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Protein

Cell division protein FtsZ

Gene

ftsZ

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produce a new cell wall between the dividing cells. Binds GTP and shows GTPase activity.2 PublicationsUniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei139 – 1391GTP1 PublicationUniRule annotation
Binding sitei143 – 1431GTP1 PublicationUniRule annotation
Binding sitei187 – 1871GTP1 PublicationUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi21 – 255GTP1 PublicationUniRule annotation
Nucleotide bindingi108 – 1103GTP1 PublicationUniRule annotation

GO - Molecular functioni

  1. GTPase activity Source: CACAO
  2. GTP binding Source: UniProtKB-HAMAP
  3. identical protein binding Source: IntAct

GO - Biological processi

  1. barrier septum assembly Source: UniProtKB-KW
  2. cell division Source: CACAO
  3. FtsZ-dependent cytokinesis Source: UniProtKB-HAMAP
  4. GTP catabolic process Source: InterPro
  5. protein polymerization Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Septation

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciBSUB:BSU15290-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Cell division protein FtsZUniRule annotation
Gene namesi
Name:ftsZUniRule annotation
Ordered Locus Names:BSU15290
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570: Chromosome

Organism-specific databases

GenoListiBSU15290. [Micado]

Subcellular locationi

Cytoplasm UniRule annotation
Note: Assembles at midcell at the inner surface of the cytoplasmic membrane.UniRule annotation

GO - Cellular componenti

  1. cell division site Source: UniProtKB-HAMAP
  2. cell septum Source: CACAO
  3. cytoplasm Source: UniProtKB-SubCell
  4. protein complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 382382Cell division protein FtsZPRO_0000114341Add
BLAST

Proteomic databases

PaxDbiP17865.

Interactioni

Subunit structurei

Homodimer. Polymerizes to form a dynamic ring structure in a strictly GTP-dependent manner (By similarity). Interacts directly with several other division proteins (By similarity). Interacts with FtsA.1 PublicationUniRule annotation

Binary interactionsi

WithEntry#Exp.IntActNotes
itself6EBI-1569853,EBI-1569853
ezrAO348944EBI-1569853,EBI-1567579
ftsAP282647EBI-1569853,EBI-2122615
sepFO317288EBI-1569853,EBI-2122748
ugtPP541663EBI-1569853,EBI-1567571
zapAP945424EBI-1569853,EBI-2122911

Protein-protein interaction databases

IntActiP17865. 9 interactions.
MINTiMINT-126054.
STRINGi224308.BSU15290.

Structurei

Secondary structure

1
382
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi14 – 196Combined sources
Helixi20 – 3213Combined sources
Beta strandi39 – 468Combined sources
Helixi47 – 515Combined sources
Beta strandi56 – 605Combined sources
Helixi63 – 664Combined sources
Helixi75 – 8410Combined sources
Helixi86 – 938Combined sources
Beta strandi97 – 10812Combined sources
Helixi109 – 12315Combined sources
Beta strandi127 – 1348Combined sources
Helixi137 – 1393Combined sources
Helixi141 – 15717Combined sources
Beta strandi159 – 1657Combined sources
Helixi166 – 1727Combined sources
Helixi179 – 19820Combined sources
Turni199 – 2013Combined sources
Beta strandi205 – 2073Combined sources
Helixi211 – 2177Combined sources
Beta strandi221 – 23313Combined sources
Helixi236 – 24510Combined sources
Helixi254 – 2563Combined sources
Beta strandi258 – 2669Combined sources
Helixi272 – 28514Combined sources
Beta strandi291 – 2988Combined sources
Beta strandi303 – 31513Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2RHHX-ray2.00A12-315[»]
2RHJX-ray1.76A12-315[»]
2RHLX-ray2.45A/B12-315[»]
2RHOX-ray2.45A/B12-315[»]
2VAMX-ray2.50A1-382[»]
2VXYX-ray1.70A1-382[»]
ProteinModelPortaliP17865.
SMRiP17865. Positions 11-316.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP17865.

