ID   FTSZ_BACSU              Reviewed;         382 AA.
AC   P17865;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 3.
DT   02-SEP-2026, entry version 186.
DE   RecName: Full=Cell division protein FtsZ {ECO:0000255|HAMAP-Rule:MF_00909};
GN   Name=ftsZ {ECO:0000255|HAMAP-Rule:MF_00909};
GN   OrderedLocusNames=BSU15290;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae;
OC   Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3139638; DOI=10.1128/jb.170.10.4855-4864.1988;
RA   Beall B., Lowe M., Lutkenhaus J.;
RT   "Cloning and characterization of Bacillus subtilis homologs of Escherichia
RT   coli cell division genes ftsZ and ftsA.";
RL   J. Bacteriol. 170:4855-4864(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   SEQUENCE REVISION TO 345-346.
RX   PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA   Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA   Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT   "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT   168 reference genome a decade later.";
RL   Microbiology 155:1758-1775(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 371-382.
RX   PubMed=2108961; DOI=10.1016/s0021-9258(19)39225-7;
RA   Wu X.-C., Nathoo S., Pang A.S.-H., Carne T., Wang S.-L.;
RT   "Cloning, genetic organization, and characterization of a structural gene
RT   encoding bacillopeptidase F from Bacillus subtilis.";
RL   J. Biol. Chem. 265:6845-6850(1990).
RN   [5]
RP   FUNCTION.
RC   STRAIN=JDB401;
RX   PubMed=15317782; DOI=10.1128/jb.186.17.5775-5781.2004;
RA   Anderson D.E., Gueiros-Filho F.J., Erickson H.P.;
RT   "Assembly dynamics of FtsZ rings in Bacillus subtilis and Escherichia coli
RT   and effects of FtsZ-regulating proteins.";
RL   J. Bacteriol. 186:5775-5781(2004).
RN   [6]
RP   FUNCTION, AND INTERACTION WITH FTSA.
RC   STRAIN=168;
RX   PubMed=16159787; DOI=10.1128/jb.187.18.6536-6544.2005;
RA   Jensen S.O., Thompson L.S., Harry E.J.;
RT   "Cell division in Bacillus subtilis: FtsZ and FtsA association is Z-ring
RT   independent, and FtsA is required for efficient midcell Z-Ring assembly.";
RL   J. Bacteriol. 187:6536-6544(2005).
RN   [7]
RP   ACTIVITY REGULATION, AND INTERACTION WITH MCIZ.
RC   STRAIN=168 / PY79;
RX   PubMed=18284588; DOI=10.1111/j.1365-2958.2008.06173.x;
RA   Handler A.A., Lim J.E., Losick R.;
RT   "Peptide inhibitor of cytokinesis during sporulation in Bacillus
RT   subtilis.";
RL   Mol. Microbiol. 68:588-599(2008).
RN   [8]
RP   INTERACTION WITH PHI29 DNA REPLICATION PROTEIN 1.
RX   PubMed=23836667; DOI=10.1073/pnas.1311524110;
RA   Ballesteros-Plaza D., Holguera I., Scheffers D.J., Salas M.,
RA   Munoz-Espin D.;
RT   "Phage 29 phi protein p1 promotes replication by associating with the FtsZ
RT   ring of the divisome in Bacillus subtilis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:12313-12318(2013).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX   PubMed=17900614; DOI=10.1016/j.jmb.2007.08.056;
RA   Oliva M.A., Trambaiolo D., Lowe J.;
RT   "Structural insights into the conformational variability of FtsZ.";
RL   J. Mol. Biol. 373:1229-1242(2007).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
RX   PubMed=18801997; DOI=10.1126/science.1159961;
RA   Haydon D.J., Stokes N.R., Ure R., Galbraith G., Bennett J.M., Brown D.R.,
RA   Baker P.J., Barynin V.V., Rice D.W., Sedelnikova S.E., Heal J.R.,
RA   Sheridan J.M., Aiwale S.T., Chauhan P.K., Srivastava A., Taneja A.,
RA   Collins I., Errington J., Czaplewski L.G.;
RT   "An inhibitor of FtsZ with potent and selective anti-staphylococcal
RT   activity.";
RL   Science 321:1673-1675(2008).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 12-315 IN COMPLEX WITH GDP.
