protein FtsZ is a GTPase."; RL Nature 359:254-256(1992). RN [14] RP GTP-DEPENDENT FILAMENT FORMATION. RX PubMed=8169229; DOI=10.1128/jb.176.9.2754-2758.1994; RA Mukherjee A., Lutkenhaus J.; RT "Guanine nucleotide-dependent assembly of FtsZ into filaments."; RL J. Bacteriol. 176:2754-2758(1994). RN [15] RP GTP-DEPENDENT FILAMENT FORMATION. RX PubMed=8016071; DOI=10.1073/pnas.91.13.5813; RA Bramhill D., Thompson C.M.; RT "GTP-dependent polymerization of Escherichia coli FtsZ protein to form RT tubules."; RL Proc. Natl. Acad. Sci. U.S.A. 91:5813-5817(1994). RN [16] RP MUTANTS. RX PubMed=8083192; DOI=10.1016/s0021-9258(17)31600-9; RA Raychaudhuri D., Park J.T.; RT "A point mutation converts Escherichia coli FtsZ septation GTPase to an RT ATPase."; RL J. Biol. Chem. 269:22941-22944(1994). RN [17] RP ACTIVITY REGULATION, AND INTERACTION WITH SULA. RX PubMed=8752322; DOI=10.1128/jb.178.17.5080-5085.1996; RA Huang J., Cao C., Lutkenhaus J.; RT "Interaction between FtsZ and inhibitors of cell division."; RL J. Bacteriol. 178:5080-5085(1996). RN [18] RP SUBCELLULAR LOCATION, AND INTERACTION WITH FTSA. RX PubMed=8917533; DOI=10.1073/pnas.93.23.12998; RA Ma X., Ehrhardt D.W., Margolin W.; RT "Colocalization of cell division proteins FtsZ and FtsA to cytoskeletal RT structures in living Escherichia coli cells by using green fluorescent RT protein."; RL Proc. Natl. Acad. Sci. U.S.A. 93:12998-13003(1996). RN [19] RP SUBUNIT, AND GTPASE ACTIVITY. RX PubMed=9430638; DOI=10.1093/emboj/17.2.462; RA Mukherjee A., Lutkenhaus J.; RT "Dynamic assembly of FtsZ regulated by GTP hydrolysis."; RL EMBO J. 17:462-469(1998). RN [20] RP SUBUNIT, AND DOMAIN. RC STRAIN=K12; RX PubMed=10231484; DOI=10.1046/j.1365-2958.1999.01344.x; RA Di Lallo G., Anderluzzi D., Ghelardini P., Paolozzi L.; RT "FtsZ dimerization in vivo."; RL Mol. Microbiol. 32:265-274(1999). RN [21] RP ACTIVITY REGULATION. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=11847116; DOI=10.1093/emboj/21.4.685; RA Pichoff S., Lutkenhaus J.; RT "Unique and overlapping roles for ZipA and FtsA in septal ring assembly in RT Escherichia coli."; RL EMBO J. 21:685-693(2002). RN [22] RP SUBUNIT, AND GTPASE ACTIVITY. RX PubMed=14705956; DOI=10.1021/bi035465r; RA Romberg L., Mitchison T.J.; RT "Rate-limiting guanosine 5'-triphosphate hydrolysis during nucleotide RT turnover by FtsZ, a prokaryotic tubulin homologue involved in bacterial RT cell division."; RL Biochemistry 43:282-288(2004). RN [23] RP PHYLOGENETIC STUDY. RX PubMed=14743312; DOI=10.1007/s00239-003-2523-5; RA Vaughan S., Wickstead B., Gull K., Addinall S.G.; RT "Molecular evolution of FtsZ protein sequences encoded within the genomes RT of archaea, bacteria, and eukaryota."; RL J. Mol. Evol. 58:19-29(2004). RN [24] RP REVIEW. RX PubMed=15491352; DOI=10.1111/j.1365-2958.2004.04283.x; RA Weiss D.S.; RT "Bacterial cell division and the septal ring."; RL Mol. Microbiol. 54:588-597(2004). RN [25] RP INTERACTION WITH FTSE. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=17307852; DOI=10.1128/jb.01581-06; RA Corbin B.D., Wang Y., Beuria T.K., Margolin W.; RT "Interaction between cell division proteins FtsE and FtsZ."; RL J. Bacteriol. 