B0S3K9
Gene name |
secA |
Protein name |
Protein translocase subunit SecA |
Names |
|
Species |
Finegoldia magna (strain ATCC 29328 / DSM 20472 / WAL 2508) (Peptostreptococcus magnus) |
KEGG Pathway |
fma:FMG_1531 |
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 B0S3K9
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-B0S3K9-F1 | Predicted | AlphaFoldDB |
No variants for B0S3K9
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for B0S3K9 | |||||
No associated diseases with B0S3K9
7 regional properties for B0S3K9
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | SecA DEAD-like, N-terminal | 2 - 392 | IPR011115 |
| domain | SecA Wing/Scaffold | 712 - 925 | IPR011116 |
| domain | SecA, preprotein cross-linking domain | 231 - 348 | IPR011130 |
| domain | Helicase superfamily 1/2, ATP-binding domain | 92 - 250 | IPR014001 |
| domain | SecA motor DEAD | 1 - 714 | IPR014018 |
| conserved_site | SecA conserved site | 492 - 507 | IPR020937 |
| domain | SecA, C-terminal helicase domain | 410 - 684 | 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 |
| MGVFESIFGS | ANKKELKKIE | PIIKKIESYD | KSMQQLSDDE | LKHKTVEFKE | RLKNGETLDD |
| 70 | 80 | 90 | 100 | 110 | 120 |
| ILPEAFAVVR | EASYRVLGMK | QYRVQLIGGV | VLHQGRIAEM | KTGEGKTLVA | TLPAYLNALS |
| 130 | 140 | 150 | 160 | 170 | 180 |
| GKGVHVVTVN | DYLAKRDKEW | MGKVHEFLGL | TVGVIVYGLD | NDERRENYAC | DITYGTNNQY |
| 190 | 200 | 210 | 220 | 230 | 240 |
| GFDYLRDNMV | IYKKDKVQRG | LNFAIVDEVD | SILIDEARTP | LIISGQGDES | TDMYMRANMF |
| 250 | 260 | 270 | 280 | 290 | 300 |
| ANGLTGRIMD | PEEDKPDIFD | REFKDETVDF | LVDEKRKTAS | LTEVGTRKAE | EYFGVENLSD |
| 310 | 320 | 330 | 340 | 350 | 360 |
| PNNMELAHHI | NQALKANNTM | KRDIDYVVKD | DEILIVDEFT | GRIMEGRRYS | DGLHQAIEAK |
| 370 | 380 | 390 | 400 | 410 | 420 |
| EGVEVKSESK | TLATVTFQNY | FRMYNKLSGM | TGTAKTEEAE | FNEIYKMDVV | EIPTNKPVAR |
| 430 | 440 | 450 | 460 | 470 | 480 |
| VDEQDRVYIN | ENAKFNAIVE | EIKEIHKTGQ | PILVGTISIE | VSERLSNLLK | KNGIKHDVLN |
| 490 | 500 | 510 | 520 | 530 | 540 |
| AKQHEREAEI | VAQAGMFDKV | TIATNMAGRG | TDILLGGNPD | FMAKHDMKKQ | GYGDYVIESL |
| 550 | 560 | 570 | 580 | 590 | 600 |
| DSFLPSTDEE | LVAARNVYNE | LHKKYKKMTD | ENKKKVLEVG | GLYIIGTERH | ESRRIDNQLR |
| 610 | 620 | 630 | 640 | 650 | 660 |
| GRSGRQGDPG | RSRFFVSLGD | NLMRLFGGET | IQKYAESGKF | PEDEPMEFRT | ITKAIERAQT |
| 670 | 680 | 690 | 700 | 710 | 720 |
| KVESNNFGIR | KNVLKYDDVM | NAQRKVIYTE | RDKVLDGEDM | HESIVAMIKD | IISNAIDTYC |
| 730 | 740 | 750 | 760 | 770 | 780 |
| QDPKSENWEM | EALMTYLNTF | IPEGTLDLTR | LNSYNKKTFT | DYVIQKALEV | YNAKEEAIGK |
| 790 | 800 | 810 | 820 | 830 | 840 |
| EKFREIERVI | LLMVVDRKWM | DHIDAMDQLR | QGIGLRAFGQ | QDPVRAYNNE | GFEMFEDMNH |
| 850 | 860 | 870 | 880 | 890 | 900 |
| SIKEDTVRGM | FNVQPVEEIE | RKQVAHETSA | TGGEEEINKP | VVKGKKIGRN | DPCPCGSGKK |
| YKNCCGKNR |