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Literature summary for 3.4.23.52 extracted from
- Pilin processing follows a different temporal route than that of archaellins in Methanococcus maripaludis (2015), Life, 5, 85-101 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene eppA, recombinant expression of C-terminally FLAG- or His-tagged wild-type enzyme in Escherichia coli strain BL21(DE3) | Methanococcus maripaludis |
| gene flak, recombinant expression of C-terminally FLAG- or His-tagged wild-type enzyme in Escherichia coli strain BL21(DE3) | Methanococcus maripaludis |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | construction of deletion mutant strains DELTAeppA, DELTAeppADELTAaglB, and DELTAflakDELTAeppA. AglB is the oligosaccharyltransferase responsible for the terminal step in the N-linked glycosylation pathway. In the DELTAeppA mutant where the signal peptide is not be removed from the pilins, the proteins EpdE and EpdD migrate faster than the same proteins in wild-type cells, despite the fact the proteins are larger due to the additional signal peptide in the DELTAeppA strain. In the DELTAaglBDELTAeppA double mutant, the electrophoretic mobility of EpdE-FLAG and EpdD-FLAG is the same as it was in the DELTAeppA strain | Methanococcus maripaludis |
| additional information | construction of deletion mutant strains DELTAflak, DELTAflakDELTAaglB, and DELTAflakDELTAeppA. AglB is the oligosaccharyltransferase responsible for the terminal step in the N-linked glycosylation pathway | Methanococcus maripaludis |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| prearchaellin + H2O | Methanococcus maripaludis | - |
archaellin + ? | - |
? |  |
| prearchaellin + H2O | Methanococcus maripaludis Mm900 | - |
archaellin + ? | - |
? | |
| prepilin EpdA + H2O | Methanococcus maripaludis | cleavage sequence of pilins EpdA signal peptide is MFKRFNRG-QISFE | pilin EpdA + EpdA signal peptide | - |
? | |
| prepilin EpdA + H2O | Methanococcus maripaludis Mm900 | cleavage sequence of pilins EpdA signal peptide is MFKRFNRG-QISFE | pilin EpdA + EpdA signal peptide | - |
? | |
| prepilin EpdB + H2O | Methanococcus maripaludis | cleavage sequence of pilins EpdB signal peptide is MSKG-QVSVE | pilin EpdB + EpdB signal peptide | - |
? | |
| prepilin EpdB + H2O | Methanococcus maripaludis Mm900 | cleavage sequence of pilins EpdB signal peptide is MSKG-QVSVE | pilin EpdB + EpdB signal peptide | - |
? | |
| prepilin EpdC + H2O | Methanococcus maripaludis | cleavage sequence of pilins EpdC signal peptide is MIKMLQLPFNKKG-QVSFD | pilin EpdC + EpdC signal peptide | - |
? | |
| prepilin EpdC + H2O | Methanococcus maripaludis Mm900 | cleavage sequence of pilins EpdC signal peptide is MIKMLQLPFNKKG-QVSFD | pilin EpdC + EpdC signal peptide | - |
? | |
| prepilin EpdD + H2O | Methanococcus maripaludis | cleavage sequence of pilins EpdD signal peptide is MSVALKKFFSKRG-QLSLE | pilin EpdD + EpdD signal peptide | - |
? | |
| prepilin EpdD + H2O | Methanococcus maripaludis Mm900 | cleavage sequence of pilins EpdD signal peptide is MSVALKKFFSKRG-QLSLE | pilin EpdD + EpdD signal peptide | - |
? | |
| prepilin EpdE + H2O | Methanococcus maripaludis | cleavage sequence of pilins EpdE signal peptide is MKFLEKLTSKKG-QIAME | pilin EpdE + EpdE signal peptide | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Methanococcus maripaludis | - |
- |
- |
| Methanococcus maripaludis Mm900 | - |
- |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| glycoprotein | EpdE is a glycoprotein with multiple sites occupied by an N-linked glycan | Methanococcus maripaludis |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| prearchaellin + H2O | - |
Methanococcus maripaludis | archaellin + ? | - |
? | |
| prearchaellin + H2O | - |
Methanococcus maripaludis Mm900 | archaellin + ? | - |
? | |
| prepilin EpdA + H2O | cleavage sequence of pilins EpdA signal peptide is MFKRFNRG-QISFE | Methanococcus maripaludis | pilin EpdA + EpdA signal peptide | - |
? | |
| prepilin EpdA + H2O | cleavage sequence of pilins EpdA signal peptide is MFKRFNRG-QISFE | Methanococcus maripaludis Mm900 | pilin EpdA + EpdA signal peptide | - |
