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ECOLI:FTSZ

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) ftsZ (ECO:0000255 with HAMAP-Rule:MF_00909) (synonyms: sfiB, sulB)
Protein Name(s) Cell division protein FtsZ (ECO:0000255 with HAMAP-Rule:MF_00909)
External Links
UniProt P0A9A6
EMBL U00096
AP009048
X55034
K02668
M19211
PIR G64731
RefSeq NP_414637.1
YP_488400.1
PDB 1F47
PDBsum 1F47
ProteinModelPortal P0A9A6
SMR P0A9A6
DIP DIP-31873N
IntAct P0A9A6
MINT MINT-8092601
STRING 511145.b0095
BindingDB P0A9A6
ChEMBL CHEMBL3999
SWISS-2DPAGE P0A9A6
PaxDb P0A9A6
PRIDE P0A9A6
EnsemblBacteria AAC73206
BAB96663
GeneID 12932893
944786
KEGG ecj:Y75_p0094
eco:b0095
PATRIC 32115295
EchoBASE EB0343
EcoGene EG10347
eggNOG COG0206
HOGENOM HOG000049094
InParanoid P0A9A6
KO K03531
OMA AQVIWGI
OrthoDB EOG6S7XZG
PhylomeDB P0A9A6
BioCyc EcoCyc:EG10347-MONOMER
ECOL316407:JW0093-MONOMER
EvolutionaryTrace P0A9A6
PRO PR:P0A9A6
Proteomes UP000000318
UP000000625
Genevestigator P0A9A6
GO GO:0032153
GO:0005737
GO:0043234
GO:0005525
GO:0003924
GO:0042802
GO:0000917
GO:0051301
GO:0043093
GO:0051258
Gene3D 3.30.1330.20
3.40.50.1440
HAMAP MF_00909
InterPro IPR000158
IPR020805
IPR024757
IPR008280
IPR018316
IPR003008
Pfam PF12327
PF00091
PRINTS PR00423
SMART SM00864
SM00865
SUPFAM SSF52490
SSF55307
TIGRFAMs TIGR00065
PROSITE PS01134
PS01135

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0051258

protein polymerization

PMID:18593876[1]

ECO:0000314

P

Figure 1.

complete

involved_in

GO:0051301

cell division

PMID:21317324[2]

ECO:0000316

genetic interaction evidence used in manual assertion

UniProtKB:P0A6H1

P

Seeded From UniProt

complete

involved_in

GO:0051301

cell division

PMID:21317324[2]

ECO:0000316

genetic interaction evidence used in manual assertion

P

Seeded From UniProt

Missing: with/from

involved_in

GO:0051301

cell division

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10347
PANTHER:PTN000768275
UniProtKB:P17865
UniProtKB:P47466

P

Seeded From UniProt

complete

part_of

GO:0032153

cell division site

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10347
PANTHER:PTN000768275

C

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10347
PANTHER:PTN000768275

C

Seeded From UniProt

complete

enables

GO:0005525

GTP binding

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10347
PANTHER:PTN000768275

F

Seeded From UniProt

complete

enables

GO:0003924

GTPase activity

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10347
PANTHER:PTN000768275
TAIR:locus:2049455
TAIR:locus:2161610
UniProtKB:P17865
UniProtKB:P9WN95

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:24316672[4]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P0A9A6

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:22566654[5]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P0A9A6

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:22515815[6]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P0A9A6

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:22064072[7]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P0A9A6

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:21216997[8]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P0A9A6

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:21216995[9]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P0A9A6

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:19541655[10]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P0A9A6

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:19415799[11]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P0A9A6

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:18394147[12]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P0A9A6

F

Seeded From UniProt

complete

involved_in

GO:0051301

cell division

PMID:2045370[13]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0051258

protein polymerization

PMID:8917533[14]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0051258

protein polymerization

PMID:21321206[15]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0032153

cell division site

PMID:9603865[16]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

PMID:1943703[17]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0005525

GTP binding

PMID:1528268[18]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0005525

GTP binding

PMID:1528267[19]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

GO:0051301

cell division

PMID:8917533[14]

