GONUTS has been updated to MW1.31 Most things seem to be working but be sure to report problems.
ECOLI:MIND
Contents
| Species (Taxon ID) | Escherichia coli (strain K12). (83333) | |
| Gene Name(s) | minD | |
| Protein Name(s) | Septum site-determining protein MinD
Cell division inhibitor MinD | |
| External Links | ||
| UniProt | P0AEZ3 | |
| EMBL | J03153 U00096 AP009048 | |
| PIR | B31877 | |
| RefSeq | NP_415693.1 YP_489442.1 | |
| PDB | 3Q9L 3R9I 3R9J | |
| PDBsum | 3Q9L 3R9I 3R9J | |
| ProteinModelPortal | P0AEZ3 | |
| SMR | P0AEZ3 | |
| DIP | DIP-35946N | |
| IntAct | P0AEZ3 | |
| STRING | 511145.b1175 | |
| SWISS-2DPAGE | P0AEZ3 | |
| PaxDb | P0AEZ3 | |
| PRIDE | P0AEZ3 | |
| EnsemblBacteria | AAC74259 BAA36009 | |
| GeneID | 12933874 945741 | |
| KEGG | ecj:Y75_p1147 eco:b1175 | |
| PATRIC | 32117594 | |
| EchoBASE | EB0592 | |
| EcoGene | EG10597 | |
| eggNOG | COG2894 | |
| HOGENOM | HOG000019419 | |
| InParanoid | P0AEZ3 | |
| KO | K03609 | |
| OMA | RNLDMIL | |
| OrthoDB | EOG6NPMB6 | |
| PhylomeDB | P0AEZ3 | |
| BioCyc | EcoCyc:EG10597-MONOMER ECOL316407:JW1164-MONOMER | |
| PRO | PR:P0AEZ3 | |
| Proteomes | UP000000318 UP000000625 | |
| Genevestigator | P0AEZ3 | |
| GO | GO:0005886 GO:0005524 GO:0016887 GO:0000918 | |
| Gene3D | 3.40.50.300 | |
| InterPro | IPR002586 IPR025501 IPR010223 IPR027417 | |
| Pfam | PF01656 | |
| PIRSF | PIRSF003092 | |
| SUPFAM | SSF52540 | |
| TIGRFAMs | TIGR01968 | |
Annotations
| Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|---|---|
| GO:0016887 |
ATPase activity |
ECO:0000314 |
F |
Purified MinD catalyzed the hydrolysis of ATP, as measured release of 32P1 from [_y-32P]ATP or by the formation of [ -P]ADP from [ct-32P]ATP. No [32P]AMP was produced from [a-32P]ATP, confirming the specificity of the reaction for the 3-'y pyrophosphoryl bond. The reaction showed Michaelis -Menten kinetics (Figure 5) with a Km of 40 ,tM and a Vmax of 2.1 nmol/mg/min. |
complete | |||||
| GO:0005886 |
plasma membrane |
ECO:0000315 |
C |
The effect is very similar to SulA in that minicells are still produced at the level that causes mild filamentation (Fig. (Fig.2).2). These results indicate that MinD is not absolutely required for MinC to distinguish internal Z rings from polar Z rings but that MinC has to be on the membrane to achieve this effect. On the other hand, a wild-type morphology can be readily achieved with MinC/MinD but not with MinC-MTS, suggesting that MinD plays other roles in addition to recruiting MinC to the membrane. |
complete | |||||
| GO:0000918 |
barrier septum site selection |
ECO:0000314 |
P |
FIG 3, midcell MinE rings result in detectable oscillation of GFP-MinD between periphery, inhibiting FtsZ assembly in aberrant locations |
complete | |||||
|
involved_in |
GO:0051782 |
negative regulation of cell division |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
EcoGene:EG10597 |
P |
Seeded From UniProt |
complete | ||
|
enables |
GO:0016887 |
ATPase activity |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
EcoGene:EG10597 |
F |
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:EG10597 |
C |
Seeded From UniProt |
complete | ||
|
part_of |
GO:0005886 |
plasma membrane |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
EcoGene:EG10597 |
C |
Seeded From UniProt |
complete | ||
|
part_of |
GO:0005829 |
cytosol |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
EcoGene:EG10597 |
C |
Seeded From UniProt |
complete | ||
|
enables |
GO:0005524 |
ATP binding |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
EcoGene:EG10597 |
F |
Seeded From UniProt |
complete | ||
|
enables |
GO:0016887 |
ATPase activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0005886 |
plasma membrane |
ECO:0000269 |
experimental 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 | |||
|
part_of |
GO:0060187 |
cell pole |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0060187 |
cell pole |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0051782 |
negative regulation of cell division |
ECO:0000314 |
direct assay 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 | |||
|
involved_in |
GO:0051301 |