189:3026-3035(2007). RN [26] RP ACTIVITY REGULATION, INTERACTION WITH MREB AND CBTA, AND MUTAGENESIS OF RP 1-MET--GLU-32 AND 317-MET--ASP-383. RC STRAIN=K12 / BW25113; RX PubMed=21166897; DOI=10.1111/j.1365-2958.2010.07433.x; RA Tan Q., Awano N., Inouye M.; RT "YeeV is an Escherichia coli toxin that inhibits cell division by targeting RT the cytoskeleton proteins, FtsZ and MreB."; RL Mol. Microbiol. 79:109-118(2011). RN [27] RP INDUCTION BY HYDROXYUREA. RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574; RX PubMed=20005847; DOI=10.1016/j.molcel.2009.11.024; RA Davies B.W., Kohanski M.A., Simmons L.A., Winkler J.A., Collins J.J., RA Walker G.C.; RT "Hydroxyurea induces hydroxyl radical-mediated cell death in Escherichia RT coli."; RL Mol. Cell 36:845-860(2009). RN [28] RP ACTIVITY REGULATION, AND INTERACTION WITH CPTA. RC STRAIN=B / BL21-DE3, and K12 / BW25113; RX PubMed=22239607; DOI=10.1111/j.1574-6968.2012.02496.x; RA Masuda H., Tan Q., Awano N., Yamaguchi Y., Inouye M.; RT "A novel membrane-bound toxin for cell division, CptA (YgfX), inhibits RT polymerization of cytoskeleton proteins, FtsZ and MreB, in Escherichia RT coli."; RL FEMS Microbiol. Lett. 328:174-181(2012). RN [29] RP ACTIVITY REGULATION, AND INTERACTION WITH CBEA. RC STRAIN=K12 / BW25113; RX PubMed=22515815; DOI=10.1111/j.1365-2958.2012.08068.x; RA Masuda H., Tan Q., Awano N., Wu K.P., Inouye M.; RT "YeeU enhances the bundling of cytoskeletal polymers of MreB and FtsZ, RT antagonizing the CbtA (YeeV) toxicity in Escherichia coli."; RL Mol. Microbiol. 84:979-989(2012). RN [30] RP INTERACTION WITH CBTA; YKFI AND YPJF. RC STRAIN=K12 / BW25113; RX PubMed=28257056; DOI=10.3390/toxins9030077; RA Wen Z., Wang P., Sun C., Guo Y., Wang X.; RT "Interaction of type IV toxin/antitoxin systems in cryptic prophages of RT Escherichia coli K-12."; RL Toxins 9:0-0(2017). RN [31] RP ADP-RIBOSYLATION AT ARG-174 AND ARG-338 (MICROBIAL INFECTION). RC STRAIN=K12 / DH5-alpha; RX PubMed=30343895; DOI=10.1016/j.cell.2018.09.037; RA Ting S.Y., Bosch D.E., Mangiameli S.M., Radey M.C., Huang S., Park Y.J., RA Kelly K.A., Filip S.K., Goo Y.A., Eng J.K., Allaire M., Veesler D., RA Wiggins P.A., Peterson S.B., Mougous J.D.; RT "Bifunctional immunity proteins protect bacteria against FtsZ-targeting RT ADP-ribosylating toxins."; RL Cell 175:1380-1392(2018). RN [32] RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 367-383 IN COMPLEX WITH ZIPA. RX PubMed=10880432; DOI=10.1093/emboj/19.13.3179; RA Mosyak L., Zhang Y., Glasfeld E., Haney S., Stahl M., Seehra J., RA Somers W.S.; RT "The bacterial cell-division protein ZipA and its interaction with an FtsZ RT fragment revealed by X-ray crystallography."; RL EMBO J. 19:3179-3191(2000). 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. Polymerization CC and bundle formation is enhanced by CbeA. CC -!- ACTIVITY REGULATION: Formation of the FtsZ ring is inhibited by SulA, CC MinCD, DicB and toxins CbtA and CptA. Inhibition by toxin CbtA, SulA or CC DicB overexpression is neutralized by cytoskeleton bundling-enhancing CC protein CbeA, while inhibition by toxin CptA is neutralized by CC antitoxin CptB (PubMed:21166897, PubMed:22239607, PubMed:22515815, CC PubMed:8752322). Either FtsA or ZipA is required for Z ring formation CC and stabilization (PubMed:11847116). {ECO:0000269|PubMed:11847116, CC ECO:0000269|PubMed:21166897, ECO:0000269|PubMed:22239607, CC ECO:0000269|PubMed:22515815, ECO:0000269|PubMed:8752322}. CC -!