ECO:0000315

P

Figure 2b and C FtsZ labeled with GDP for flourences, shows formation of ring during intermediate and late stages of division.

complete
CACAO 3799

enables

GO:0003924

GTPase activity

PMID:1528268[18]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

GO:0043164

Gram-negative-bacterium-type cell wall biogenesis

PMID:19346310[20]

ECO:0000316

UniProtKB:P0A9A6


P

Table 1 strain 3 In the absence of MreB, FtsZ can tether and direct a generalized and evenly dispersed peptidoglycan, via a PBP2 pathway, producing a spherical-shaped cell

complete
CACAO 3945

enables

GO:0003924

GTPase activity

PMID:1528267[19]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

GO:0003924

GTPase activity

PMID:22056926[21]

ECO:0000315

F

FIG 2 Deletion of ZapB specifically reduces FtsZ division potential. Overnight cultures of TS mutant strains were grown to equal density in LB medium at 30°C and serially diluted (10−1 to 10−6) in LB medium. Aliquots (10 μl) were spotted on NA plates incubated at 30°C overnight.

complete
CACAO 3969

enables

GO:0003924

GTPase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR003008

F

Seeded From UniProt

complete

GO:0000910

cytokinesis

PMID:8917533[14]

ECO:0000315

P

Figure 2b and C FtsZ labeled with GDP for flourences, shows formation of ring during intermediate and late stages of division, indication of involvement in cytokinesis.

complete
CACAO 10539

enables

GO:0005525

GTP binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000158
InterPro:IPR020805

F

Seeded From UniProt

complete

GO:0000910

cytokinesis

PMID:8917533[14]

ECO:0000315

P

Figure 2b and C FtsZ labeled with GDP for flourences, shows formation of ring during intermediate and late stages of division.

complete
CACAO 4252

enables

GO:0005525

GTP binding

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000100343

F

Seeded From UniProt

complete

GO:0051301

cell division

PMID:21317324[2]

ECO:0000316

UniProtKB:P0A6H1


P

Fig 1.

complete
CACAO 6836

involved_in

GO:0043093

FtsZ-dependent cytokinesis

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000100343

P

Seeded From UniProt

complete

involved_in

GO:0051258

protein polymerization

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000100343

P

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000100343

C

Seeded From UniProt

complete

part_of

GO:0032153

cell division site

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000100343

C

Seeded From UniProt

complete

involved_in

GO:0090529

cell septum assembly

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000100343

P

Seeded From UniProt

complete

enables

GO:0003924

GTPase activity

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000100343

F

Seeded From UniProt

complete

involved_in

GO:0051301

cell division

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0132

P

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0963
UniProtKB-SubCell:SL-0086

C

Seeded From UniProt

complete

involved_in

GO:0000917

division septum assembly

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0717

P

Seeded From UniProt

complete

involved_in

GO:0007049

cell cycle

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0131

P

Seeded From UniProt

complete

enables

GO:0005525

GTP binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0342

F

Seeded From UniProt

complete

enables

GO:0000166

nucleotide binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0547

F

Seeded From UniProt

complete

GO:0043093

FtsZ-dependent cytokinesis

PMID:9882666[22]

ECO:0000314

P

Table 3 Localization of GFP-FtsQ in fts mutants, shows how denaturation of temperature-sensitive FtsZ at 42°C prevents FtsQ localization and results in no cytokinetic ring formation.

complete
CACAO 11013

GO:0051301

cell division

PMID:2045370[13]

ECO:0000315

P

Fig 3. The researcher constructed a null allele of ftsZ in a strain carrying additional copies offtsZ on a plasmid with a temperature-sensitive replication defect. This strain was temperature sensitive for cell division and viability, confirming that ftsZ is an essential cell division gene.