RX   PubMed=19383143; DOI=10.1186/1472-6750-9-37;
RA   Raymond A., Lovell S., Lorimer D., Walchli J., Mixon M., Wallace E.,
RA   Thompkins K., Archer K., Burgin A., Stewart L.;
RT   "Combined protein construct and synthetic gene engineering for heterologous
RT   protein expression and crystallization using Gene Composer.";
RL   BMC Biotechnol. 9:37-37(2009).
RN   [12] {ECO:0007744|PDB:4U39}
RP   X-RAY CRYSTALLOGRAPHY (3.19 ANGSTROMS) OF 11-315 IN COMPLEX WITH MCIZ,
RP   ACTIVITY REGULATION, AND MUTAGENESIS OF ASP-280.
RC   STRAIN=168 / PY79;
RX   PubMed=25848052; DOI=10.1073/pnas.1414242112;
RA   Bisson-Filho A.W., Discola K.F., Castellen P., Blasios V., Martins A.,
RA   Sforca M.L., Garcia W., Zeri A.C., Erickson H.P., Dessen A.,
RA   Gueiros-Filho F.J.;
RT   "FtsZ filament capping by MciZ, a developmental regulator of bacterial
RT   division.";
RL   Proc. Natl. Acad. Sci. U.S.A. 112:E2130-E2138(2015).
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:0000255|HAMAP-Rule:MF_00909, ECO:0000269|PubMed:15317782,
CC       ECO:0000269|PubMed:16159787}.
CC   -!- ACTIVITY REGULATION: During sporulation, is negatively regulated by
CC       MciZ, which binds to FtsZ and inhibits its polymerization and the
CC       formation of the Z ring. {ECO:0000269|PubMed:18284588,
CC       ECO:0000269|PubMed:25848052}.
CC   -!- SUBUNIT: Homodimer. Polymerizes to form a dynamic ring structure in a
CC       strictly GTP-dependent manner (By similarity). Interacts directly with
CC       several other division proteins (By similarity). Interacts with FtsA
CC       (PubMed:16159787). Interacts with Phi29 DNA replication protein 1
CC       (PubMed:23836667). Interacts with the cell division inhibitor MciZ
CC       (PubMed:23836667, PubMed:25848052). {ECO:0000255|HAMAP-Rule:MF_00909,
CC       ECO:0000269|PubMed:16159787, ECO:0000269|PubMed:23836667,
CC       ECO:0000269|PubMed:25848052}.
CC   -!- INTERACTION:
CC       P17865; O34894: ezrA; NbExp=4; IntAct=EBI-1569853, EBI-1567579;
CC       P17865; P28264: ftsA; NbExp=7; IntAct=EBI-1569853, EBI-2122615;
CC       P17865; P17865: ftsZ; NbExp=6; IntAct=EBI-1569853, EBI-1569853;
CC       P17865; O31728: sepF; NbExp=8; IntAct=EBI-1569853, EBI-2122748;
CC       P17865; P54166: ugtP; NbExp=3; IntAct=EBI-1569853, EBI-1567571;
CC       P17865; P94542: zapA; NbExp=4; IntAct=EBI-1569853, EBI-2122911;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00909}.
CC       Note=Assembles at midcell at the inner surface of the cytoplasmic
CC       membrane. {ECO:0000255|HAMAP-Rule:MF_00909}.
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://www.proteinspotlight.org/back_issues/171/";
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DR   EMBL; M22630; AAA22457.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB13402.2; -; Genomic_DNA.
