Protein profile

PA4243

preprotein translocase subunit SecY

Genome: NC_002516.2

Gene: secY PA4243 Structure source: AlphaFold UniProt Q9HWF5
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Amino acids 442
Annotations 8
Features 57
PDB binders 3
Druggability 0.83

Overview

Basic information about this protein and its source genome.

Accession
PA4243
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
secY PA4243
Status
annotated
Amino acids
442
Structure source
AlphaFold
GO
GO:0031522 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. GO:0005886 The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. GO:0008320 Enables the transfer of a protein from one side of a membrane to the other. GO:0005048 Binding to a signal sequence, a specific peptide sequence found on protein precursors or mature proteins that dictates where the mature protein is localized. GO:0043952 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. GO:0006616 The process during cotranslational membrane targeting wherein proteins move across a membrane. SRP and its receptor initiate the transfer of the nascent chain across the endoplasmic reticulum (ER) membrane; they then dissociate from the chain, which is transferred to a set of transmembrane proteins, collectively called the translocon. Once the nascent chain translocon complex is assembled, the elongating chain passes directly from the large ribosomal subunit into the centers of the translocon, a protein-lined channel within the membrane. The growing chain is never exposed to the cytosol and does not fold until it reaches the ER lumen.

Target profile

Computed evidence for target prioritization.

Human off-target
No hit
Gut microbiome off-target
hit
Essential (DEG)
Y
Localization
CytoplasmicMembrane

Selected Druggability evidence

Selected Druggability is the FPocket score chosen for ranking using the curated structure priority. The 3D viewer may show a different loaded structure, so its visible pockets can differ.

FPocket 0.83
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

8 GO

Gene Ontology (GO)

8
  • GO:0031522 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.
  • GO:0005886 The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
  • GO:0008320 Enables the transfer of a protein from one side of a membrane to the other.
  • GO:0005048 Binding to a signal sequence, a specific peptide sequence found on protein precursors or mature proteins that dictates where the mature protein is localized.
  • GO:0043952 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.
  • GO:0006616 The process during cotranslational membrane targeting wherein proteins move across a membrane. SRP and its receptor initiate the transfer of the nascent chain across the endoplasmic reticulum (ER) membrane; they then dissociate from the chain, which is transferred to a set of transmembrane proteins, collectively called the translocon. Once the nascent chain translocon complex is assembled, the elongating chain passes directly from the large ribosomal subunit into the centers of the translocon, a protein-lined channel within the membrane. The growing chain is never exposed to the cytosol and does not fold until it reaches the ER lumen.
  • GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it.
  • GO:0015031 The directed movement of proteins into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.

Sequence Features

Domain/signature hits from InterPro and related databases.

