B1GZK7
Gene name |
ftsH |
Protein name |
ATP-dependent zinc metalloprotease FtsH |
Names |
|
Species |
Endomicrobium trichonymphae |
KEGG Pathway |
rsd:TGRD_206 |
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 B1GZK7
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-B1GZK7-F1 | Predicted | AlphaFoldDB |
No variants for B1GZK7
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for B1GZK7 | |||||
No associated diseases with B1GZK7
5 regional properties for B1GZK7
2 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. |
| plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
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). |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| 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 |
| MKKSNPWFVF | FWITLLVIVL | MFINFARQGG | NEVELEYSQF | KQHIKAGSVF | KVLVAPGLIR |
| 70 | 80 | 90 | 100 | 110 | 120 |
| GQFRDGDGVF | KRFKTVPMDD | PNLVKDMEDN | KVLEFSATEK | SGWLGSLLLN | WGPVVLLILF |
| 130 | 140 | 150 | 160 | 170 | 180 |
| CFWMMRGMSM | GNKQAMSFGK | TKAKLAVGAS | KKITFKDVAG | CDEAKEELQE | LIEFLKDPAR |
| 190 | 200 | 210 | 220 | 230 | 240 |
| FQKLGGKIPK | GVLLFGSPGT | GKTLLAKAVA | GEANVPFFSS | SGSEFVEMFV | GVGASRVRDL |
| 250 | 260 | 270 | 280 | 290 | 300 |
| FDHGRKSAPC | LLFIDEIDAV | GRHRFAGIGG | GHDEREQTLN | QLLVEMDGFD | SKEGVILIAA |
| 310 | 320 | 330 | 340 | 350 | 360 |
| TNRPDVLDPA | LLRPGRFDRQ | VIILSPDLKD | REEILGVHSK | KIRLDNDVNL | NVIARRTPGF |
| 370 | 380 | 390 | 400 | 410 | 420 |
| VGADLANLVN | EAALLAARNS | QNAVNMKNME | EAIDRILAGP | QRKSRLMSDK | EKNIIAYHEA |
| 430 | 440 | 450 | 460 | 470 | 480 |
| GHTLVAKFLP | SADPVHKVSI | IPRGPALGYT | LQLPEEDKYL | TSKSELLDKL | SILFGGRVAE |
| 490 | 500 | 510 | 520 | 530 | 540 |
| ELVFSEITTG | AQNDISKATG | IAMRMVTEFG | MSDKIGPMAL | QRPNEEVFLG | RDISRDARHS |
| 550 | 560 | 570 | 580 | 590 | 600 |
| GKTSELIDEE | VKNIIYSSKS | RASKIIKDNV | SILNKIVSYL | LERENLSGED | IDKIIKGEEL |
| 610 | 620 | 630 | |||
| APLSESSSVD | EETKKKSTVE | KKVINEKVII | S |