Family & Domainsi

Sequence similaritiesi

Belongs to the FtsZ family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0206.
HOGENOMiHOG000049094.
InParanoidiP17865.
KOiK03531.
OMAiDSHANII.
OrthoDBiEOG6S7XZG.
PhylomeDBiP17865.

Family and domain databases

Gene3Di3.30.1330.20. 1 hit.
3.40.50.1440. 1 hit.
HAMAPiMF_00909. FtsZ.
InterProiIPR000158. Cell_div_FtsZ.
IPR020805. Cell_div_FtsZ_CS.
IPR024757. FtsZ_C.
IPR008280. Tub_FtsZ_C.
IPR018316. Tubulin/FtsZ_2-layer-sand-dom.
IPR003008. Tubulin_FtsZ_GTPase.
[Graphical view]
PfamiPF12327. FtsZ_C. 1 hit.
PF00091. Tubulin. 1 hit.
[Graphical view]
PRINTSiPR00423. CELLDVISFTSZ.
SMARTiSM00864. Tubulin. 1 hit.
SM00865. Tubulin_C. 1 hit.
[Graphical view]
SUPFAMiSSF52490. SSF52490. 1 hit.
SSF55307. SSF55307. 1 hit.
TIGRFAMsiTIGR00065. ftsZ. 1 hit.
PROSITEiPS01134. FTSZ_1. 1 hit.
PS01135. FTSZ_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P17865-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLEFETNIDG LASIKVIGVG GGGNNAVNRM IENEVQGVEY IAVNTDAQAL
60 70 80 90 100
NLSKAEVKMQ IGAKLTRGLG AGANPEVGKK AAEESKEQIE EALKGADMVF
110 120 130 140 150
VTAGMGGGTG TGAAPVIAQI AKDLGALTVG VVTRPFTFEG RKRQLQAAGG
160 170 180 190 200
ISAMKEAVDT LIVIPNDRIL EIVDKNTPML EAFREADNVL RQGVQGISDL
210 220 230 240 250
IATPGLINLD FADVKTIMSN KGSALMGIGI ATGENRAAEA AKKAISSPLL
260 270 280 290 300
EAAIDGAQGV LMNITGGTNL SLYEVQEAAD IVASASDQDV NMIFGSVINE
310 320 330 340 350
NLKDEIVVTV IATGFIEQEK DVTKPQRPSL NQSIKTHNQS VPKREPKREE
360 370 380
PQQQNTVSRH TSQPADDTLD IPTFLRNRNK RG
Length:382
Mass (Da):40,395
Last modified:June 16, 2009 - v3
Checksum:i24E908DEC9685614
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti345 – 3462EP → DA in AAA22457 (PubMed:3139638).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M22630 Genomic DNA. Translation: AAA22457.1.
AL009126 Genomic DNA. Translation: CAB13402.2.
J05400 Genomic DNA. Translation: AAA83361.1.
PIRiI39848.
RefSeqiNP_389412.2. NC_000964.3.

Genome annotation databases

EnsemblBacteriaiCAB13402; CAB13402; BSU15290.
GeneIDi935971.
KEGGibsu:BSU15290.
PATRICi18974863. VBIBacSub10457_1623.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M22630 Genomic DNA. Translation: AAA22457.1.
AL009126 Genomic DNA. Translation: CAB13402.2.
J05400 Genomic DNA. Translation: AAA83361.1.
PIRiI39848.
RefSeqiNP_389412.2. NC_000964.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2RHHX-ray2.00A12-315[»]
2RHJX-ray1.76A12-315[»]
2RHLX-ray2.45A/B12-315[»]
2RHOX-ray2.45A/B12-315[»]
2VAMX-ray2.50A1-382[»]
2VXYX-ray1.70A1-382[»]
ProteinModelPortaliP17865.
SMRiP17865. Positions 11-316.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP17865. 9 interactions.
MINTiMINT-126054.
STRINGi224308.BSU15290.

