3.4.23.52: preflagellin peptidase
This is an abbreviated version!
For detailed information about preflagellin peptidase, go to the full flat file.
Word Map on EC 3.4.23.52
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3.4.23.52
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preflagellins
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methanococcus
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flagellins
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prepilins
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voltae
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flagellation
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flak
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maripaludis
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methanogen
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archaeon
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flagella
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pilins
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non-motile
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glass
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glycans
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sulfolobus
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iv-like
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unprocessed
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n-linked
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cotranscribed
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pilus-like
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non-flagellated
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preproteins
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12-amino-acid
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archaella
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synthesis
- 3.4.23.52
- preflagellins
- methanococcus
- flagellins
- prepilins
- voltae
-
flagellation
-
flak
- maripaludis
-
methanogen
- archaeon
-
flagella
- pilins
-
non-motile
-
glass
- glycans
-
sulfolobus
-
iv-like
-
unprocessed
-
n-linked
-
cotranscribed
-
pilus-like
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non-flagellated
- preproteins
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12-amino-acid
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archaella
- synthesis
Reaction
Cleaves the signal peptide of 3 to 12 amino acids from the N-terminal of preflagellin, usually at Arg-Gly-/- or Lys-Gly-/-, to release flagellin. =
Synonyms
EppA, FlaK, peptidase-like enzyme, PibD, preflagellin peptidase, Prepilin peptidase, prepilin-like peptidase, RMVO00262, saci_0139, signal peptidase III, SPaseIII, SSO0131, type IV prepilin peptidase
ECTree
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General Information
General Information on EC 3.4.23.52 - preflagellin peptidase
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evolution
physiological function
additional information
evolution
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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
evolution
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FlaK can only process archaellins and EppA only pilins
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evolution
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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
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the enzyme plays an essential role in flagellation
physiological function
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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)
physiological function
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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
physiological function
type IV prepilin peptidase PibD processes flagellin/pilin precursors, that are essential for the biogenesis and function of the archaellum and other cell surface structures in Haloferax volcanii
physiological function
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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)
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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
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physiological function
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the enzyme plays an essential role in flagellation
-
physiological function
-
type IV prepilin peptidase PibD processes flagellin/pilin precursors, that are essential for the biogenesis and function of the archaellum and other cell surface structures in Haloferax volcanii
-
-
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
additional information
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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
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