FTSZ_BACSU
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 03-AUG-2022, entry version 168.
DE RecName: Full=Cell division protein FtsZ {ECO:0000255|HAMAP-Rule:MF_00909};
GN Name=ftsZ {ECO:0000255|HAMAP-Rule:MF_00909}; OrderedLocusNames=BSU15290;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; 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://web.expasy.org/spotlight/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; NZ_JNCM01000035.1.
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=12-315.
DR PDBsum; 2RHH; -.
DR PDBsum; 2RHJ; -.
DR PDBsum; 2RHL; -.
DR PDBsum; 2RHO; -.
DR PDBsum; 2VAM; -.
DR PDBsum; 2VXY; -.
DR PDBsum; 4U39; -.
DR AlphaFoldDB; P17865; -.
DR SMR; P17865; -.
DR IntAct; P17865; 9.
DR MINT; P17865; -.
DR STRING; 224308.BSU15290; -.
DR BindingDB; P17865; -.
DR ChEMBL; CHEMBL5690; -.
DR jPOST; P17865; -.
DR PaxDb; P17865; -.
DR PRIDE; P17865; -.
DR EnsemblBacteria; CAB13402; CAB13402; BSU_15290.
DR GeneID; 935971; -.
DR KEGG; bsu:BSU15290; -.
DR PATRIC; fig|224308.179.peg.1667; -.
DR eggNOG; COG0206; Bacteria.
DR InParanoid; P17865; -.
DR OMA; GNPSIGQ; -.
DR PhylomeDB; P17865; -.
DR BioCyc; BSUB:BSU15290-MON; -.
DR EvolutionaryTrace; P17865; -.
DR PRO; PR:P17865; -.
DR Proteomes; UP000001570; Chromosome.
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; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
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: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 DisProt; DP02202; -.
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; 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 325..339
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..354
FT /note="Basic and acidic 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