- SUBUNIT: Homodimer. Polymerizes to form a dynamic ring structure in a CC strictly GTP-dependent manner. Polymers persist as long as GTP is CC present and disappear rapidly as soon as it is consumed. Interacts CC directly with several other division proteins, including FtsA and ZipA. CC Interacts with polymerization inhibitors SulA, CbtA and CptA. Interacts CC with MreB and polymerization bundling-enhancing factor CbeA. Interacts CC with CbtA, YkfI and YpjF (PubMed:28257056). CC {ECO:0000269|PubMed:10231484, ECO:0000269|PubMed:10880432, CC ECO:0000269|PubMed:14705956, ECO:0000269|PubMed:14731269, CC ECO:0000269|PubMed:17307852, ECO:0000269|PubMed:21166897, CC ECO:0000269|PubMed:22239607, ECO:0000269|PubMed:22515815, CC ECO:0000269|PubMed:28257056, ECO:0000269|PubMed:8016071, CC ECO:0000269|PubMed:8169229, ECO:0000269|PubMed:8752322, CC ECO:0000269|PubMed:8917533, ECO:0000269|PubMed:9430638}. CC -!- INTERACTION: CC P0A9A6; P76364: cbeA; NbExp=2; IntAct=EBI-370963, EBI-1126877; CC P0A9A6; P0A6H1: clpX; NbExp=2; IntAct=EBI-370963, EBI-547386; CC P0A9A6; P0ABH0: ftsA; NbExp=8; IntAct=EBI-370963, EBI-550562; CC P0A9A6; P0A9R7: ftsE; NbExp=2; IntAct=EBI-370963, EBI-550637; CC P0A9A6; P0A9A6: ftsZ; NbExp=11; IntAct=EBI-370963, EBI-370963; CC P0A9A6; P0A9X4: mreB; NbExp=7; IntAct=EBI-370963, EBI-371008; CC P0A9A6; P36979: rlmN; NbExp=3; IntAct=EBI-370963, EBI-559071; CC P0A9A6; P75862: zapC; NbExp=5; IntAct=EBI-370963, EBI-552519; CC P0A9A6; P36680: zapD; NbExp=3; IntAct=EBI-370963, EBI-1113728; CC P0A9A6; P77173: zipA; NbExp=5; IntAct=EBI-370963, EBI-1029213; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00909, CC ECO:0000269|PubMed:1944597, ECO:0000269|PubMed:8917533}. Note=Assembles CC in a ring-like structure at midcell at the inner surface of the CC cytoplasmic membrane. {ECO:0000269|PubMed:14731269, CC ECO:0000269|PubMed:1944597, ECO:0000269|PubMed:30343895, CC ECO:0000269|PubMed:8917533}. CC -!- INDUCTION: Repressed 1.3-fold by hydroxyurea (at protein level). CC {ECO:0000269|PubMed:20005847}. CC -!- DOMAIN: The central and C-terminal regions are required for CC dimerization. {ECO:0000269|PubMed:10231484}. CC -!- PTM: (Microbial infection) ADP-ribosylated on Arg-174 and sometimes CC Arg-338 by Tre1 when infected by S.proteamaculans strain 568. This CC prevents the formation of Z rings, inhibiting cell division, leading to CC cell elongation and disadvantaging E.coli over S.proteamaculans during CC competition for nutrients. In vitro it can be de-ADP-ribosylated by CC S.proteamaculans Tri1. {ECO:0000269|PubMed:30343895}. CC -!