Protein profile

PA0768

signal peptidase I

Genome: NC_002516.2

Gene: lepB PA0768 Structure source: AlphaFold UniProt Q9I5G7
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Amino acids 284
Annotations 9
Features 29
PDB binders 1

Overview

Basic information about this protein and its source genome.

Accession
PA0768
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
lepB PA0768
Status
annotated
Amino acids
284
Structure source
AlphaFold
EC
3.4.21.89
GO
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:0008233 Catalysis of the hydrolysis of a peptide bond. A peptide bond is a covalent bond formed when the carbon atom from the carboxyl group of one amino acid shares electrons with the nitrogen atom from the amino group of a second amino acid. GO:0004252 Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine). GO:0009003 An endopeptidase that cleaves a hydrophobic, N-terminal signal or leader sequences from mitochondrial, secreted and periplasmic proteins. GO:0006465 OBSOLETE. The proteolytic removal of a signal peptide from a protein during or after transport to a specific location in the cell. GO:0008236 Catalysis of the hydrolysis of peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine).

Target profile

Computed evidence for target prioritization.

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

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 8 GO

Enzyme Commission (EC)

1

Gene Ontology (GO)

8
  • 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:0008233 Catalysis of the hydrolysis of a peptide bond. A peptide bond is a covalent bond formed when the carbon atom from the carboxyl group of one amino acid shares electrons with the nitrogen atom from the amino group of a second amino acid.
  • GO:0004252 Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine).
  • GO:0009003 An endopeptidase that cleaves a hydrophobic, N-terminal signal or leader sequences from mitochondrial, secreted and periplasmic proteins.
  • GO:0006465 OBSOLETE. The proteolytic removal of a signal peptide from a protein during or after transport to a specific location in the cell.
  • GO:0008236 Catalysis of the hydrolysis of peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine).
  • GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it.
  • GO:0006508 The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.

Sequence Features

Domain/signature hits from InterPro and related databases.

29 records
Show feature table
Start End DB Term Name
145 157 ProSitePatterns PS00760 Signal peptidases I lysine active site.
145 157 InterPro IPR019757 Peptidase S26A, signal peptidase I, lysine active site
62 80 Phobius TRANSMEMBRANE Region of a membrane-bound protein predicted to be embedded in the membrane.
216 235 PRINTS PR00727 Bacterial leader peptidase 1 (S26A) family signature
216 235 InterPro IPR000223 Peptidase S26A, signal peptidase I
143 155 PRINTS PR00727 Bacterial leader peptidase 1 (S26A) family signature
143 155 InterPro IPR000223 Peptidase S26A, signal peptidase I
79 95 PRINTS PR00727 Bacterial leader peptidase 1 (S26A) family signature
79 95 InterPro IPR000223 Peptidase S26A, signal peptidase I
29 61 Phobius CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
64 266 NCBIfam TIGR02227 signal peptidase I
64 266 InterPro IPR000223 Peptidase S26A, signal peptidase I
77 271 SUPERFAMILY SSF51306 LexA/Signal peptidase
77 271 InterPro IPR036286 LexA/Signal peptidase-like superfamily
88 95 ProSitePatterns PS00501 Signal peptidases I serine active site.
88 95 InterPro IPR019756 Peptidase S26A, signal peptidase I, serine active site
221 234 ProSitePatterns PS00761 Signal peptidases I signature 3.
221 234 InterPro IPR019758 Peptidase S26A, signal peptidase I, conserved site
1 5 Phobius NON_CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
82 259 CDD cd06530 S26_SPase_I
82 259 InterPro IPR019533 Peptidase S26
6 28 Phobius TRANSMEMBRANE Region of a membrane-bound protein predicted to be embedded in the membrane.
55 265 PANTHER PTHR43390 SIGNAL PEPTIDASE I
55 265 InterPro IPR000223 Peptidase S26A, signal peptidase I
5 27 TMHMM TMhelix Region of a membrane-bound protein predicted to be embedded in the membrane.
81 284 Phobius NON_CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
75 280 Gene3D G3DSA:2.10.109.10 Umud Fragment, subunit A
60 264 Pfam PF10502 Signal peptidase, peptidase S26
60 264 InterPro IPR019533 Peptidase S26

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 PA0768
AlphaFold — — full sequence — Viewing

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.

29 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
CZD
6B88
P00803 892.1 Da LogP 2.05 TPSA 282.9 3 viol. ✓ Clean [H]/N=C\CNC(=O)[C@@H]1Cc2ccc(c(c2)-c3cc(ccc3OCC…

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.