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P17865

- FTSZ_BACSU

UniProt

P17865 - FTSZ_BACSU

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Protein

Cell division protein FtsZ

Gene

ftsZ

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - 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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi104 – 1129GTPUniRule 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. 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-HAMAP
  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 – 196
Helixi20 – 3213
Beta strandi39 – 468
Helixi47 – 515
Beta strandi56 – 605
Helixi63 – 664
Helixi75 – 8410
Helixi86 – 938
Beta strandi97 – 10812
Helixi109 – 12315
Beta strandi127 – 1348
Helixi137 – 1393
Helixi141 – 15717
Beta strandi159 – 1657
Helixi166 – 1727
Helixi179 – 19820
Turni199 – 2013
Beta strandi205 – 2073
Helixi211 – 2177
Beta strandi221 – 23313
Helixi236 – 24510
Helixi254 – 2563
Beta strandi258 – 2669
Helixi272 – 28514
Beta strandi291 – 2988
Beta strandi303 – 31513

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.
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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
M22630 Genomic DNA. Translation: AAA22457.1 .
AL009126 Genomic DNA. Translation: CAB13402.2 .
J05400 Genomic DNA. Translation: AAA83361.1 .
PIRi I39848.
RefSeqi NP_389412.2. NC_000964.3.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2RHH X-ray 2.00 A 12-315 [» ]
2RHJ X-ray 1.76 A 12-315 [» ]
2RHL X-ray 2.45 A/B 12-315 [» ]
2RHO X-ray 2.45 A/B 12-315 [» ]
2VAM X-ray 2.50 A 1-382 [» ]
2VXY X-ray 1.70 A 1-382 [» ]
ProteinModelPortali P17865.
SMRi P17865. Positions 11-316.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P17865. 9 interactions.
MINTi MINT-126054.
STRINGi 224308.BSU15290.

Chemistry

BindingDBi P17865.
ChEMBLi CHEMBL5690.

Proteomic databases

PaxDbi P17865.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAB13402 ; CAB13402 ; BSU15290 .
GeneIDi 935971.
KEGGi bsu:BSU15290.
PATRICi 18974863. VBIBacSub10457_1623.

Organism-specific databases

GenoListi BSU15290. [Micado ]

Phylogenomic databases

eggNOGi COG0206.
HOGENOMi HOG000049094.
InParanoidi P17865.
KOi K03531.
OrthoDBi EOG6S7XZG.
PhylomeDBi P17865.

Enzyme and pathway databases

BioCyci BSUB:BSU15290-MONOMER.

Miscellaneous databases

EvolutionaryTracei P17865.

Family and domain databases

Gene3Di 3.30.1330.20. 1 hit.
3.40.50.1440. 1 hit.
HAMAPi MF_00909. FtsZ.
InterProi IPR000158. 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 ]
Pfami PF12327. FtsZ_C. 1 hit.
PF00091. Tubulin. 1 hit.
[Graphical view ]
PRINTSi PR00423. CELLDVISFTSZ.
SMARTi SM00864. Tubulin. 1 hit.
SM00865. Tubulin_C. 1 hit.
[Graphical view ]
SUPFAMi SSF52490. SSF52490. 1 hit.
SSF55307. SSF55307. 1 hit.
TIGRFAMsi TIGR00065. ftsZ. 1 hit.
PROSITEi PS01134. FTSZ_1. 1 hit.
PS01135. FTSZ_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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.

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: October 29, 2014
This is version 120 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