ftsZ:Gene Product(s)

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Nomenclature Function Interactions Localization Sequence Domains Structure Resources Accessions Links References Suggestions

Nomenclature

See Help:Product_nomenclature for help entering or editing information in this section of EcoliWiki.

Standard name

FtsZ

Synonyms

GTP-binding tubulin-like cell division protein[1], B0095[2][1], SulB[2][1], SfiB[2][1], FtsZ[2][1] , ECK0096, JW0093, sfiB, sulB, b0095

Product description

essential cell division protein FtsZ[2][3]

Septal ring GTPase required for cell division and growth; initiation of septation[4]

EC number (for enzymes)


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Notes

Function

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<protect> Gene Ontology
See Help:Gene_ontology for help entering or editing GO terms and GO annotations in EcoliWiki.

Qualifier GO ID GO term name Reference Evidence Code with/from Aspect Notes Status
GO:0003924

GTPase activity

PMID:1528267[5]

IDA: Inferred from Direct Assay

F

complete

GO:0005737

cytoplasm

PMID:1943703[6]

IDA: Inferred from Direct Assay

C

complete

GO:0051258

protein polymerization

PMID:8917533[7]

IDA: Inferred from Direct Assay

P

complete

GO:0000166

nucleotide binding

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0547

F

Seeded from EcoCyc (v14.0)

complete

GO:0000917

barrier septum formation

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0717

P

Seeded from EcoCyc (v14.0)

complete

GO:0003924

GTPase activity

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR008280

F

Seeded from EcoCyc (v14.0)

complete

GO:0003924

GTPase activity

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR018316

F

Seeded from EcoCyc (v14.0)

complete

GO:0032153

cell division site

PMID:9603865[8]

IDA: Inferred from Direct Assay

C

complete

GO:0005515

protein binding

PMID:17307852[9]

IDA: Inferred from Direct Assay

F

Seeded from EcoCyc (v14.0)

complete

GO:0051301

cell division

PMID:2045370[10]

IMP: Inferred from Mutant Phenotype

P

complete

GO:0005515

protein binding

PMID:8752322[11]

IPI: Inferred from Physical Interaction

F

Seeded from EcoCyc (v14.0)

Missing: with/from

GO:0005525

GTP binding

PMID:1528267[5]

IDA: Inferred from Direct Assay

F

complete

GO:0005515

protein binding

PMID:9008158[12]

IDA: Inferred from Direct Assay

F

Seeded from EcoCyc (v14.0)

complete

GO:0005525

GTP binding

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR000158

F

Seeded from EcoCyc (v14.0)

complete

GO:0003924

GTPase activity

PMID:1528268[13]

IDA: Inferred from Direct Assay

F

complete

GO:0005525

GTP binding

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR008280

F

Seeded from EcoCyc (v14.0)

complete

GO:0005525

GTP binding

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR018316

F

Seeded from EcoCyc (v14.0)

complete

GO:0005525

GTP binding

PMID:1528268[13]

IDA: Inferred from Direct Assay

F

complete

GO:0005515

protein binding

PMID:17307852[9]

IDA: Inferred from Direct Assay

F

EcoliWiki:ftsE

complete

GO:0005525

GTP binding

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR020805

F

Seeded from EcoCyc (v14.0)

complete

GO:0005515

protein binding

PMID:8917533[7]

IDA: Inferred from Direct Assay

F

EcoliWiki:ftsA

complete

GO:0005515

protein binding

PMID:9008158[12]

IDA: Inferred from Direct Assay

F

EcoliWiki:zipA

complete

GO:0005525

GTP binding

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0342

F

Seeded from EcoCyc (v14.0)

complete

GO:0005515

protein binding

PMID:8752322[11]

IPI: Inferred from Physical Interaction

EcoliWiki:sulA


F

complete

GO:0005737

cytoplasm

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR000158

C

Seeded from EcoCyc (v14.0)

complete

GO:0005737

cytoplasm

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR020805

C

Seeded from EcoCyc (v14.0)

complete

GO:0005737

cytoplasm

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0963

C

Seeded from EcoCyc (v14.0)

complete

GO:0005737

cytoplasm

GO_REF:0000023

IEA: Inferred from Electronic Annotation

SP_SL:SL-0086

C

Seeded from EcoCyc (v14.0)

complete

GO:0007049

cell cycle

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0131

P

Seeded from EcoCyc (v14.0)

