3.4.21.89: Signal peptidase I
This is an abbreviated version!
For detailed information about Signal peptidase I, go to the full flat file.
Word Map on EC 3.4.21.89
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3.4.21.89
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polyproteins
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lipoprotein
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preproteins
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cleavable
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foot-and-mouth
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unprocessed
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dyad
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membrane-spanning
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prolipoproteins
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translocons
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pilins
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uncleaved
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beta-lactamase
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drug development
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flavivirus
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ompa
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nonstructural
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cotranslationally
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co-translational
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sec-dependent
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globomycin
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presequence
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papain-like
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prepeptide
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polytopic
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oligonucleotide-directed
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ns2b
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signal-anchored
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pharmacology
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medicine
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analysis
- 3.4.21.89
- polyproteins
- lipoprotein
- preproteins
-
cleavable
- foot-and-mouth
-
unprocessed
-
dyad
-
membrane-spanning
- prolipoproteins
-
translocons
- pilins
-
uncleaved
- beta-lactamase
- drug development
- flavivirus
- ompa
-
nonstructural
-
cotranslationally
-
co-translational
-
sec-dependent
- globomycin
- presequence
-
papain-like
- prepeptide
-
polytopic
-
oligonucleotide-directed
- ns2b
-
signal-anchored
- pharmacology
- medicine
- analysis
Reaction
Cleavage of hydrophobic, N-terminal signal or leader sequences =
Synonyms
Bacterial leader peptidase 1, bacterial type I signal peptidase, big signal peptidase, canine signal peptidase complex, chloroplast processing peptidase, EC 3.4.99.36, Escherichia coli leader peptidase, Eukaryotic signal peptidase, Eukaryotic signal proteinase, hen oviduct signal peptidase, HOSP, imp1p, Leader peptidase, Leader peptidase I, Leader peptide hydrolase, Leader proteinase, LEP, LepB, PA1303, Pcp1, Peptidase, signal, Pilin leader peptidase, plastidic SPase I, plastidic SPase I 1, plastidic type I signal peptidase 1, Plsp1, Prokaryotic leader peptidase, Prokaryotic signal peptidase, Prokaryotic signal proteinase, Propeptidase, protease IV, Proteinase, eukaryotic signal, Proteinase, signal, PuIO prepilin peptidase, Rv2903c, SEC11, secretory protein 11, Signal peptidase, signal peptidase I, signal peptidase I-3, Signal peptidase IB, signal peptidase type I, Signal peptide hydrolase, Signal peptide peptidase, Signalase, Sip1, Sip2, Sip3, SipP (pTA1015), SipP (pTA1040), SipS, SipT, SipU, SipV, SipW, SipX, SipY, SipZ, SP, SP I, SP-I, SPase, Spase I, SPase I 1, SPase IB, SPaseI, SPC, Spc1, SPI, SPP, SpsB, thylakoidal processing peptidase, TPP, type I signal (leader) peptidase, type I signal peptidase, type I signal peptidase 1, type I signal peptidase Sec11a, type I signal peptidase Sec11b, type I SPase
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3.4.21.89 Signal peptidase IAdvanced search results
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General Information on EC 3.4.21.89 - Signal peptidase I
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
evolution
malfunction
metabolism
SPase may influence flagellar assembly and type IV secretion systems (T4SSs), as components of the translocation machinery itself are predicted to require SPase processing.79,80 For example, the T4SS mediates the direct transfer of proteins into target cells, but is perhaps best known for its role in the direct transfer of DNA, as this has been implicated as a primary means by which bacteria acquire foreign DNA leading to antibiotic resistance
physiological function
additional information
evolution
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bacterial type I signal peptidase is evolutionarily related to the penicillin-binding proteins (PBPs)
evolution
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bacterial type I signal peptidase is evolutionarily related to the penicillin-binding proteins (PBPs)