complete
CACAO 3968

edit table

Notes

References

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

  1. ↑ Srinivasan, R et al. (2008) The bacterial cell division protein FtsZ assembles into cytoplasmic rings in fission yeast. Genes Dev. 22 1741-6 PubMed GONUTS page
  2. ↑ 2.0 2.1 2.2 Camberg, JL et al. (2011) The interplay of ClpXP with the cell division machinery in Escherichia coli. J. Bacteriol. 193 1911-8 PubMed GONUTS page
  3. ↑ 3.0 3.1 3.2 3.3 3.4 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  4. ↑ Loose, M & Mitchison, TJ (2014) The bacterial cell division proteins FtsA and FtsZ self-organize into dynamic cytoskeletal patterns. Nat. Cell Biol. 16 38-46 PubMed GONUTS page
  5. ↑ Mateos-Gil, P et al. (2012) Depolymerization dynamics of individual filaments of bacterial cytoskeletal protein FtsZ. Proc. Natl. Acad. Sci. U.S.A. 109 8133-8 PubMed GONUTS page
  6. ↑ Masuda, H et al. (2012) YeeU enhances the bundling of cytoskeletal polymers of MreB and FtsZ, antagonizing the CbtA (YeeV) toxicity in Escherichia coli. Mol. Microbiol. 84 979-89 PubMed GONUTS page
  7. ↑ Salvarelli, E et al. (2011) Independence between GTPase active sites in the Escherichia coli cell division protein FtsZ. FEBS Lett. 585 3880-3 PubMed GONUTS page
  8. ↑ Hale, CA et al. (2011) Identification of Escherichia coli ZapC (YcbW) as a component of the division apparatus that binds and bundles FtsZ polymers. J. Bacteriol. 193 1393-404 PubMed GONUTS page
  9. ↑ Durand-Heredia, JM et al. (2011) Identification and characterization of ZapC, a stabilizer of the FtsZ ring in Escherichia coli. J. Bacteriol. 193 1405-13 PubMed GONUTS page
  10. ↑ Camberg, JL et al. (2009) ClpXP protease degrades the cytoskeletal protein, FtsZ, and modulates FtsZ polymer dynamics. Proc. Natl. Acad. Sci. U.S.A. 106 10614-9 PubMed GONUTS page
  11. ↑ Shen, B & Lutkenhaus, J (2009) The conserved C-terminal tail of FtsZ is required for the septal localization and division inhibitory activity of MinC(C)/MinD. Mol. Microbiol. 72 410-24 PubMed GONUTS page
  12. ↑ Ebersbach, G et al. (2008) Novel coiled-coil cell division factor ZapB stimulates Z ring assembly and cell division. Mol. Microbiol. 68 720-35 PubMed GONUTS page
  13. ↑ 13.0 13.1 Dai, K & Lutkenhaus, J (1991) ftsZ is an essential cell division gene in Escherichia coli. J. Bacteriol. 173 3500-6 PubMed GONUTS page
  14. ↑ 14.0 14.1 14.2 14.3 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 GONUTS page
  15. ↑ 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 GONUTS page
  16. ↑ Wang, L et al. (1998) FtsI and FtsW are localized to the septum in Escherichia coli. J. Bacteriol. 180 2810-6 PubMed GONUTS page
  17. ↑ Pla, J et al. (1991) Preferential cytoplasmic location of FtsZ, a protein essential for Escherichia coli septation. Mol. Microbiol. 5 1681-6 PubMed GONUTS page
  18. ↑ 18.0 18.1 de Boer, P et al. (1992) The essential bacterial cell-division protein FtsZ is a GTPase. Nature 359 254-6 PubMed GONUTS page
  19. ↑ 19.0 19.1 RayChaudhuri, D & Park, JT (1992) Escherichia coli cell-division gene ftsZ encodes a novel GTP-binding protein. Nature 359 251-4 PubMed GONUTS page
  20. ↑ Varma, A & Young, KD (2009) In Escherichia coli, MreB and FtsZ direct the synthesis of lateral cell wall via independent pathways that require PBP 2. J. Bacteriol. 191 3526-33 PubMed GONUTS page
  21. ↑ Galli, E & Gerdes, K (2012) FtsZ-ZapA-ZapB interactome of Escherichia coli. J. Bacteriol. 194 292-302 PubMed GONUTS page
  22. ↑ Chen, JC et al. (1999) Septal localization of FtsQ, an essential cell division protein in Escherichia coli. J. Bacteriol. 181 521-30 PubMed GONUTS page
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