complete

GO:0043234

protein complex

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR003008

C

Seeded from EcoCyc (v14.0)

complete

GO:0043234

protein complex

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR008280

C

Seeded from EcoCyc (v14.0)

complete

GO:0043234

protein complex

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR018316

C

Seeded from EcoCyc (v14.0)

complete

GO:0051258

protein polymerization

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR003008

P

Seeded from EcoCyc (v14.0)

complete

GO:0051258

protein polymerization

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR008280

P

Seeded from EcoCyc (v14.0)

complete

GO:0051258

protein polymerization

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR018316

P

Seeded from EcoCyc (v14.0)

complete

GO:0051301

cell division

IEA: Inferred from Electronic Annotation

SP_KW:KW-0132


P

Seeded from EcoCyc (v14.0)

Missing: reference

GO:0005515

protein binding

PMID:20497333[14]

IPI: Inferred from Physical Interaction

EcoliWiki:zapA


F

complete

GO:0005515

protein binding

PMID:20497333[14]

IPI: Inferred from Physical Interaction

EcoliWiki:ftsZ


F

complete

GO:0051258

protein polymerization

PMID:21321206[15]

IDA: Inferred from Direct Assay

P

Figure 3

complete

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Interactions See Help:Product_interactions for help entering or editing information about gene product interactions in this section of EcoliWiki.

Partner Type Partner Notes References Evidence

Protein

add

PMID:15690043[16]

Experiment(s):EBI-889279

Protein

dnaK

PMID:15690043[16]

Experiment(s):EBI-889279

Protein

ftsK

PMID:15690043[16]

Experiment(s):EBI-889279

Protein

fusA

PMID:15690043[16]

Experiment(s):EBI-889279

Protein

gatY

PMID:15690043[16]

Experiment(s):EBI-889279

Protein

malK

PMID:15690043[16]

Experiment(s):EBI-889279

Protein

mreB

PMID:15690043[16]

Experiment(s):EBI-889279

Protein

pstB

PMID:15690043[16]

Experiment(s):EBI-889279

Protein

recA

PMID:15690043[16]

Experiment(s):EBI-889279

Protein

rplE

PMID:15690043[16]

Experiment(s):EBI-889279

Protein

rpsB

PMID:15690043[16]

Experiment(s):EBI-889279

Protein

rpsE

PMID:15690043[16]

Experiment(s):EBI-889279

Protein

rpsJ

PMID:15690043[16]

Experiment(s):EBI-889279

Protein

secA

PMID:15690043[16]

Experiment(s):EBI-889279

Protein

tufA

PMID:15690043[16]

Experiment(s):EBI-889279

Protein

pflB

PMID:16606699[17]

Experiment(s):EBI-1135563

Protein

rpsD

PMID:16606699[17]

Experiment(s):EBI-1135563

Protein

uspG

PMID:16606699[17]

Experiment(s):EBI-1135563

Protein

yedD

PMID:16606699[17]

Experiment(s):EBI-1135563

Protein

moaC

PMID:16606699[17]

Experiment(s):EBI-1135563

Protein

tatE

PMID:16606699[17]

Experiment(s):EBI-1135563

Protein

rplN

PMID:16606699[17]

Experiment(s):EBI-1135563

Protein

secA

PMID:19402753[18]

MALDI(Z-score):18.856613

Protein

fusA

PMID:19402753[18]

MALDI(Z-score):20.694080

Protein

ftsK

PMID:19402753[18]

MALDI(Z-score):18.687667

Protein

recA

PMID:19402753[18]

MALDI(Z-score):38.547831

Protein

malT

PMID:19402753[18]

MALDI(Z-score):19.663296

Protein

pstB

PMID:19402753[18]

MALDI(Z-score):38.846575

Protein

gatY

PMID:19402753[18]

MALDI(Z-score):31.574250

Protein

add

PMID:19402753[18]

MALDI(Z-score):27.158866

Protein

SulA

FtsZ full length and truncations

PMID:8752322[11]

2 hybrid

Protein

FtsA

FtsA/FtsZ ratio is important for cell division


PMID:1400163[19]

PMID:1400183[20]


Genetic Interference

Protein

FtsA

FtsA may link Z-ring to septal specific peptidoglycan biosynthesis

PMID:6365891[21]

Protein

SlmA

PMID:21321206[15]

Bacterial 2 hybrid

Protein

MinCD

overproduction of MinCD blocks localization of FtsZ

PMID:8432706[22]

Protein

sdiA

ftsZ84 strains grown at 42C showed restored ability to form colonies with introduction of sdiA plasmids

PMID:1915297[23]


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Notes

  • FtsZ is a key player in Septation
  • FtsZ contains a fairly strong activation domain (AD) and cannot be used as the bait in 2 hybrid screens.[11]

Localization

See Help:Product_localization for how to add or edit information in this section of EcoliWiki.

