P61184
Gene name |
htpG |
Protein name |
Chaperone protein HtpG |
Names |
Heat shock protein HtpG, High temperature protein G |
Species |
Bdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIMB 9529 / HD100) |
KEGG Pathway |
bba:Bd1806 |
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 P61184
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P61184-F1 | Predicted | AlphaFoldDB |
No variants for P61184
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P61184 | |||||
No associated diseases with P61184
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
4 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 protein folding chaperone | Binding to a protein or a protein-containing complex to assist the protein folding process, driven by ATP hydrolysis. |
| unfolded protein binding | Binding to an unfolded protein. |
No GO annotations of biological process
| Name | Definition |
|---|---|
| No GO annotations for biological process |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MAKQVQNFNA | EIKQLLDIVI | HSLYSHKEIF | LRELLSNASD | AIDKLKFNSL | THPSLLPENW |
| 70 | 80 | 90 | 100 | 110 | 120 |
| QPAIRLEPNS | ETKTLKIIDN | GIGMTQEEVV | EFIGTIARSG | AKAFMQMNAE | MKTKPELIGQ |
| 130 | 140 | 150 | 160 | 170 | 180 |
| FGVGFYSAFM | VADRVTLHTQ | KAGSNDGTVW | ESMGDGTYSL | DSVPRPEGTG | TTITLHMKDF |
| 190 | 200 | 210 | 220 | 230 | 240 |
| KEEDEVQNFT | DKWVLKSLVK | KYSDFIAHPI | KMMGETEEET | LNSQKALWLK | SPSEVTKEEY |
| 250 | 260 | 270 | 280 | 290 | 300 |
| KEFYQHLTHD | WNEPLRTVHY | RAEGTMEFNA | LLYVPGKKPW | NYNMRDMEYG | LSLYIKRVFI |
| 310 | 320 | 330 | 340 | 350 | 360 |
| MADCKDLLPP | YLRFVKGLVD | SSDLSLNVSR | ELLQQDRQVT | QIRKNVTNKA | LSTLKDLLTK |
| 370 | 380 | 390 | 400 | 410 | 420 |
| ERSAYEDFWT | EFGATLKEGL | PSDAANKEKL | QDLLLFHSTS | SDKMTTMDEY | VARMKETQKD |
| 430 | 440 | 450 | 460 | 470 | 480 |
| IYYITGDSLS | QVSNSPYLEK | LKEKGFEVLL | LVDPVDEWVV | DALSEFKGKK | LQSIMREGLD |
| 490 | 500 | 510 | 520 | 530 | 540 |
| LDTAEEKQQK | EQEKKQAEVT | LKPVLESMKK | TLESDVKDVV | LSDRLTNTPA | CLVASSADPS |
| 550 | 560 | 570 | 580 | 590 | 600 |
| AHMQKLMAQM | GKEYAGQQVK | RIMEINPNHP | VFEKMLKASP | EQQTKWAEIL | YAQALLTEGS |
| 610 | 620 | ||||
| NLPDPVKFSQ | QIAELMVQAA | DSTKH |