? | |
| prepilin EpdB + H2O | cleavage sequence of pilins EpdB signal peptide is MSKG-QVSVE | Methanococcus maripaludis | pilin EpdB + EpdB signal peptide | - |
? | |
| prepilin EpdB + H2O | cleavage sequence of pilins EpdB signal peptide is MSKG-QVSVE | Methanococcus maripaludis Mm900 | pilin EpdB + EpdB signal peptide | - |
? | |
| prepilin EpdC + H2O | cleavage sequence of pilins EpdC signal peptide is MIKMLQLPFNKKG-QVSFD | Methanococcus maripaludis | pilin EpdC + EpdC signal peptide | - |
? | |
| prepilin EpdC + H2O | cleavage sequence of pilins EpdC signal peptide is MIKMLQLPFNKKG-QVSFD | Methanococcus maripaludis Mm900 | pilin EpdC + EpdC signal peptide | - |
? | |
| prepilin EpdD + H2O | cleavage sequence of pilins EpdD signal peptide is MSVALKKFFSKRG-QLSLE | Methanococcus maripaludis | pilin EpdD + EpdD signal peptide | - |
? | |
| prepilin EpdD + H2O | cleavage sequence of pilins EpdD signal peptide is MSVALKKFFSKRG-QLSLE | Methanococcus maripaludis Mm900 | pilin EpdD + EpdD signal peptide | - |
? | |
| prepilin EpdE + H2O | cleavage sequence of pilins EpdE signal peptide is MKFLEKLTSKKG-QIAME | Methanococcus maripaludis | pilin EpdE + EpdE signal peptide | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 15000-17000, recombinant EpdE from purified pili, SDS-PAGE | Methanococcus maripaludis |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| EppA | - |
Methanococcus maripaludis |
| FlaK | - |
Methanococcus maripaludis |
| peptidase-like enzyme | - |
Methanococcus maripaludis |
| Prepilin peptidase | - |
Methanococcus maripaludis |
| signal peptidase III | - |
Methanococcus maripaludis |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | FlaK can only process archaellins and EppA only pilins | Methanococcus maripaludis |
| evolution | in Methanococcus maripaludis, the pilins have their own dedicated prepilin peptidase, EppA, which cleaves the signal peptide from pilins but not archaellins. This is in contrast to other studied Archaea which have a single prepilin peptidase-like enzyme, PibD, that cleaves all type IV pilin-like proteins, including archaellins, pilins and sugar binding proteins. Pilins in the organism are encoded by five genes, epdA-E. FlaK can only process archaellins and EppA only pilins | Methanococcus maripaludis |
| additional information | in Methanococcus maripaludis, the archaella are composed of three structural glycoproteins (the archaellins, FlaB1, FlaB2 and FlaB3) that are all modified at multiple positions with an N-linked tetrasaccharide | Methanococcus maripaludis |
| physiological function | Methanococcus maripaludis has two different surface appendages: type IV-like pili and archaella. Both structures are believed to be assembled using a bacterial type IV pilus mechanism. Each structure is composed of multiple subunits, either pilins or archaellins. Both pilins and archaellins are made initially as preproteins with type IV pilin-like signal peptides, which must be removed by a prepilin peptidase-like enzyme. This enzyme is FlaK for archaellins and EppA for pilins. Both archaella and archaeal type IV pili are assembled from structural proteins synthesized initially as preproteins with a class III (type IV pilin-like) signal peptide which is subsequently cleaved by a dedicated prepilin peptidase-like enzyme (signal peptidase III) | Methanococcus maripaludis |
| physiological function | Methanococcus maripaludis has two different surface appendages: type IV-like pili and archaella. Both structures are believed to be assembled using a bacterial type IV pilus mechanism. Each structure is composed of multiple subunits, either pilins or archaellins. Both pilins and archaellins are made initially as preproteins with type IV pilin-like signal peptides, which must be removed by a prepilin peptidase-like enzyme. This enzyme is FlaK for archaellins and EppA for pilins. The Epd pili of Methanococcus maripaludis are less numerous and thinner than archaella. Prepilin peptidase EppA cleaves the signal peptide from pilins but not archaellins | Methanococcus maripaludis |
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