Compartment Description Evidence Reference/Source Notes

cytoplasm

From EcoCyc[3]

cytoplasm

fractionation experiments

PMID:1943703[6]

cytoplasm

fractionation

PMID:1528267[5]

membrane-associated in the presence of GTP

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Notes

Structure and Physical Properties

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<protect> Physical Properties See Help:Product_physical_properties for help entering or editing information about the physical properties of this gene product.

Name
Sequence

at EcoCyc 

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
Length

383

Mol. Wt

40.323 kDa

pI

4.5 (calculated)

Extinction coefficient

4,470 (calc based on 3 Y, 0 W, and 0 C residues)

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Domains/Motifs/Modification Sites

See Help:Product_domains_motifs for help entering or editing information in this section of EcoliWiki.

Type Residues Description Notes References

Domain

12..184

PF00091 Tubulin/FtsZ family, GTPase domain

PMID:19920124[24]

Domain

221..318

PF12327 FtsZ family, C-terminal domain

PMID:19920124[24]

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<motif_map/>

Structure
See Help:Product_structure for help entering or editing information in this section of EcoliWiki.

Structures

<beststructure> gene=ftsZ taxon=562,83333 </beststructure>

Models

View models at:

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Structure figures

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Notes

  • The dynamics of FtsZ ring formation/constriction was investigated in Addinall et al.(1997)[25].
  • Aluminum fluoride abolishes FtsZ GTPase activity[26].

Gene Product Resources

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See Help:Product_resources for help with entering or editing information in this section of EcoliWiki.

Resource type Source Notes/Reference

Purified protein

FtsZ D212N- defective GTPase activity

PMID:21321206[15]

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Notes

Accessions in Other Databases

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See Help:Gene_accessions for help with entering information into the Gene Accessions table.

Database Accession Notes

NCBI (Protein) (EcoliWiki Page)

GI:16128088

Escherichia coli str. K-12 substr. MG1655

NCBI (Protein) (EcoliWiki Page)

GeneID:944786

Escherichia coli str. K-12 substr. MG1655

ASAP

ASAP:ABE-0000333

Escherichia coli str. K-12 substr. MG1655

UniProt (EcoliWiki Page)

UniProtKB/Swiss-Prot:P0A9A6

Escherichia coli str. K-12 substr. MG1655

EcoCyc

EcoCyc:EG10347

Escherichia coli str. K-12 substr. MG1655

EcoGene

EcoGene:EG10347

Escherichia coli str. K-12 substr. MG1655

NCBI (Gene) (EcoliWiki Page)

GeneID:944786

Escherichia coli str. K-12 substr. MG1655

RegulonDB

RegulonDB:ECK120000341

Escherichia coli str. K-12 substr. MG1655

EchoBASE

EchoBASE:EB0343

Escherichia coli str. K-12 substr. MG1655

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Notes

Links

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References

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See Help:References for how to manage references in EcoliWiki.

