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ECOLI:FTSA
Contents
| Species (Taxon ID) | Escherichia coli (strain K12). (83333) | |
| Gene Name(s) | ftsA (synonyms: divA) | |
| Protein Name(s) | Cell division protein FtsA | |
| External Links | ||
| UniProt | P0ABH0 | |
| EMBL | K02668 M36531 X55034 U00096 AP009048 | |
| PIR | B23318 | |
| RefSeq | NP_414636.1 YP_488399.1 | |
| ProteinModelPortal | P0ABH0 | |
| SMR | P0ABH0 | |
| DIP | DIP-47983N | |
| IntAct | P0ABH0 | |
| STRING | 511145.b0094 | |
| PaxDb | P0ABH0 | |
| PRIDE | P0ABH0 | |
| EnsemblBacteria | AAC73205 BAB96662 | |
| GeneID | 12932892 944778 | |
| KEGG | ecj:Y75_p0093 eco:b0094 | |
| PATRIC | 32115293 | |
| EchoBASE | EB0335 | |
| EcoGene | EG10339 | |
| eggNOG | COG0849 | |
| HOGENOM | HOG000049205 | |
| InParanoid | P0ABH0 | |
| KO | K03590 | |
| OMA | AGGHTNY | |
| OrthoDB | EOG6TR0B6 | |
| PhylomeDB | P0ABH0 | |
| BioCyc | EcoCyc:EG10339-MONOMER ECOL316407:JW0092-MONOMER | |
| PRO | PR:P0ABH0 | |
| Proteomes | UP000000318 UP000000625 | |
| Genevestigator | P0ABH0 | |
| GO | GO:0032153 GO:0009898 GO:0005524 GO:0042802 GO:0007049 GO:0051301 GO:0008360 | |
| InterPro | IPR020823 IPR003494 | |
| Pfam | PF02491 | |
| PIRSF | PIRSF003101 | |
| SMART | SM00842 | |
| TIGRFAMs | TIGR01174 | |
Annotations
| Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|---|---|
| GO:0051301 |
cell division |
ECO:0000314 |
P |
Figure 3 shows the interactions of ftsA with lipid/membrane structures. Figure 3c specifically shows ionic strength of ftsA binding. |
complete | |||||
| GO:0051301 |
cell division |
other:PNAS April 1, 2003 vol. 100 no. 7 4197-4202 |
ECO:0000269 |
P |
Fig 3. Demonstrates colony growth on LB chloramphenicol plates without zipA indicating the prescence of FTsA is enough for cell division to by pass need for ZipA. |
complete | ||||
|
involved_in |
GO:0051301 |
cell division |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
EcoGene:EG10339 |
P |
Seeded From UniProt |
complete | ||
|
part_of |
GO:0032153 |
cell division site |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
EcoGene:EG10339 |
C |
Seeded From UniProt |
complete | ||
|
part_of |
GO:0009898 |
cytoplasmic side of plasma membrane |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
EcoGene:EG10339 |
C |
Seeded From UniProt |
complete | ||
|
enables |
GO:0042802 |
identical protein binding |
ECO:0000353 |
physical interaction evidence used in manual assertion |
F |
occurs_in:(GO:0005886) |
Seeded From UniProt |
complete | ||
|
enables |
GO:0042802 |
identical protein binding |
ECO:0000353 |
physical interaction evidence used in manual assertion |
F |
occurs_in:(GO:0005886) |
Seeded From UniProt |
complete | ||
|
enables |
GO:0042802 |
identical protein binding |
ECO:0000353 |
physical interaction evidence used in manual assertion |
F |
occurs_in:(GO:0005886) |
Seeded From UniProt |
complete | ||
|
enables |
GO:0042802 |
identical protein binding |
ECO:0000353 |
physical interaction evidence used in manual assertion |
F |
occurs_in:(GO:0005886) |
Seeded From UniProt |
complete | ||
|
involved_in |
GO:0051301 |
cell division |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0051301 |
cell division |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0032153 |
cell division site |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
|
enables |
GO:0042802 |
identical protein binding |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0009898 |
cytoplasmic side of plasma membrane |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0005829 |
cytosol |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
|
enables |
GO:0005524 |
ATP binding |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0051301 |
cell division |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0009898 |
cytoplasmic side of plasma membrane |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
UniRule:UR000184764 |
C |
Seeded From UniProt |
complete | ||
|
involved_in |
GO:0043093 |
FtsZ-dependent cytokinesis |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
UniRule:UR000184764 |
P |
Seeded From UniProt |
complete | ||
|
part_of |
GO:0032153 |
cell division site |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
UniRule:UR000184764 |
C |
Seeded From UniProt |
complete | ||
|
involved_in |
GO:0007049 |
cell cycle |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0016020 |
membrane |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0005886 |
plasma membrane |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
UniProtKB-KW:KW-0997 |
C |
Seeded From UniProt |
complete | ||
|
involved_in |
GO:0051301 |
cell division |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ Martos, A et al. (2012) Isolation, characterization and lipid-binding properties of the recalcitrant FtsA division protein from Escherichia coli. PLoS ONE 7 e39829 PubMed GONUTS page
- ↑ 2.0 2.1 2.2 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
- ↑ 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
- ↑ Shiomi, D & Margolin, W (2008) Compensation for the loss of the conserved membrane targeting sequence of FtsA provides new insights into its function. Mol. Microbiol. 67 558-69 PubMed GONUTS page
- ↑ 5.0 5.1 Shiomi, D & Margolin, W (2007) Dimerization or oligomerization of the actin-like FtsA protein enhances the integrity of the cytokinetic Z ring. Mol. Microbiol. 66 1396-415 PubMed GONUTS page
- ↑ Karimova, G et al. (2005) Interaction network among Escherichia coli membrane proteins involved in cell division as revealed by bacterial two-hybrid analysis. J. Bacteriol. 187 2233-43 PubMed GONUTS page
- ↑ 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 GONUTS page
- ↑ Ricard, M & Hirota, Y (1973) Process of cellular division in Escherichia coli: physiological study on thermosensitive mutants defective in cell division. J. Bacteriol. 116 314-22 PubMed GONUTS page
- ↑ Pla, J et al. (1990) The native form of FtsA, a septal protein of Escherichia coli, is located in the cytoplasmic membrane. J. Bacteriol. 172 5097-102 PubMed GONUTS page
- ↑ Lopez-Campistrous, A et al. (2005) Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth. Mol. Cell Proteomics 4 1205-9 PubMed GONUTS page
- ↑ Beuria, TK et al. (2009) Adenine nucleotide-dependent regulation of assembly of bacterial tubulin-like FtsZ by a hypermorph of bacterial actin-like FtsA. J. Biol. Chem. 284 14079-86 PubMed GONUTS page