Chemistry

BindingDBiP17865.
ChEMBLiCHEMBL5690.

Proteomic databases

PaxDbiP17865.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB13402; CAB13402; BSU15290.
GeneIDi935971.
KEGGibsu:BSU15290.
PATRICi18974863. VBIBacSub10457_1623.

Organism-specific databases

GenoListiBSU15290. [Micado]

Phylogenomic databases

eggNOGiCOG0206.
HOGENOMiHOG000049094.
InParanoidiP17865.
KOiK03531.
OMAiDSHANII.
OrthoDBiEOG6S7XZG.
PhylomeDBiP17865.

Enzyme and pathway databases

BioCyciBSUB:BSU15290-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP17865.

Family and domain databases

Gene3Di3.30.1330.20. 1 hit.
3.40.50.1440. 1 hit.
HAMAPiMF_00909. FtsZ.
InterProiIPR000158. Cell_div_FtsZ.
IPR020805. Cell_div_FtsZ_CS.
IPR024757. FtsZ_C.
IPR008280. Tub_FtsZ_C.
IPR018316. Tubulin/FtsZ_2-layer-sand-dom.
IPR003008. Tubulin_FtsZ_GTPase.
[Graphical view]
PfamiPF12327. FtsZ_C. 1 hit.
PF00091. Tubulin. 1 hit.
[Graphical view]
PRINTSiPR00423. CELLDVISFTSZ.
SMARTiSM00864. Tubulin. 1 hit.
SM00865. Tubulin_C. 1 hit.
[Graphical view]
SUPFAMiSSF52490. SSF52490. 1 hit.
SSF55307. SSF55307. 1 hit.
TIGRFAMsiTIGR00065. ftsZ. 1 hit.
PROSITEiPS01134. FTSZ_1. 1 hit.
PS01135. FTSZ_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of Bacillus subtilis homologs of Escherichia coli cell division genes ftsZ and ftsA."
    Beall B., Lowe M., Lutkenhaus J.
    J. Bacteriol. 170:4855-4864(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
    Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
    , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
    Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 168.
  3. "From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later."
    Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.
    Microbiology 155:1758-1775(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION TO 345-346.
  4. "Cloning, genetic organization, and characterization of a structural gene encoding bacillopeptidase F from Bacillus subtilis."
    Wu X.-C., Nathoo S., Pang A.S.-H., Carne T., Wang S.-L.
    J. Biol. Chem. 265:6845-6850(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 371-382.
  5. "Assembly dynamics of FtsZ rings in Bacillus subtilis and Escherichia coli and effects of FtsZ-regulating proteins."
    Anderson D.E., Gueiros-Filho F.J., Erickson H.P.
    J. Bacteriol. 186:5775-5781(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
    Strain: JDB401.
  6. "Cell division in Bacillus subtilis: FtsZ and FtsA association is Z-ring independent, and FtsA is required for efficient midcell Z-Ring assembly."
    Jensen S.O., Thompson L.S., Harry E.J.
    J. Bacteriol. 187:6536-6544(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH FTSA.
    Strain: 168.
  7. "Structural insights into the conformational variability of FtsZ."
    Oliva M.A., Trambaiolo D., Lowe J.
    J. Mol. Biol. 373:1229-1242(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
  8. Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
  9. "Combined protein construct and synthetic gene engineering for heterologous protein expression and crystallization using Gene Composer."
    Raymond A., Lovell S., Lorimer D., Walchli J., Mixon M., Wallace E., Thompkins K., Archer K., Burgin A., Stewart L.
    BMC Biotechnol. 9:37-37(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 12-315 IN COMPLEX WITH GDP.

Entry informationi

Entry nameiFTSZ_BACSU
AccessioniPrimary (citable) accession number: P17865
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: June 16, 2009
Last modified: March 4, 2015
This is version 123 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.