  1. ↑ 1.0 1.1 1.2 1.3 1.4 Riley, M. et al. (2006) Nucleic Acids Res 34:1-6 (corrected supplemental data from B. Wanner)
  2. ↑ 2.0 2.1 2.2 2.3 2.4 EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  3. ↑ 3.0 3.1 EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  4. ↑ EcoGene: Rudd, KE (2000) EcoGene: a genome sequence database for Escherichia coli K-12. Nucleic Acids Res 28:60-4.
  5. ↑ 5.0 5.1 5.2 RayChaudhuri, D & Park, JT (1992) Escherichia coli cell-division gene ftsZ encodes a novel GTP-binding protein. Nature 359 251-4 PubMed
  6. ↑ 6.0 6.1 Pla, J et al. (1991) Preferential cytoplasmic location of FtsZ, a protein essential for Escherichia coli septation. Mol. Microbiol. 5 1681-6 PubMed
  7. ↑ 7.0 7.1 Ma, X et al. (1996) Colocalization of cell division proteins FtsZ and FtsA to cytoskeletal structures in living Escherichia coli cells by using green fluorescent protein. Proc. Natl. Acad. Sci. U.S.A. 93 12998-3003 PubMed
  8. ↑ Wang, L et al. (1998) FtsI and FtsW are localized to the septum in Escherichia coli. J. Bacteriol. 180 2810-6 PubMed
  9. ↑ 9.0 9.1 Corbin, BD et al. (2007) Interaction between cell division proteins FtsE and FtsZ. J. Bacteriol. 189 3026-35 PubMed
  10. ↑ Dai, K & Lutkenhaus, J (1991) ftsZ is an essential cell division gene in Escherichia coli. J. Bacteriol. 173 3500-6 PubMed
  11. ↑ 11.0 11.1 11.2 11.3 Huang, J et al. (1996) Interaction between FtsZ and inhibitors of cell division. J. Bacteriol. 178 5080-5 PubMed
  12. ↑ 12.0 12.1 Hale, CA & de Boer, PA (1997) Direct binding of FtsZ to ZipA, an essential component of the septal ring structure that mediates cell division in E. coli. Cell 88 175-85 PubMed
  13. ↑ 13.0 13.1 de Boer, P et al. (1992) The essential bacterial cell-division protein FtsZ is a GTPase. Nature 359 254-6 PubMed
  14. ↑ 14.0 14.1 Alexeeva, S et al. (2010) Direct interactions of early and late assembling division proteins in Escherichia coli cells resolved by FRET. Mol. Microbiol. 77 384-98 PubMed
  15. ↑ 15.0 15.1 15.2 Cho, H et al. (2011) Nucleoid occlusion factor SlmA is a DNA-activated FtsZ polymerization antagonist. Proc. Natl. Acad. Sci. U.S.A. 108 3773-8 PubMed
  16. ↑ 16.00 16.01 16.02 16.03 16.04 16.05 16.06 16.07 16.08 16.09 16.10 16.11 16.12 16.13 16.14 Butland, G et al. (2005) Interaction network containing conserved and essential protein complexes in Escherichia coli. Nature 433 531-7 PubMed
  17. ↑ 17.0 17.1 17.2 17.3 17.4 17.5 17.6 Arifuzzaman, M et al. (2006) Large-scale identification of protein-protein interaction of Escherichia coli K-12. Genome Res. 16 686-91 PubMed
  18. ↑ 18.0 18.1 18.2 18.3 18.4 18.5 18.6 18.7 Hu, P et al. (2009) Global functional atlas of Escherichia coli encompassing previously uncharacterized proteins. PLoS Biol. 7 e96 PubMed
  19. ↑ Dai, K & Lutkenhaus, J (1992) The proper ratio of FtsZ to FtsA is required for cell division to occur in Escherichia coli. J. Bacteriol. 174 6145-51 PubMed
  20. ↑ Dewar, SJ et al. (1992) Inhibition of cell division initiation by an imbalance in the ratio of FtsA to FtsZ. J. Bacteriol. 174 6314-6 PubMed
  21. ↑ Tormo, A & Vicente, M (1984) The ftsA gene product participates in formation of the Escherichia coli septum structure. J. Bacteriol. 157 779-84 PubMed
  22. ↑ Bi, E & Lutkenhaus, J (1993) Cell division inhibitors SulA and MinCD prevent formation of the FtsZ ring. J. Bacteriol. 175 1118-25 PubMed
  23. ↑ Wang, XD et al. (1991) A factor that positively regulates cell division by activating transcription of the major cluster of essential cell division genes of Escherichia coli. EMBO J. 10 3363-72 PubMed
  24. ↑ 24.0 24.1 Finn, RD et al. (2010) The Pfam protein families database. Nucleic Acids Res. 38 D211-22 PubMed
  25. ↑ Addinall, SG et al. (1997) Temperature shift experiments with an ftsZ84(Ts) strain reveal rapid dynamics of FtsZ localization and indicate that the Z ring is required throughout septation and cannot reoccupy division sites once constriction has initiated. J. Bacteriol. 179 4277-84 PubMed
  26. ↑ RayChaudhuri, D & Park, JT (1994) A point mutation converts Escherichia coli FtsZ septation GTPase to an ATPase. J. Biol. Chem. 269 22941-4 PubMed

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