DR   EMBL; J05400; AAA83361.1; -; Genomic_DNA.
DR   PIR; I39848; I39848.
DR   RefSeq; NP_389412.2; NC_000964.3.
DR   RefSeq; WP_003232167.1; NC_000964.3.
DR   PDB; 2RHH; X-ray; 2.00 A; A=12-315.
DR   PDB; 2RHJ; X-ray; 1.76 A; A=12-315.
DR   PDB; 2RHL; X-ray; 2.45 A; A/B=12-315.
DR   PDB; 2RHO; X-ray; 2.45 A; A/B=12-315.
DR   PDB; 2VAM; X-ray; 2.50 A; A=1-382.
DR   PDB; 2VXY; X-ray; 1.70 A; A=1-382.
DR   PDB; 4U39; X-ray; 3.19 A; A/B/C/D/E/F/G/H/I=11-315.
DR   AlphaFoldDB; P17865; -.
DR   SMR; P17865; -.
DR   FunCoup; P17865; 590.
DR   IntAct; P17865; 9.
DR   MINT; P17865; -.
DR   STRING; 224308.BSU15290; -.
DR   BindingDB; P17865; -.
DR   ChEMBL; CHEMBL5690; -.
DR   jPOST; P17865; -.
DR   PaxDb; 224308-BSU15290; -.
DR   EnsemblBacteria; CAB13402; CAB13402; BSU_15290.
DR   GeneID; 11241907; -.
DR   GeneID; 306027040; -.
DR   GeneID; 935971; -.
DR   KEGG; bsu:BSU15290; -.
DR   PATRIC; fig|224308.179.peg.1667; -.
DR   eggNOG; COG0206; Bacteria.
DR   InParanoid; P17865; -.
DR   OrthoDB; 9813375at2; -.
DR   PhylomeDB; P17865; -.
DR   BioCyc; BSUB:BSU15290-MONOMER; -.
DR   EvolutionaryTrace; P17865; -.
DR   PRO; PR:P17865; -.
DR   Proteomes; UP000001570; Chromosome.
DR   AbasyAtlas; P17865; -.
DR   GO; GO:0032153; C:cell division site; IBA:GO_Central.
DR   GO; GO:0030428; C:cell septum; IDA:CACAO.
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; IDA:CACAO.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0051301; P:cell division; IMP:CACAO.
DR   GO; GO:0090529; P:cell septum assembly; IEA:UniProtKB-UniRule.
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   DisProt; DP02202; -.
DR   FunFam; 3.30.1330.20:FF:000005; Cell division protein FtsZ; 1.
DR   FunFam; 3.40.50.1440:FF:000023; Cell division protein FtsZ; 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.
DR   PDBsum; 2RHH; -.
DR   PDBsum; 2RHJ; -.
DR   PDBsum; 2RHL; -.
DR   PDBsum; 2RHO; -.
DR   PDBsum; 2VAM; -.
DR   PDBsum; 2VXY; -.
DR   PDBsum; 4U39; -.
PE   1: Evidence at protein level;
KW   3D-structure; Cell cycle; Cell division; Cytoplasm; GTP-binding;
KW   Nucleotide-binding; Reference proteome; Septation.
FT   CHAIN           1..382
FT                   /note="Cell division protein FtsZ"
FT                   /id="PRO_0000114341"
FT   REGION          320..382
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        326..341
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        342..351
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        352..365
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         21..25
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00909,
FT                   ECO:0000269|PubMed:19383143"
FT   BINDING         108..110
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00909,
FT                   ECO:0000269|PubMed:19383143"
FT   BINDING         139
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00909,
FT                   ECO:0000269|PubMed:19383143"
FT   BINDING         143
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00909,
FT                   ECO:0000269|PubMed:19383143"
FT   BINDING         187
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00909,
FT                   ECO:0000269|PubMed:19383143"
FT   MUTAGEN         280
FT                   /note="D->R: Disrupts interaction with MciZ."