evolution
bacterial type I signal peptidase is evolutionarily related to the penicillin-binding proteins (PBPs)
evolution
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Escherichia coli and Bacillus subtilis primarily express a signal peptidase I contains a serine-lysine catalytic dyad, whilst those of archaeal and eukaryotic origin generally have a serine-histidine catalytic dyad
evolution
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Escherichia coli and Bacillus subtilis primarily express a signal peptidase I contains a serine-lysine catalytic dyad, whilst those of archaeal and eukaryotic origin generally have a serine-histidine catalytic dyad
evolution
Escherichia coli and Bacillus subtilis primarily express a signal peptidase I contains a serine-lysine catalytic dyad, whilst those of archaeal and eukaryotic origin generally have a serine-histidine catalytic dyad
evolution
Escherichia coli and Bacillus subtilis primarily express a signal peptidase I contains a serine-lysine catalytic dyad, whilst those of archaeal and eukaryotic origin generally have a serine-histidine catalytic dyad. Bacillus subtilis contains five chromosomally encoded signal peptidases
evolution
Escherichia coli and Bacillus subtilis primarily express a signal peptidase I that contains a serine-lysine catalytic dyad, whilst those of archaeal and eukaryotic origin generally have a serine-histidine catalytic dyad
evolution
evolutionary adaptation from the ribosome-dependent co-translational insertion to the chaperone-dependent post-translational transport of SPase I
evolution
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Escherichia coli and Bacillus subtilis primarily express a signal peptidase I contains a serine-lysine catalytic dyad, whilst those of archaeal and eukaryotic origin generally have a serine-histidine catalytic dyad. Bacillus subtilis contains five chromosomally encoded signal peptidases
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evolution
-
Escherichia coli and Bacillus subtilis primarily express a signal peptidase I contains a serine-lysine catalytic dyad, whilst those of archaeal and eukaryotic origin generally have a serine-histidine catalytic dyad
-
evolution
-
Escherichia coli and Bacillus subtilis primarily express a signal peptidase I contains a serine-lysine catalytic dyad, whilst those of archaeal and eukaryotic origin generally have a serine-histidine catalytic dyad
-
evolution
-
Escherichia coli and Bacillus subtilis primarily express a signal peptidase I contains a serine-lysine catalytic dyad, whilst those of archaeal and eukaryotic origin generally have a serine-histidine catalytic dyad
-
evolution
-
bacterial type I signal peptidase is evolutionarily related to the penicillin-binding proteins (PBPs)
-
evolution
-
bacterial type I signal peptidase is evolutionarily related to the penicillin-binding proteins (PBPs)
-
evolution
Yersinia pestis KIM+6
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bacterial type I signal peptidase is evolutionarily related to the penicillin-binding proteins (PBPs)
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malfunction
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potential consequences of SPase inhibition on bacterial virulence, overview. The antivirulence effects of inhibiting SPase are expected due to the many proteinaceous virulence factors that rely on SPase for processing into functional forms. SPase inhibition results in the accumulation of unprocessed proteins in the cytoplasmic membrane, which eventually causes it to lose its integrity and leads to cell death
malfunction
-
potential consequences of SPase inhibition on bacterial virulence, overview. The antivirulence effects of inhibiting SPase are expected due to the many proteinaceous virulence factors that rely on SPase for processing into functional forms. SPase inhibition results in the accumulation of unprocessed proteins in the cytoplasmic membrane, which eventually causes it to lose its integrity and leads to cell death
malfunction
-
potential consequences of SPase inhibition on bacterial virulence, overview. The antivirulence effects of inhibiting SPase are expected due to the many proteinaceous virulence factors that rely on SPase for processing into functional forms. SPase inhibition results in the accumulation of unprocessed proteins in the cytoplasmic membrane, which eventually causes it to lose its integrity and leads to cell death
malfunction
-
potential consequences of SPase inhibition on bacterial virulence, overview. The antivirulence effects of inhibiting SPase are expected due to the many proteinaceous virulence factors that rely on SPase for processing into functional forms. SPase inhibition results in the accumulation of unprocessed proteins in the cytoplasmic membrane, which eventually causes it to lose its integrity and leads to cell death
malfunction
-
potential consequences of SPase inhibition on bacterial virulence, overview. The antivirulence effects of inhibiting SPase are expected due to the many proteinaceous virulence factors that rely on SPase for processing into functional forms. SPase inhibition results in the accumulation of unprocessed proteins in the cytoplasmic membrane, which eventually causes it to lose its integrity and leads to cell death