57 records
Show feature table
Start End DB Term Name
74 97 Phobius TRANSMEMBRANE Region of a membrane-bound protein predicted to be embedded in the membrane.
305 327 TMHMM TMhelix Region of a membrane-bound protein predicted to be embedded in the membrane.
333 367 Phobius CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
1 19 Phobius CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
199 209 Phobius NON_CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
181 198 Phobius TRANSMEMBRANE Region of a membrane-bound protein predicted to be embedded in the membrane.
291 309 Phobius NON_CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
268 290 TMHMM TMhelix Region of a membrane-bound protein predicted to be embedded in the membrane.
363 382 TMHMM TMhelix Region of a membrane-bound protein predicted to be embedded in the membrane.
138 148 Phobius NON_CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
210 232 Phobius TRANSMEMBRANE Region of a membrane-bound protein predicted to be embedded in the membrane.
98 117 Phobius CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
74 96 TMHMM TMhelix Region of a membrane-bound protein predicted to be embedded in the membrane.
414 442 Phobius CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
20 38 Phobius TRANSMEMBRANE Region of a membrane-bound protein predicted to be embedded in the membrane.
122 144 TMHMM TMhelix Region of a membrane-bound protein predicted to be embedded in the membrane.
39 73 Phobius NON_CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
178 200 TMHMM TMhelix Region of a membrane-bound protein predicted to be embedded in the membrane.
210 232 TMHMM TMhelix Region of a membrane-bound protein predicted to be embedded in the membrane.
21 424 NCBIfam TIGR00967 preprotein translocase subunit SecY
21 424 InterPro IPR002208 SecY/SEC61-alpha family
13 424 Gene3D G3DSA:1.10.3370.10 SecY subunit domain
13 424 InterPro IPR023201 SecY domain superfamily
386 408 TMHMM TMhelix Region of a membrane-bound protein predicted to be embedded in the membrane.
75 94 ProSitePatterns PS00755 Protein secY signature 1.
75 94 InterPro IPR030659 SecY conserved site
170 180 Phobius CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
389 393 Phobius NON_CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
394 413 Phobius TRANSMEMBRANE Region of a membrane-bound protein predicted to be embedded in the membrane.
310 332 Phobius TRANSMEMBRANE Region of a membrane-bound protein predicted to be embedded in the membrane.
74 94 PRINTS PR00303 Preprotein translocase SecY subunit signature
115 138 PRINTS PR00303 Preprotein translocase SecY subunit signature
175 198 PRINTS PR00303 Preprotein translocase SecY subunit signature
267 286 PRINTS PR00303 Preprotein translocase SecY subunit signature
310 332 PRINTS PR00303 Preprotein translocase SecY subunit signature
365 383 PRINTS PR00303 Preprotein translocase SecY subunit signature
149 174 PRINTS PR00303 Preprotein translocase SecY subunit signature
22 40 PRINTS PR00303 Preprotein translocase SecY subunit signature
397 415 PRINTS PR00303 Preprotein translocase SecY subunit signature
9 428 Hamap MF_01465 Protein translocase subunit SecY [secY].
9 428 InterPro IPR026593 Protein translocase subunit SecY
149 171 TMHMM TMhelix Region of a membrane-bound protein predicted to be embedded in the membrane.
15 419 SUPERFAMILY SSF103491 Preprotein translocase SecY subunit
15 419 InterPro IPR023201 SecY domain superfamily
75 412 Pfam PF00344 SecY
75 412 InterPro IPR002208 SecY/SEC61-alpha family
8 436 PIRSF PIRSF004557 SecY_Sec61alpha
8 436 InterPro IPR002208 SecY/SEC61-alpha family
7 424 FunFam G3DSA:1.10.3370.10:FF:000001 Preprotein translocase subunit SecY
118 137 Phobius TRANSMEMBRANE Region of a membrane-bound protein predicted to be embedded in the membrane.
20 426 PANTHER PTHR10906 SECY/SEC61-ALPHA FAMILY MEMBER
20 426 InterPro IPR002208 SecY/SEC61-alpha family
21 43 TMHMM TMhelix Region of a membrane-bound protein predicted to be embedded in the membrane.
269 290 Phobius TRANSMEMBRANE Region of a membrane-bound protein predicted to be embedded in the membrane.
233 268 Phobius CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
149 169 Phobius TRANSMEMBRANE Region of a membrane-bound protein predicted to be embedded in the membrane.
368 388 Phobius TRANSMEMBRANE Region of a membrane-bound protein predicted to be embedded in the membrane.

3D Structure

Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; predicted models typically cover the full protein.

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Structural evidence

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Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.

Entry Method Resolution Chain Coverage Links Status
AlphaFold PA4243
AlphaFold — — full sequence — Viewing
Pocket details FPocket · P2Rank — toggle visibility and zoom from here, or open full viewer

Pockets (FPOCKET)

Showing top-ranked FPocket candidates by druggability. Druggability is color-coded: high (0.7 or higher), medium (0.4 to 0.69), low (below 0.4).

FPOCKET Sticks Spheres Surfaces Druggability Labels Zoom Positions
2 0.83
1 0.722

Ligand evidence

Ligands grouped by evidence source. PDB ligands keep the source crystal visible, and loaded crystals can be opened directly in the structure viewer.

53 records

Structural evidence inferred from similar proteins. The source crystal indicates where the ligand was observed; the UniProt column identifies the homologous protein carrying that ligand.

Show only:
Ligand Source crystal UniProt (homolog) MW · LogP · TPSA Lipinski PAINS SMILES
BEF
5EUL
A4IJK8 66.0 Da LogP 0.88 TPSA 0.0 ✓ Ro5 ✓ Clean [Be-](F)(F)F
OLC
5AWW
Q5SHQ8 356.5 Da LogP 4.92 TPSA 66.8 ✓ Ro5 ✓ Clean CCCCCCCC\C=C/CCCCCCCC(=O)OC[C@@H](CO)O
PGV
6ITC
A4IJK8 749.0 Da LogP 10.45 TPSA 148.8 2 viol. ✓ Clean CCCCCCCCCCCCCCCC(=O)OC[C@H](CO[P@](=O)(O)OC[C@H…

PDB and ChEMBL records on this protein are shown in full. ChEMBL records from similar proteins are capped at the top 100 per protein (by pchembl) and ZINC at the top 50 (Tanimoto ≥ 0.5). ADME columns are descriptor-based screening flags, not experimental toxicity results.