GONUTS has been updated to MW1.31 Most things seem to be working but be sure to report problems.

Have any questions? Please email us at ecoliwiki@gmail.com

BACSU:FTSZ

From GONUTS
Jump to: navigation, search
Species (Taxon ID) Bacillus subtilis (strain 168). (224308)
Gene Name(s) ftsZ (ECO:0000255 with HAMAP-Rule:MF_00909)
Protein Name(s) Cell division protein FtsZ (ECO:0000255 with HAMAP-Rule:MF_00909)
External Links
UniProt P17865
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
MINT MINT-126054
STRING 224308.BSU15290
BindingDB P17865
ChEMBL CHEMBL5690
PaxDb P17865
EnsemblBacteria CAB13402
GeneID 935971
KEGG bsu:BSU15290
PATRIC 18974863
GenoList BSU15290
eggNOG COG0206
HOGENOM HOG000049094
InParanoid P17865
KO K03531
OMA DSHANII
OrthoDB EOG6S7XZG
PhylomeDB P17865
BioCyc BSUB:BSU15290-MONOMER
EvolutionaryTrace P17865
Proteomes UP000001570
GO GO:0032153
GO:0030428
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:0030428

cell septum

PMID:18573169[1]

ECO:0000314

C

Fig. 1

complete
CACAO 2014

GO:0051301

cell division

PMID:18573169[1]

ECO:0000315

P

Fig. 2

complete
CACAO 2015

GO:0051258

protein polymerization

PMID:20711458[2]

ECO:0000314

P

Figure 2

complete
CACAO 4850

GO:0000917

barrier septum assembly

PMID:22457634[3]

ECO:0000270

P

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

complete

involved_in

GO:0051301

cell division

PMID:18573169[1]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0030428

cell septum

PMID:18573169[1]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

GO:0003924

GTPase activity

PMID:23577149[4]

ECO:0000314

F

supplement figure 6

complete
CACAO 8163

enables

GO:0003924

GTPase activity

PMID:23577149[4]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

GO:0005515

protein binding

PMID:23577149[4]

ECO:0000021

UniProtKB:Q01463


F

Figure 5

complete
CACAO 8164

involved_in

GO:0051301

cell division

PMID:21873635[5]

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[5]

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[5]

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[5]

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[5]

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:21630458[6]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P17865

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:21224850[7]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P17865

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:17662947[8]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P17865

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:16796675[9]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P17865

F

Seeded From UniProt

complete

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

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

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

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

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

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

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: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

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

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

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: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

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

edit table

Notes

References

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

  1. ↑ 1.0 1.1 1.2 1.3 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
  2. ↑ de Oliveira, IF et al. (2010) Characterization of ftsZ mutations that render Bacillus subtilis resistant to MinC. PLoS ONE 5 e12048 PubMed GONUTS page
  3. ↑ 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
  4. ↑ 4.0 4.1 4.2 Blasios, V et al. (2013) Genetic and biochemical characterization of the MinC-FtsZ interaction in Bacillus subtilis. PLoS ONE 8 e60690 PubMed GONUTS page
  5. ↑ 5.0 5.1 5.2 5.3 5.4 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  6. ↑ Marchadier, E et al. (2011) An expanded protein-protein interaction network in Bacillus subtilis reveals a group of hubs: Exploration by an integrative approach. Proteomics 11 2981-91 PubMed GONUTS page
  7. ↑ Gündoğdu, ME et al. (2011) Large ring polymers align FtsZ polymers for normal septum formation. EMBO J. 30 617-26 PubMed GONUTS page
  8. ↑ Weart, RB et al. (2007) A metabolic sensor governing cell size in bacteria. Cell 130 335-47 PubMed GONUTS page
  9. ↑ 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
Retrieved from "https://gowiki.tamu.edu/wiki/index.php?title=BACSU:FTSZ&oldid=5953016"