malfunction
potential consequences of SPase inhibition on bacterial virulence, overview. The antivirulence effects of inhibiting SPase are expected due to the many proteinaceous virulence factors that rely on SPase for processing into functional forms. SPase inhibition results in the accumulation of unprocessed proteins in the cytoplasmic membrane, which eventually causes it to lose its integrity and leads to cell death
malfunction
-
potential consequences of SPase inhibition on bacterial virulence, overview. The antivirulence effects of inhibiting SPase are expected due to the many proteinaceous virulence factors that rely on SPase for processing into functional forms. SPase inhibition results in the accumulation of unprocessed proteins in the cytoplasmic membrane, which eventually causes it to lose its integrity and leads to cell death
malfunction
potential consequences of SPase inhibition on bacterial virulence, overview. The antivirulence effects of inhibiting SPase are expected due to the many proteinaceous virulence factors that rely on SPase for processing into functional forms. SPase inhibition results in the accumulation of unprocessed proteins in the cytoplasmic membrane, which eventually causes it to lose its integrity and leads to cell death
malfunction
potential consequences of SPase inhibition on bacterial virulence, overview. The antivirulence effects of inhibiting SPase are expected due to the many proteinaceous virulence factors that rely on SPase for processing into functional forms. SPase inhibition results in the accumulation of unprocessed proteins in the cytoplasmic membrane, which eventually causes it to lose its integrity and leads to cell death
malfunction
potential consequences of SPase inhibition on bacterial virulence, overview. The antivirulence effects of inhibiting SPase are expected due to the many proteinaceous virulence factors that rely on SPase for processing into functional forms. SPase inhibition results in the accumulation of unprocessed proteins in the cytoplasmic membrane, which eventually causes it to lose its integrity and leads to cell death
malfunction
potential consequences of SPase inhibition on bacterial virulence, overview. The antivirulence effects of inhibiting SPase are expected due to the many proteinaceous virulence factors that rely on SPase for processing into functional forms. SPase inhibition results in the accumulation of unprocessed proteins in the cytoplasmic membrane, which eventually causes it to lose its integrity and leads to cell death
malfunction
potential consequences of SPase inhibition on bacterial virulence, overview. The antivirulence effects of inhibiting SPase are expected due to the many proteinaceous virulence factors that rely on SPase for processing into functional forms. SPase inhibition results in the accumulation of unprocessed proteins in the cytoplasmic membrane, which eventually causes it to lose its integrity and leads to cell death
malfunction
potential consequences of SPase inhibition on bacterial virulence, overview. The antivirulence effects of inhibiting SPase are expected due to the many proteinaceous virulence factors that rely on SPase for processing into functional forms. SPase inhibition results in the accumulation of unprocessed proteins in the cytoplasmic membrane, which eventually causes it to lose its integrity and leads to cell death
malfunction
A0A1S0QR24
potential consequences of SPase inhibition on bacterial virulence, overview. The antivirulence effects of inhibiting SPase are expected due to the many proteinaceous virulence factors that rely on SPase for processing into functional forms. SPase inhibition results in the accumulation of unprocessed proteins in the cytoplasmic membrane, which eventually causes it to lose its integrity and leads to cell death
malfunction
potential consequences of SPase inhibition on bacterial virulence, overview. The antivirulence effects of inhibiting SPase are expected due to the many proteinaceous virulence factors that rely on SPase for processing into functional forms. SPase inhibition results in the accumulation of unprocessed proteins in the cytoplasmic membrane, which eventually causes it to lose its integrity and leads to cell death
malfunction
potential consequences of SPase inhibition on bacterial virulence, overview. The antivirulence effects of inhibiting SPase are expected due to the many proteinaceous virulence factors that rely on SPase for processing into functional forms. SPase inhibition results in the accumulation of unprocessed proteins in the cytoplasmic membrane, which eventually causes it to lose its integrity and leads to cell death
malfunction
-
potential consequences of SPase inhibition on bacterial virulence, overview. The antivirulence effects of inhibiting SPase are expected due to the many proteinaceous virulence factors that rely on SPase for processing into functional forms. SPase inhibition results in the accumulation of unprocessed proteins in the cytoplasmic membrane, which eventually causes it to lose its integrity and leads to cell death. Deletion of sipZ results in an almost complete loss of infectivity in a mouse model