cell division |
ECO:0000314 |
direct assay evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
enables |
GO:0042802 |
identical protein binding |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0042802 |
identical protein binding |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0031226 |
intrinsic component of plasma membrane |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
|
enables |
GO:0016887 |
ATPase activity |
ECO:0000314 |
direct assay 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:0009898 |
cytoplasmic side of plasma membrane |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0007059 |
chromosome segregation |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0005886 |
plasma membrane |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0005886 |
plasma membrane |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0005886 |
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 | |||
|
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 | |||
|
enables |
GO:0016887 |
ATPase activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0005886 |
plasma membrane |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
UniProtKB-KW:KW-1003 |
C |
Seeded From UniProt |
complete | ||
|
part_of |
GO:0016020 |
membrane |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
|
enables |
GO:0005524 |
ATP binding |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0000166 |
nucleotide binding |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
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 | |||
|
involved_in |
GO:0007049 |
cell cycle |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0000917 |
division septum assembly |
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.
- ↑ 1.0 1.1 1.2 1.3 1.4 1.5 1.6 1.7 de Boer, PA et al. (1991) The MinD protein is a membrane ATPase required for the correct placement of the Escherichia coli division site. EMBO J. 10 4371-80 PubMed GONUTS page
- ↑ Shen, B & Lutkenhaus, J (2011) Differences in MinC/MinD sensitivity between polar and internal Z rings in Escherichia coli. J. Bacteriol. 193 367-76 PubMed GONUTS page
- ↑ 3.0 3.1 3.2 Raskin, DM & de Boer, PA (1999) Rapid pole-to-pole oscillation of a protein required for directing division to the middle of Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 96 4971-6 PubMed GONUTS page
- ↑ 4.0 4.1 4.2 4.3 4.4 4.5 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
- ↑ 5.0 5.1 Rowland, SL et al. (2000) Membrane redistribution of the Escherichia coli MinD protein induced by MinE. J. Bacteriol. 182 613-9 PubMed GONUTS page
- ↑ 6.0 6.1 Hu, Z & Lutkenhaus, J (1999) Topological regulation of cell division in Escherichia coli involves rapid pole to pole oscillation of the division inhibitor MinC under the control of MinD and MinE. Mol. Microbiol. 34 82-90 PubMed GONUTS page
- ↑ Labie, C et al. (1990) Minicell-forming mutants of Escherichia coli: suppression of both DicB- and MinD-dependent division inhibition by inactivation of the minC gene product. J. Bacteriol. 172 5852-5 PubMed GONUTS page
- ↑ Hu, Z et al. (2003) Recruitment of MinC, an inhibitor of Z-ring formation, to the membrane in Escherichia coli: role of MinD and MinE. J. Bacteriol. 185 196-203 PubMed GONUTS page
- ↑ Szeto, J et al. (2001) Gonococcal MinD affects cell division in Neisseria gonorrhoeae and Escherichia coli and exhibits a novel self-interaction. J. Bacteriol. 183 6253-64 PubMed GONUTS page
- ↑ Wu, W et al. (2011) Determination of the structure of the MinD-ATP complex reveals the orientation of MinD on the membrane and the relative location of the binding sites for MinE and MinC. Mol. Microbiol. 79 1515-28 PubMed GONUTS page
- ↑ Di Ventura, B et al. (2013) Chromosome segregation by the Escherichia coli Min system. Mol. Syst. Biol. 9 686 PubMed GONUTS page
- ↑ Szeto, TH et al. (2002) Membrane localization of MinD is mediated by a C-terminal motif that is conserved across eubacteria, archaea, and chloroplasts. Proc. Natl. Acad. Sci. U.S.A. 99 15693-8 PubMed GONUTS page
- ↑ Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 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
