P28366
Gene name |
secA |
Protein name |
Protein translocase subunit SecA |
Names |
|
Species |
Bacillus subtilis (strain 168) |
KEGG Pathway |
bsu:BSU35300 |
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
14 structures for P28366
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 1M6N | X-ray | 270 A | A | 1-802 | PDB |
| 1M74 | X-ray | 300 A | A | 1-802 | PDB |
| 1TF2 | X-ray | 290 A | A | 1-841 | PDB |
| 1TF5 | X-ray | 218 A | A | 1-841 | PDB |
| 2IBM | X-ray | 320 A | A/B | 1-780 | PDB |
| 3DL8 | X-ray | 750 A | A/B | 1-779 | PDB |
| 3IQM | X-ray | 340 A | A | 1-802 | PDB |
| 3IQY | X-ray | 330 A | A | 1-841 | PDB |
| 3JV2 | X-ray | 250 A | A/B | 1-780 | PDB |
| 5EUL | X-ray | 370 A | A | 1-780 | PDB |
| 6ITC | EM | 345 A | A | 1-780 | PDB |
| 7XHA | EM | 335 A | A | 1-778 | PDB |
| 7XHB | EM | 333 A | A | 1-778 | PDB |
| AF-P28366-F1 | Predicted | AlphaFoldDB |
No variants for P28366
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P28366 | |||||
No associated diseases with P28366
9 regional properties for P28366
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Helicase, C-terminal | 421 - 575 | IPR001650 |
| conserved_site | SEC-C motif | 821 - 839 | IPR004027 |
| domain | SecA DEAD-like, N-terminal | 5 - 382 | IPR011115 |
| domain | SecA Wing/Scaffold | 568 - 778 | IPR011116 |
| domain | SecA, preprotein cross-linking domain | 226 - 338 | IPR011130 |
| domain | Helicase superfamily 1/2, ATP-binding domain | 87 - 257 | IPR014001 |
| domain | SecA motor DEAD | 1 - 570 | IPR014018 |
| conserved_site | SecA conserved site | 480 - 495 | IPR020937 |
| domain | SecA, C-terminal helicase domain | 400 - 540 | 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 | |
4 GO annotations of cellular component
| Name | Definition |
|---|---|
| cell envelope Sec protein transport complex | A transmembrane protein complex involved in the translocation of proteins across the cytoplasmic membrane. In Gram-negative bacteria, Sec-translocated proteins are subsequently secreted via the type II, IV, or V secretion systems. Sec complex components include SecA, D, E, F, G, Y and YajC. |
| cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
| integral component of plasma membrane | The component of the plasma 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. |
| membrane raft | Any of the small (10-200 nm), heterogeneous, highly dynamic, sterol- and sphingolipid-enriched membrane domains that compartmentalize cellular processes. Small rafts can sometimes be stabilized to form larger platforms through protein-protein and protein-lipid interactions. |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| ABC-type protein transporter 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(out) = ADP + phosphate + protein(in). |
| 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. |
4 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. |
| protein transport by the Sec complex | The process in which unfolded proteins are transported across the cytoplasmic membrane in Gram-positive and Gram-negative bacteria by the Sec complex, in a process involving proteolytic cleavage of an N-terminal signal peptide. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MLGILNKMFD | PTKRTLNRYE | KIANDIDAIR | GDYENLSDDA | LKHKTIEFKE | RLEKGATTDD |
| 70 | 80 | 90 | 100 | 110 | 120 |
| LLVEAFAVVR | EASRRVTGMF | PFKVQLMGGV | ALHDGNIAEM | KTGEGKTLTS | TLPVYLNALT |
| 130 | 140 | 150 | 160 | 170 | 180 |
| GKGVHVVTVN | EYLASRDAEQ | MGKIFEFLGL | TVGLNLNSMS | KDEKREAYAA | DITYSTNNEL |
| 190 | 200 | 210 | 220 | 230 | 240 |
| GFDYLRDNMV | LYKEQMVQRP | LHFAVIDEVD | SILIDEARTP | LIISGQAAKS | TKLYVQANAF |
| 250 | 260 | 270 | 280 | 290 | 300 |
| VRTLKAEKDY | TYDIKTKAVQ | LTEEGMTKAE | KAFGIDNLFD | VKHVALNHHI | NQALKAHVAM |
| 310 | 320 | 330 | 340 | 350 | 360 |
| QKDVDYVVED | GQVVIVDSFT | GRLMKGRRYS | EGLHQAIEAK | EGLEIQNESM | TLATITFQNY |
| 370 | 380 | 390 | 400 | 410 | 420 |
| FRMYEKLAGM | TGTAKTEEEE | FRNIYNMQVV | TIPTNRPVVR | DDRPDLIYRT | MEGKFKAVAE |
| 430 | 440 | 450 | 460 | 470 | 480 |
| DVAQRYMTGQ | PVLVGTVAVE | TSELISKLLK | NKGIPHQVLN | AKNHEREAQI | IEEAGQKGAV |
| 490 | 500 | 510 | 520 | 530 | 540 |
| TIATNMAGRG | TDIKLGEGVK | ELGGLAVVGT | ERHESRRIDN | QLRGRSGRQG | DPGITQFYLS |
| 550 | 560 | 570 | 580 | 590 | 600 |
| MEDELMRRFG | AERTMAMLDR | FGMDDSTPIQ | SKMVSRAVES | SQKRVEGNNF | DSRKQLLQYD |
| 610 | 620 | 630 | 640 | 650 | 660 |
| DVLRQQREVI | YKQRFEVIDS | ENLREIVENM | IKSSLERAIA | AYTPREELPE | EWKLDGLVDL |
| 670 | 680 | 690 | 700 | 710 | 720 |
| INTTYLDEGA | LEKSDIFGKE | PDEMLELIMD | RIITKYNEKE | EQFGKEQMRE | FEKVIVLRAV |
| 730 | 740 | 750 | 760 | 770 | 780 |
| DSKWMDHIDA | MDQLRQGIHL | RAYAQTNPLR | EYQMEGFAMF | EHMIESIEDE | VAKFVMKAEI |
| 790 | 800 | 810 | 820 | 830 | 840 |
| ENNLEREEVV | QGQTTAHQPQ | EGDDNKKAKK | APVRKVVDIG | RNAPCHCGSG | KKYKNCCGRT |
| E |