- SIMILARITY: Belongs to the FtsZ family. {ECO:0000255|HAMAP- CC Rule:MF_00909}. CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Becoming two - Issue 171 of CC July 2015; CC URL="https://web.expasy.org/spotlight/back_issues/171/"; 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; U00096; AAC73206.1; -; Genomic_DNA. DR EMBL; AP009048; BAB96663.2; -; Genomic_DNA. DR EMBL; X55034; CAA38872.1; -; Genomic_DNA. DR EMBL; K02668; AAA23818.1; -; Genomic_DNA. DR EMBL; M19211; AAA83848.1; -; Genomic_DNA. DR PIR; G64731; CEECZ. DR RefSeq; NP_414637.1; NC_000913.3. DR RefSeq; WP_000462776.1; NZ_STEB01000010.1. DR PDB; 1F47; X-ray; 1.95 A; A=367-383. DR PDB; 5HAW; X-ray; 1.89 A; K/L=370-379. DR PDB; 5HBU; X-ray; 2.60 A; K=370-379. DR PDB; 5HSZ; X-ray; 2.30 A; K=372-382. DR PDB; 5K58; X-ray; 2.77 A; K/L/M/N=372-379. DR PDB; 5KOA; X-ray; 2.67 A; D=370-381. DR PDB; 6LL6; X-ray; 2.50 A; A=11-316. DR PDB; 6UMK; X-ray; 1.35 A; A=10-316. DR PDB; 6UNX; X-ray; 1.40 A; A=12-316. DR PDBsum; 1F47; -. DR PDBsum; 5HAW; -. DR PDBsum; 5HBU; -. DR PDBsum; 5HSZ; -. DR PDBsum; 5K58; -. DR PDBsum; 5KOA; -. DR PDBsum; 6LL6; -. DR PDBsum; 6UMK; -. DR PDBsum; 6UNX; -. DR AlphaFoldDB; P0A9A6; -. DR SMR; P0A9A6; -. DR BioGRID; 4261887; 577. DR BioGRID; 849188; 8. DR ComplexPortal; CPX-1936; Divisome complex. DR DIP; DIP-31873N; -. DR IntAct; P0A9A6; 61. DR MINT; P0A9A6; -. DR STRING; 511145.b0095; -. DR BindingDB; P0A9A6; -. DR ChEMBL; CHEMBL3999; -. DR jPOST; P0A9A6; -. DR PaxDb; 511145-b0095; -. DR EnsemblBacteria; AAC73206; AAC73206; b0095. DR GeneID; 75202088; -. DR GeneID; 944786; -. DR KEGG; ecj:JW0093; -. DR KEGG; eco:b0095; -. DR PATRIC; fig|1411691.4.peg.2185; -. DR EchoBASE; EB0343; -. DR eggNOG; COG0206; Bacteria. DR HOGENOM; CLU_024865_0_1_6; -. DR InParanoid; P0A9A6; -. DR OMA; GNPSIGQ; -. DR OrthoDB; 9813375at2; -. DR PhylomeDB; P0A9A6; -. DR BioCyc; EcoCyc:EG10347-MONOMER; -. DR BRENDA; 3.6.5.6; 2026. DR EvolutionaryTrace; P0A9A6; -. DR PRO; PR:P0A9A6; -. DR Proteomes; UP000000318; Chromosome. DR Proteomes; UP000000625; Chromosome. DR GO; GO:0032153; C:cell division site; IDA:EcoliWiki. DR GO; GO:0005737; C:cytoplasm; IDA:EcoliWiki. DR GO; GO:1990586; C:divisome complex; NAS:ComplexPortal. DR GO; GO:0005886; C:plasma membrane; NAS:ComplexPortal. DR GO; GO:0005525; F:GTP binding; IDA:EcoliWiki. DR GO; GO:0003924; F:GTPase activity; IDA:EcoliWiki. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0051301; P:cell division; IMP:EcoliWiki. DR GO; GO:0000917; P:division septum assembly; NAS:ComplexPortal. DR GO; GO:0043093; P:FtsZ-dependent cytokinesis; NAS:ComplexPortal. DR GO; GO:0051258; P:protein polymerization; IDA:EcoliWiki. DR CDD; cd02201; FtsZ_type1; 1. DR DisProt; DP02201; -. 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. DR SWISS-2DPAGE; P0A9A6; -. PE 1: Evidence at protein level; KW 3D-structure; ADP-ribosylation; Cell cycle; Cell division; Cytoplasm; KW Direct protein sequencing; GTP-binding; Nucleotide-binding; KW Reference proteome; Septation. FT CHAIN 1..383 FT /note="Cell division protein FtsZ" FT /id="PRO_0000114349" FT BINDING 20..24 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909" FT BINDING 107..109 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909" FT BINDING 138 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909" FT BINDING 142 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909" FT BINDING 186 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00909" FT MOD_RES 174 FT /note="(Microbial