FTSZ_ECOLI
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 03-AUG-2022, entry version 146.
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; Proteobacteria; 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 0-
RT 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/";
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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 SWISS-2DPAGE; P0A9A6; -.
DR jPOST; P0A9A6; -.
DR PaxDb; P0A9A6; -.
DR PRIDE; P0A9A6; -.
DR EnsemblBacteria; AAC73206; AAC73206; b0095.
DR EnsemblBacteria; BAB96663; BAB96663; BAB96663.
DR GeneID; 66671615; -.
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 PhylomeDB; P0A9A6; -.
DR BioCyc; EcoCyc:EG10347-MON; -.
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; IC:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IC: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; IC:ComplexPortal.
DR GO; GO:0043093; P:FtsZ-dependent cytokinesis; IC: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; -; 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; 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 PANTHER; PTHR30314; PTHR30314; 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; 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 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