FT                   /evidence="ECO:0000269|PubMed:25848052"
FT   CONFLICT        345..346
FT                   /note="EP -> DA (in Ref. 1; AAA22457)"
FT                   /evidence="ECO:0000305"
FT   STRAND          14..19
FT                   /evidence="ECO:0007829|PDB:2VXY"
FT   HELIX           20..32
FT                   /evidence="ECO:0007829|PDB:2VXY"
FT   STRAND          39..46
FT                   /evidence="ECO:0007829|PDB:2VXY"
FT   HELIX           47..51
FT                   /evidence="ECO:0007829|PDB:2VXY"
FT   STRAND          56..60
FT                   /evidence="ECO:0007829|PDB:2VXY"
FT   HELIX           63..66
FT                   /evidence="ECO:0007829|PDB:2VXY"
FT   HELIX           75..84
FT                   /evidence="ECO:0007829|PDB:2VXY"
FT   HELIX           86..93
FT                   /evidence="ECO:0007829|PDB:2VXY"
FT   STRAND          97..108
FT                   /evidence="ECO:0007829|PDB:2VXY"
FT   HELIX           109..123
FT                   /evidence="ECO:0007829|PDB:2VXY"
FT   STRAND          127..134
FT                   /evidence="ECO:0007829|PDB:2VXY"
FT   HELIX           137..139
FT                   /evidence="ECO:0007829|PDB:2VXY"
FT   HELIX           141..157
FT                   /evidence="ECO:0007829|PDB:2VXY"
FT   STRAND          159..165
FT                   /evidence="ECO:0007829|PDB:2VXY"
FT   HELIX           166..172
FT                   /evidence="ECO:0007829|PDB:2VXY"
FT   HELIX           179..198
FT                   /evidence="ECO:0007829|PDB:2VXY"
FT   TURN            199..201
FT                   /evidence="ECO:0007829|PDB:2VXY"
FT   STRAND          205..207
FT                   /evidence="ECO:0007829|PDB:2RHH"
FT   HELIX           211..217
FT                   /evidence="ECO:0007829|PDB:2VXY"
FT   STRAND          221..233
FT                   /evidence="ECO:0007829|PDB:2VXY"
FT   HELIX           236..245
FT                   /evidence="ECO:0007829|PDB:2VXY"
FT   HELIX           254..256
FT                   /evidence="ECO:0007829|PDB:2VXY"
FT   STRAND          258..266
FT                   /evidence="ECO:0007829|PDB:2VXY"
FT   HELIX           272..285
FT                   /evidence="ECO:0007829|PDB:2VXY"
FT   STRAND          291..298
FT                   /evidence="ECO:0007829|PDB:2VXY"
FT   STRAND          303..315
FT                   /evidence="ECO:0007829|PDB:2VXY"
SQ   SEQUENCE   382 AA;  40395 MW;  24E908DEC9685614 CRC64;
     MLEFETNIDG LASIKVIGVG GGGNNAVNRM IENEVQGVEY IAVNTDAQAL NLSKAEVKMQ
     IGAKLTRGLG AGANPEVGKK AAEESKEQIE EALKGADMVF VTAGMGGGTG TGAAPVIAQI
     AKDLGALTVG VVTRPFTFEG RKRQLQAAGG ISAMKEAVDT LIVIPNDRIL EIVDKNTPML
     EAFREADNVL RQGVQGISDL IATPGLINLD FADVKTIMSN KGSALMGIGI ATGENRAAEA
     AKKAISSPLL EAAIDGAQGV LMNITGGTNL SLYEVQEAAD IVASASDQDV NMIFGSVINE
     NLKDEIVVTV IATGFIEQEK DVTKPQRPSL NQSIKTHNQS VPKREPKREE PQQQNTVSRH
     TSQPADDTLD IPTFLRNRNK RG
//