infection) ADP-ribosylarginine; by FT S.proteamaculans Tre1" FT /evidence="ECO:0000269|PubMed:30343895" FT MOD_RES 338 FT /note="(Microbial infection) ADP-ribosylarginine; by FT S.proteamaculans Tre1" FT /evidence="ECO:0000269|PubMed:30343895" FT MUTAGEN 1..32 FT /note="Missing: No interaction with MreB or CbtA (YeeV)." FT /evidence="ECO:0000269|PubMed:21166897" FT MUTAGEN 33..49 FT /note="Missing: No interaction with CtpA." FT MUTAGEN 105 FT /note="G->S: In FtsZ-84; loss of GTPase-activity and FT conversion to an ATPase." FT /evidence="ECO:0000269|PubMed:8083192" FT MUTAGEN 108 FT /note="T->A: In FtsZ-Z3; lethal; greatly reduced GTP FT binding." FT MUTAGEN 174 FT /note="R->D: Protein has decreased affinity for the cell FT inner membrane, polymerizes into filaments less efficiently FT than wild-type, the protofilaments no longer form bundles, FT still forms rings." FT /evidence="ECO:0000269|PubMed:14731269" FT MUTAGEN 317..383 FT /note="Missing: No interaction with MreB or CbtA (YeeV)." FT /evidence="ECO:0000269|PubMed:21166897" FT CONFLICT 32..39 FT /note="ERIEGVEF -> DALKVLNS (in Ref. 5; AAA23818)" FT /evidence="ECO:0000305" FT CONFLICT 158 FT /note="D -> N (in Ref. 1; CAA38872)" FT /evidence="ECO:0000305" FT CONFLICT 222 FT /note="Y -> H (in Ref. 1; CAA38872)" FT /evidence="ECO:0000305" FT STRAND 13..18 FT /evidence="ECO:0007829|PDB:6UMK" FT HELIX 19..32 FT /evidence="ECO:0007829|PDB:6UMK" FT STRAND 38..44 FT /evidence="ECO:0007829|PDB:6UMK" FT HELIX 46..51 FT /evidence="ECO:0007829|PDB:6UMK" FT STRAND 55..59 FT /evidence="ECO:0007829|PDB:6UMK" FT HELIX 70..72 FT /evidence="ECO:0007829|PDB:6UMK" FT HELIX 74..83 FT /evidence="ECO:0007829|PDB:6UMK" FT HELIX 85..92 FT /evidence="ECO:0007829|PDB:6UMK" FT STRAND 96..103 FT /evidence="ECO:0007829|PDB:6UMK" FT HELIX 108..122 FT /evidence="ECO:0007829|PDB:6UMK" FT STRAND 126..133 FT /evidence="ECO:0007829|PDB:6UMK" FT HELIX 136..138 FT /evidence="ECO:0007829|PDB:6UMK" FT HELIX 140..154 FT /evidence="ECO:0007829|PDB:6UMK" FT STRAND 158..164 FT /evidence="ECO:0007829|PDB:6UMK" FT HELIX 165..168 FT /evidence="ECO:0007829|PDB:6UMK" FT HELIX 178..201 FT /evidence="ECO:0007829|PDB:6UMK" FT HELIX 210..217 FT /evidence="ECO:0007829|PDB:6UMK" FT STRAND 221..230 FT /evidence="ECO:0007829|PDB:6UMK" FT HELIX 235..244 FT /evidence="ECO:0007829|PDB:6UMK" FT TURN 247..251 FT /evidence="ECO:0007829|PDB:6UMK" FT HELIX 254..256 FT /evidence="ECO:0007829|PDB:6UMK" FT STRAND 258..266 FT /evidence="ECO:0007829|PDB:6UMK" FT HELIX 272..285 FT /evidence="ECO:0007829|PDB:6UMK" FT STRAND 288..298 FT /evidence="ECO:0007829|PDB:6UMK" FT STRAND 306..315 FT /evidence="ECO:0007829|PDB:6UMK" FT HELIX 374..382 FT /evidence="ECO:0007829|PDB:1F47" SQ SEQUENCE 383 AA; 40324 MW; B3A53340367DBBA0 CRC64; MFEPMELTND AVIKVIGVGG GGGNAVEHMV RERIEGVEFF AVNTDAQALR KTAVGQTIQI GSGITKGLGA GANPEVGRNA ADEDRDALRA ALEGADMVFI AAGMGGGTGT GAAPVVAEVA KDLGILTVAV VTKPFNFEGK KRMAFAEQGI TELSKHVDSL ITIPNDKLLK VLGRGISLLD AFGAANDVLK GAVQGIAELI TRPGLMNVDF ADVRTVMSEM GYAMMGSGVA SGEDRAEEAA EMAISSPLLE DIDLSGARGV LVNITAGFDL RLDEFETVGN TIRAFASDNA TVVIGTSLDP DMNDELRVTV VATGIGMDKR PEITLVTNKQ VQQPVMDRYQ QHGMAPLTQE QKPVAKVVND NAPQTAKEPD YLDIPAFLRK QAD //