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BACSU:FTSZ

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Contents

Species (Taxon ID) Bacillus subtilis. ([1])
Gene Name(s) ftsZ
Protein Name(s) Cell division protein ftsZ
External Links
EMBL M22630
AL009126
J05400
PIR I39848
RefSeq NP_389412.2
PDB 2RHH
2RHJ
2RHL
2RHO
2VAM
2VXY
PDBsum 2RHH
2RHJ
2RHL
2RHO
2VAM
2VXY
ProteinModelPortal P17865
SMR P17865
IntAct P17865
EnsemblBacteria EBBACT00000002972
GeneID 935971
GenomeReviews AL009126_GR
KEGG bsu:BSU15290
NMPDR fig|224308.1.peg.1531
GenoList BSU15290
GeneTree EBGT00050000002417
HOGENOM HBG478075
ProtClustDB PRK09330
BioCyc BSUB:BSU15290-MON
GO GO:0005737
GO:0043234
GO:0005525
GO:0003924
GO:0042802
GO:0000917
GO:0007049
GO:0051258
InterPro IPR020805
IPR000158
IPR008280
IPR018316
IPR003008
Gene3D G3DSA:3.30.1330.20
G3DSA:3.40.50.1440
Pfam PF00091
PRINTS PR00423
SMART SM00864
SM00865
SUPFAM SSF55307
SSF52490
TIGRFAMs TIGR00065
PROSITE PS01134
PS01135

Annotations

Qualifier GO ID GO term name Reference Evidence Code with/from Aspect Notes Status
GO:0000166

nucleotide binding

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0547

F

Seeded From UniProt

GO:0000917

barrier septum formation

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0717

P

Seeded From UniProt

GO:0003924

GTPase activity

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR008280

F

Seeded From UniProt

GO:0003924

GTPase activity

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR018316

F

Seeded From UniProt

GO:0005515

protein binding

PMID:16796675[1]

IPI: Inferred from Physical Interaction

UniProtKB:O31728

F

Seeded From UniProt

GO:0005515

protein binding

PMID:16796675[1]

IPI: Inferred from Physical Interaction

UniProtKB:O34894

F

Seeded From UniProt

GO:0005515

protein binding

PMID:16796675[1]

IPI: Inferred from Physical Interaction

UniProtKB:P28264

F

Seeded From UniProt

GO:0005515

protein binding

PMID:16796675[1]

IPI: Inferred from Physical Interaction

UniProtKB:P94542

F

Seeded From UniProt

GO:0005515

protein binding

PMID:17662947[2]

IPI: Inferred from Physical Interaction

UniProtKB:P54166

F

Seeded From UniProt

GO:0005525

GTP binding

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR000158

F

Seeded From UniProt

GO:0005525

GTP binding

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR008280

F

Seeded From UniProt

GO:0005525

GTP binding

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR018316

F

Seeded From UniProt

GO:0005525

GTP binding

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR020805

F

Seeded From UniProt

GO:0005525

GTP binding

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0342

F

Seeded From UniProt

GO:0005737

cytoplasm

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR000158

C

Seeded From UniProt

GO:0005737

cytoplasm

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR020805

C

Seeded From UniProt

GO:0005737

cytoplasm

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0963

C

Seeded From UniProt

GO:0005737

cytoplasm

GO_REF:0000023

IEA: Inferred from Electronic Annotation

SP_SL:SL-0086

C

Seeded From UniProt

GO:0006184

GTP catabolic process

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR008280

P

Seeded From UniProt

GO:0006184

GTP catabolic process

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR018316

P

Seeded From UniProt

GO:0007049

cell cycle

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0131

P

Seeded From UniProt

GO:0042802

identical protein binding

PMID:16796675[1]

IPI: Inferred from Physical Interaction

UniProtKB:P17865

F

Seeded From UniProt

GO:0043234

protein complex

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR003008

C

Seeded From UniProt

GO:0043234

protein complex

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR008280

C

Seeded From UniProt

GO:0043234

protein complex

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR018316

C

Seeded From UniProt

GO:0051258

protein polymerization

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR003008

P

Seeded From UniProt

GO:0051258

protein polymerization

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR008280

P

Seeded From UniProt

GO:0051258

protein polymerization

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR018316

P

Seeded From UniProt

GO:0051301

cell division

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0132

P

Seeded From UniProt

GO:0030428

cell septum

PMID:18573169[3]

IDA: Inferred from Direct Assay

C

Fig. 1

complete

GO:0051301

cell division

PMID:18573169[3]

IMP: Inferred from Mutant Phenotype

P

Fig. 2

complete

GO:0043234

protein binding

PMID:10747015[4]

IDA: Inferred from Direct Assay

F

figure 5

complete

GO:0051258

protein polymerization

PMID:20711458[5]

IDA: Inferred from Direct Assay

P

Figure 2

complete

GO:0000917

barrier septum assembly

PMID:22457634[6]

IEP: Inferred from Expression Pattern

P

Figure 2 shows FtsZ overproduction reduces the delay in Z ring assembly at midcell in the noc minCD double mutant.

complete

Notes

References

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

  1. 1.0 1.1 1.2 1.3 1.4 Ishikawa S et al. (2006) A new FtsZ-interacting protein, YlmF, complements the activity of FtsA during progression of cell division in Bacillus subtilis. Mol Microbiol 60: 1364-80 PubMed GONUTS page
  2. Weart RB et al. (2007) A metabolic sensor governing cell size in bacteria. Cell 130: 335-47 PubMed GONUTS page
  3. 3.0 3.1 Fukushima T et al. (2008) A sensor histidine kinase co-ordinates cell wall architecture with cell division in Bacillus subtilis. Mol Microbiol 69: 621-32 PubMed GONUTS page
  4. Lucet I et al. (2000) Direct interaction between the cell division protein FtsZ and the cell differentiation protein SpoIIE. EMBO J 19: 1467-75 PubMed GONUTS page
  5. de Oliveira IF et al. (2010) Characterization of ftsZ mutations that render Bacillus subtilis resistant to MinC. PLoS One 5: e12048 PubMed GONUTS page
  6. Rodrigues CD & Harry EJ (2012) The Min system and nucleoid occlusion are not required for identifying the division site in Bacillus subtilis but ensure its efficient utilization. PLoS Genet 8: e1002561 PubMed GONUTS page
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