malfunction
Staphylococcus aureus bacteria lacking the SPase I SpsB are viable and able to grow in vitro when overexpressing a native gene cassette encoding for a putative ABC transporter. This transporter apparently compensates for SpsB's essential function by mediating alternative cleavage of a subset of proteins at a site distinct from the SpsB-cleavage site, leading to SpsB-independent secretion
malfunction
the biofilm mutant, DELTASSA_0351, is deficient in type I signal peptidase (SPase), phenotype, overview. Proteomic analysis of mutant strain DELTASSA_0351, list of transcripts that are differentially regulated in DELTASSA_0351
malfunction
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potential consequences of SPase inhibition on bacterial virulence, overview. The antivirulence effects of inhibiting SPase are expected due to the many proteinaceous virulence factors that rely on SPase for processing into functional forms. SPase inhibition results in the accumulation of unprocessed proteins in the cytoplasmic membrane, which eventually causes it to lose its integrity and leads to cell death
-
malfunction
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the biofilm mutant, DELTASSA_0351, is deficient in type I signal peptidase (SPase), phenotype, overview. Proteomic analysis of mutant strain DELTASSA_0351, list of transcripts that are differentially regulated in DELTASSA_0351
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malfunction
-
potential consequences of SPase inhibition on bacterial virulence, overview. The antivirulence effects of inhibiting SPase are expected due to the many proteinaceous virulence factors that rely on SPase for processing into functional forms. SPase inhibition results in the accumulation of unprocessed proteins in the cytoplasmic membrane, which eventually causes it to lose its integrity and leads to cell death
-
malfunction
-
potential consequences of SPase inhibition on bacterial virulence, overview. The antivirulence effects of inhibiting SPase are expected due to the many proteinaceous virulence factors that rely on SPase for processing into functional forms. SPase inhibition results in the accumulation of unprocessed proteins in the cytoplasmic membrane, which eventually causes it to lose its integrity and leads to cell death
-
malfunction
-
potential consequences of SPase inhibition on bacterial virulence, overview. The antivirulence effects of inhibiting SPase are expected due to the many proteinaceous virulence factors that rely on SPase for processing into functional forms. SPase inhibition results in the accumulation of unprocessed proteins in the cytoplasmic membrane, which eventually causes it to lose its integrity and leads to cell death
-
malfunction
-
potential consequences of SPase inhibition on bacterial virulence, overview. The antivirulence effects of inhibiting SPase are expected due to the many proteinaceous virulence factors that rely on SPase for processing into functional forms. SPase inhibition results in the accumulation of unprocessed proteins in the cytoplasmic membrane, which eventually causes it to lose its integrity and leads to cell death
-
malfunction
-
potential consequences of SPase inhibition on bacterial virulence, overview. The antivirulence effects of inhibiting SPase are expected due to the many proteinaceous virulence factors that rely on SPase for processing into functional forms. SPase inhibition results in the accumulation of unprocessed proteins in the cytoplasmic membrane, which eventually causes it to lose its integrity and leads to cell death
-
malfunction
-
potential consequences of SPase inhibition on bacterial virulence, overview. The antivirulence effects of inhibiting SPase are expected due to the many proteinaceous virulence factors that rely on SPase for processing into functional forms. SPase inhibition results in the accumulation of unprocessed proteins in the cytoplasmic membrane, which eventually causes it to lose its integrity and leads to cell death
-
malfunction
-
potential consequences of SPase inhibition on bacterial virulence, overview. The antivirulence effects of inhibiting SPase are expected due to the many proteinaceous virulence factors that rely on SPase for processing into functional forms. SPase inhibition results in the accumulation of unprocessed proteins in the cytoplasmic membrane, which eventually causes it to lose its integrity and leads to cell death
-
malfunction
-
potential consequences of SPase inhibition on bacterial virulence, overview. The antivirulence effects of inhibiting SPase are expected due to the many proteinaceous virulence factors that rely on SPase for processing into functional forms. SPase inhibition results in the accumulation of unprocessed proteins in the cytoplasmic membrane, which eventually causes it to lose its integrity and leads to cell death
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physiological function
