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BACSU:FTSH
Contents
| Species (Taxon ID) | Bacillus subtilis (strain 168). (224308) | |
| Gene Name(s) | ftsH (ECO:0000255 with HAMAP-Rule:MF_01458) | |
| Protein Name(s) | ATP-dependent zinc metalloprotease FtsH (ECO:0000255 with HAMAP-Rule:MF_01458)
Cell division protease FtsH | |
| External Links | ||
| UniProt | P37476 | |
| EMBL | D26185 AL009126 | |
| PIR | E69627 | |
| RefSeq | NP_387950.1 | |
| ProteinModelPortal | P37476 | |
| SMR | P37476 | |
| IntAct | P37476 | |
| MINT | MINT-8365816 | |
| STRING | 224308.BSU00690 | |
| MEROPS | M41.009 | |
| PaxDb | P37476 | |
| EnsemblBacteria | CAB11845 | |
| GeneID | 938094 | |
| KEGG | bsu:BSU00690 | |
| PATRIC | 18971613 | |
| GenoList | BSU00690 | |
| eggNOG | COG0465 | |
| HOGENOM | HOG000217276 | |
| InParanoid | P37476 | |
| KO | K03798 | |
| OMA | AGGYVIM | |
| OrthoDB | EOG6PKFBJ | |
| PhylomeDB | P37476 | |
| BioCyc | BSUB:BSU00690-MONOMER | |
| Proteomes | UP000001570 | |
| GO | GO:0030428 GO:0016021 GO:0005886 GO:0005524 GO:0016887 GO:0004222 GO:0008233 GO:0008270 GO:0007049 GO:0051301 GO:0030163 GO:0043934 | |
| Gene3D | 3.40.50.300 | |
| HAMAP | MF_01458 | |
| InterPro | IPR003593 IPR003959 IPR003960 IPR005936 IPR027417 IPR011546 IPR000642 | |
| Pfam | PF00004 PF06480 PF01434 | |
| SMART | SM00382 | |
| SUPFAM | SSF52540 | |
| TIGRFAMs | TIGR01241 | |
| PROSITE | PS00674 | |
Annotations
| Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|---|---|
| GO:0006113 |
fermentation |
ECO:0000315 |
P |
Figure 5B: Mutant strains of ftsH did not grow anaerobically by fermentation. |
complete | |||||
| GO:0006970 |
response to osmotic stress |
ECO:0000315 |
P |
Figure 4: Growth of the ftsH mutant was limited when the bacteria grew in medium that contained 7% NaCl. Wild type cultures experienced a lag followed by a resumption of normal growth. |
complete | |||||
| GO:0019332 |
aerobic respiration, using nitrite as electron donor |
ECO:0000315 |
P |
Figure 4B. Mutant strains of ftsH did not grow anaerobically by nitrate respiration. |
complete | |||||
| GO:0004556 |
alpha-amylase activity |
ECO:0000315 |
F |
Figure 7A: the alpha-amylase activity increased in wild type ftsH strain, whereas the alpha-amylase activity decreased in the mutant strain. |
complete | |||||
| GO:0004291 |
subtilisin activity |
ECO:0000315 |
F |
Figure 7B: Mutant ftsH strain limits the activity of subtilisin, whereas the wild type does not. |
complete | |||||
|
involved_in |
GO:0043934 |
sporulation |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0030428 |
cell septum |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0030163 |
protein catabolic process |
ECO:0000314 |
direct assay evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
enables |
GO:0008233 |
peptidase activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0030163 |
protein catabolic process |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
PANTHER:PTN000554354 |
P |
Seeded From UniProt |
complete | ||
|
involved_in |
GO:0006508 |
proteolysis |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
EcoGene:EG11506 |
P |
Seeded From UniProt |
complete | ||
|
part_of |
GO:0005886 |
plasma membrane |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
PANTHER:PTN000554354 |
C |
Seeded From UniProt |
complete | ||
|
enables |
GO:0004176 |
ATP-dependent peptidase activity |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
EcoGene:EG11506 |
F |
Seeded From UniProt |
complete | ||
|
enables |
GO:0004222 |
metalloendopeptidase activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
InterPro:IPR000642 |
F |
Seeded From UniProt |
complete | ||
|
enables |
GO:0005524 |
ATP binding |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
InterPro:IPR000642 |
F |
Seeded From UniProt |
complete | ||
|
involved_in |
GO:0006508 |
proteolysis |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
|
enables |
GO:0008270 |
zinc ion binding |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0016020 |
membrane |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0016021 |
integral component of membrane |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
|
enables |
GO:0005524 |
ATP binding |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
UniRule:UR000078252 |
F |
Seeded From UniProt |
complete | ||
|
part_of |
GO:0005886 |
plasma membrane |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
UniRule:UR000078252 |
C |
Seeded From UniProt |
complete | ||
|
enables |
GO:0008270 |
zinc ion binding |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
UniRule:UR000078252 |
F |
Seeded From UniProt |
complete | ||
|
enables |
GO:0008233 |
peptidase activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
UniRule:UR000078252 |
F |
Seeded From UniProt |
complete | ||
|
enables |
GO:0016887 |
ATPase activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
UniRule:UR000078252 |
F |
Seeded From UniProt |
complete | ||
|
involved_in |
GO:0030163 |
protein catabolic process |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
UniRule:UR000078252 |
P |
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:0007049 |
cell cycle |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
P |
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 | |||
|
part_of |
GO:0005886 |
plasma membrane |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
|
enables |
GO:0046872 |
metal ion binding |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0006508 |
proteolysis |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
|
enables |
GO:0008233 |
peptidase activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0016021 |
integral component of 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 | |||
|
part_of |
GO:0016020 |
membrane |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
|
enables |
GO:0016787 |
hydrolase activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0008237 |
metallopeptidase activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ 1.0 1.1 Nakano, MM et al. (1997) Characterization of anaerobic fermentative growth of Bacillus subtilis: identification of fermentation end products and genes required for growth. J. Bacteriol. 179 6749-55 PubMed GONUTS page
- ↑ Lysenko, E et al. (1997) Characterization of the ftsH gene of Bacillus subtilis. Microbiology (Reading, Engl.) 143 ( Pt 3) 971-8 PubMed GONUTS page
- ↑ 3.0 3.1 3.2 Deuerling, E et al. (1997) The ftsH gene of Bacillus subtilis is involved in major cellular processes such as sporulation, stress adaptation and secretion. Mol. Microbiol. 23 921-33 PubMed GONUTS page
- ↑ Wehrl, W et al. (2000) The FtsH protein accumulates at the septum of Bacillus subtilis during cell division and sporulation. J. Bacteriol. 182 3870-3 PubMed GONUTS page
- ↑ 5.0 5.1 Kotschwar, M et al. (2004) Construction and analyses of mutant ftsH alleles of Bacillus subtilis involving the ATPase- and Zn-binding domains. Curr. Microbiol. 49 180-5 PubMed GONUTS page
- ↑ 6.0 6.1 6.2 6.3 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
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