A1AM15
Gene name |
secA |
Protein name |
Protein translocase subunit SecA |
Names |
|
Species |
Pelobacter propionicus (strain DSM 2379 / NBRC 103807 / OttBd1) |
KEGG Pathway |
ppd:Ppro_0755 |
EC number |
7.4.2.8: Linked to the hydrolysis of a nucleoside triphosphate |
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 A1AM15
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-A1AM15-F1 | Predicted | AlphaFoldDB |
No variants for A1AM15
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for A1AM15 | |||||
No associated diseases with A1AM15
9 regional properties for A1AM15
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Helicase, C-terminal | 422 - 643 | IPR001650 |
| conserved_site | SEC-C motif | 878 - 896 | IPR004027 |
| domain | SecA DEAD-like, N-terminal | 6 - 402 | IPR011115 |
| domain | SecA Wing/Scaffold | 625 - 835 | IPR011116 |
| domain | SecA, preprotein cross-linking domain | 228 - 358 | IPR011130 |
| domain | Helicase superfamily 1/2, ATP-binding domain | 89 - 247 | IPR014001 |
| domain | SecA motor DEAD | 3 - 627 | IPR014018 |
| conserved_site | SecA conserved site | 500 - 515 | IPR020937 |
| domain | SecA, C-terminal helicase domain | 420 - 597 | IPR044722 |
Functions
| Description | ||
|---|---|---|
| EC Number | 7.4.2.8 | Linked to the hydrolysis of a nucleoside triphosphate |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| metal ion binding | Binding to a metal ion. |
| protein-exporting ATPase activity | Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + protein+(in) -> ADP + phosphate + protein+(out); drives the concomitant secretion of proteins. |
3 GO annotations of biological process
| Name | Definition |
|---|---|
| intracellular protein transmembrane transport | The directed movement of proteins in a cell, from one side of a membrane to another by means of some agent such as a transporter or pore. |
| protein import | The targeting and directed movement of proteins into a cell or organelle. Not all import involves an initial targeting event. |
| protein targeting | The process of targeting specific proteins to particular regions of the cell, typically membrane-bounded subcellular organelles. Usually requires an organelle specific protein sequence motif. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MFGSLVKKVF | GSKNEREIKK | LWPIVARINE | LEASISPLSD | EQLRDKTAEF | KERHGKGESL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| DALMPEAFAV | CREASKRVLG | MRHFDVQLIG | GMVLHSGKIS | EMKTGEGKTL | VATLPAYLNA |
| 130 | 140 | 150 | 160 | 170 | 180 |
| ISGKGVHVVT | VNDYLARRDS | EWMGRLYSFL | GLTVGVIVHG | VEDDQRRINY | AADITYGTNN |
| 190 | 200 | 210 | 220 | 230 | 240 |
| EFGFDYLRDN | MKFSLDDYVQ | RGFNFAIVDE | VDSILIDEAR | TPLIISGPTE | DSTDKYYVID |
| 250 | 260 | 270 | 280 | 290 | 300 |
| RIIPLLKKGE | VKEEEANTLS | GKRKLYTGDF | TIDEKAKSAT | LTEQGVLKVE | KLLKVDNLYD |
| 310 | 320 | 330 | 340 | 350 | 360 |
| PRNIEFLHHT | QQALRAHAMY | RRDVDYVVKD | GEVMIVDEFT | GRLMPGRRWS | DGLHQAIEAK |
| 370 | 380 | 390 | 400 | 410 | 420 |
| EGVTIENENQ | TLATITFQNY | FRMYKKLGGM | TGTADTEAEE | FHKIYKLDVV | VIPTNRPLLR |
| 430 | 440 | 450 | 460 | 470 | 480 |
| PDFPDVIYKT | EREKFGAVIQ | DIKEHYATGQ | PCLVGTISIE | KSEVLSELLK | REGIPHNVLN |
| 490 | 500 | 510 | 520 | 530 | 540 |
| AKQHEREAEI | VSQAGRLKAI | TIATNMAGRG | TDILLGGNAD | ALASQWRRAN | PEAGEEEYQA |
| 550 | 560 | 570 | 580 | 590 | 600 |
| ILKNYKTVCA | AEHDEVVRLG | GLHIIGTERH | ESRRIDNQLR | GRSGRQGDPG | SSRFYLSLED |
| 610 | 620 | 630 | 640 | 650 | 660 |
| DLLRIFGSER | VSKIMDFLKI | EEGEAITHAM | INKSIENAQK | KVEAHNFDIR | KHLIEYDDVM |
| 670 | 680 | 690 | 700 | 710 | 720 |
| NKQREVIYTQ | RREILGGQDI | RESFLEMLDE | TVEEIVASYA | IEKSPAEEWD | WQAINEAVFK |
| 730 | 740 | 750 | 760 | 770 | 780 |
| CFNLQFELPQ | DTMARLTPAG | LKEMLAEQAH | ALFAARVKEM | GDDLIDHLIK | VMMLQAIDTH |
| 790 | 800 | 810 | 820 | 830 | 840 |
| WKDHLLNIDH | LKEGIGLRGY | GQKDPKQEYK | KEAYELFMGL | IMRIREEVVE | RIFWVQLERP |
| 850 | 860 | 870 | 880 | 890 | |
| EEVEEIEEEQ | RSKKIVFNLS | EEEERVQEPA | RSNRVAGRND | PCPCGSGKKY | KKCCGK |