Q55700
Gene name |
ftsH2 (slr0228) |
Protein name |
ATP-dependent zinc metalloprotease FtsH 2 |
Names |
|
Species |
Synechocystis sp (strain PCC 6803 / Kazusa) |
KEGG Pathway |
syn:slr0228 |
EC number |
|
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for Q55700
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q55700-F1 | Predicted | AlphaFoldDB |
No variants for Q55700
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q55700 | |||||
No associated diseases with Q55700
6 regional properties for Q55700
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Peptidase M41 | 422 - 610 | IPR000642 |
| domain | AAA+ ATPase domain | 204 - 343 | IPR003593 |
| domain | ATPase, AAA-type, core | 208 - 339 | IPR003959 |
| conserved_site | ATPase, AAA-type, conserved site | 311 - 329 | IPR003960 |
| domain | Peptidase M41, FtsH extracellular | 9 - 105 | IPR011546 |
| domain | AAA ATPase, AAA+ lid domain | 364 - 401 | IPR041569 |
Functions
3 GO annotations of cellular component
| Name | Definition |
|---|---|
| integral component of membrane | The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane. |
| thylakoid | A membranous cellular structure that bears the photosynthetic pigments in plants, algae, and cyanobacteria. In cyanobacteria thylakoids are of various shapes and are attached to, or continuous with, the plasma membrane. In eukaryotes they are flattened, membrane-bounded disk-like structures located in the chloroplasts; in the chloroplasts of higher plants the thylakoids form dense stacks called grana. Isolated thylakoid preparations can carry out photosynthetic electron transport and the associated phosphorylation. |
| thylakoid membrane | The pigmented membrane of any thylakoid. |
5 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| ATP hydrolysis activity | Catalysis of the reaction: ATP + H2O = ADP + H+ phosphate. ATP hydrolysis is used in some reactions as an energy source, for example to catalyze a reaction or drive transport against a concentration gradient. |
| ATP-dependent peptidase activity | Catalysis of the hydrolysis of peptide bonds, driven by ATP hydrolysis. |
| metalloendopeptidase activity | Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions. |
| zinc ion binding | Binding to a zinc ion (Zn). |
3 GO annotations of biological process
| Name | Definition |
|---|---|
| photosystem II repair | Proteolysis of the damaged D1 protein and re-assembly of a new D1 subunit in the photosystem II following photoinhibition. |
| protein catabolic process | The chemical reactions and pathways resulting in the breakdown of a protein by the destruction of the native, active configuration, with or without the hydrolysis of peptide bonds. |
| proteolysis | The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MKFSWRTALL | WSLPLLVVGF | FFWQGSFGGA | DANLGSNTAN | TRMTYGRFLE | YVDAGRITSV |
| 70 | 80 | 90 | 100 | 110 | 120 |
| DLYENGRTAI | VQVSDPEVDR | TLRSRVDLPT | NAPELIARLR | DSNIRLDSHP | VRNNGMVWGF |
| 130 | 140 | 150 | 160 | 170 | 180 |
| VGNLIFPVLL | IASLFFLFRR | SSNMPGGPGQ | AMNFGKSKAR | FQMDAKTGVM | FDDVAGIDEA |
| 190 | 200 | 210 | 220 | 230 | 240 |
| KEELQEVVTF | LKQPERFTAV | GAKIPKGVLL | VGPPGTGKTL | LAKAIAGEAG | VPFFSISGSE |
| 250 | 260 | 270 | 280 | 290 | 300 |
| FVEMFVGVGA | SRVRDLFKKA | KENAPCLIFI | DEIDAVGRQR | GAGIGGGNDE | REQTLNQLLT |
| 310 | 320 | 330 | 340 | 350 | 360 |
| EMDGFEGNTG | IIIIAATNRP | DVLDSALMRP | GRFDRQVMVD | APDYSGRKEI | LEVHARNKKL |
| 370 | 380 | 390 | 400 | 410 | 420 |
| APEVSIDSIA | RRTPGFSGAD | LANLLNEAAI | LTARRRKSAI | TLLEIDDAVD | RVVAGMEGTP |
| 430 | 440 | 450 | 460 | 470 | 480 |
| LVDSKSKRLI | AYHEVGHAIV | GTLLKDHDPV | QKVTLIPRGQ | AQGLTWFTPN | EEQGLTTKAQ |
| 490 | 500 | 510 | 520 | 530 | 540 |
| LMARIAGAMG | GRAAEEEVFG | DDEVTTGAGG | DLQQVTEMAR | QMVTRFGMSN | LGPISLESSG |
| 550 | 560 | 570 | 580 | 590 | 600 |
| GEVFLGGGLM | NRSEYSEEVA | TRIDAQVRQL | AEQGHQMARK | IVQEQREVVD | RLVDLLIEKE |
| 610 | 620 | ||||
| TIDGEEFRQI | VAEYAEVPVK | EQLIPQL |