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bacterial SPases I play a key role in protein secretion as they are responsible for the cleavage of signal peptides from secreted proteins
physiological function
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Plsp1 is vital for proper thylakoid development in Arabidopsis thaliana chloroplasts. Plsp1 is also necessary for processing of an envelope protein, Toc75, and a thylakoid lumenal protein, OE33
physiological function
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SPase I is responsible for removing the signal peptide from secretory pre-proteins and releasing mature proteins to cellular or extra-cellular space. SPase I may have an important role in Leishmania infectivity, e.g. in differentiation and survival of amastigotes
physiological function
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the enzyme cleaves off the signal peptide from secreted proteins, making it essential for protein secretion, and hence for bacterial cell viability
physiological function
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deletion of membrane-bound signal peptidases SipX, SipY and SipZ and construction of SipX/SipY and SipY/SipZ double mutants. The amounts of listeriolysin O, phosphatidylcholine phospholipase C and zinc metalloproteinase Mpl in the extracellular milieu are significantly decreased upon inactivation of SipZ. For the majority of the Sec-secreted exoproteins identified, protein secretion is not affected by the inactivation of one or two of the signal peptidases
physiological function
gene is essential, and reduced lepB expression is detrimental to growth
physiological function
RNAi-mediated knockdown of the catalytic subunit gene results in high mortality. Sixty-nine per cent of dead nymphs died of abnormal moulting, corresponding to decreased activity of moulting fluid protease. Insects in the RNAi group experience a decline in food intake, and a decrease in the secretion of total protein and digestive enzymes from midgut tissues to the midgut lumen. The females produce fewer eggs and eggs with disrupted embryogenesis
physiological function
the gene is not essential for viability. Similar growth rates are observed for the PA1303 deletion mutant and the wild-type, and in stationary-phase cells no obvious changes in cell morphology are found. Chromosomal deletion mutation leads to the increased secretion of extracellular proteins, increased N-butanoyl homoserine lactone production and influences several quorum-sensing-controlled phenotypic traits, including swarming motility and the production of rhamnolipid and elastinolytic activity
physiological function
exported proteins require an N-terminal signal peptide to direct them from the cytoplasm to the periplasm. Once the protein has been translocated across the cytoplasmic membrane, the signal peptide is cleaved by a signal peptidase, allowing the remainder of the protein to fold into its mature state in the periplasm. Signal peptidase I (LepB) cleaves non-lipoproteins and recognises the sequence Ala-X-Ala. Amino acids present at the N-terminus of mature, exported proteins affect the efficiency at which the protein is exported
physiological function
involvement of signal peptidase I in Streptococcus sanguinis biofilm formation. Streptococcus sanguinis, a Gram-positive bacterium, is one of the most abundant species of the oral microbiota and it contributes to biofilm development in the oral cavity
physiological function
proteins that carry a type I signal peptide are released from their membrane anchored signal peptide by signal peptidase I (SPI). They can then remain in the periplasm, or be transported further. In Bacteroidetes, signal peptide cleavage exposes N-terminal glutamine residues in most signal peptidase I (SPI) substrates. The newly exposed glutamines are cyclized to pyroglutamate (also termed 5-oxoproline) residues. Porphyromonas gingivalis SPI substrates typically have a glutamine residue downstream of the SPI cleavage site. A Gln residue downstream of the SPI cleavage site affects RgpA, but not RgpB and Kgp gingipains secretion
physiological function
-
signal peptides direct proteins from the cytoplasm to the periplasm. These N-terminal peptides are cleaved upon entry to the periplasm by either signal peptidase I, or signal peptidase II for lipoproteins. Signal peptidase I is a serine protease that has either a serine-lysine or serine-histidine catalytic dyad present in the active site. The recognition site for signal peptide cleavage by signal peptidase I has been defined primarily by an Ala-X-Ala motif at the C-terminal end of the signal peptide, one amino acid away from the cleavage site
physiological function
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signal peptides direct proteins from the cytoplasm to the periplasm. These N-terminal peptides are cleaved upon entry to the periplasm by either signal peptidase I, or signal peptidase II for lipoproteins. Signal peptidase I is a serine protease that has either a serine-lysine or serine-histidine catalytic dyad present in the active site. The recognition site for signal peptide cleavage by signal peptidase I has been defined primarily by an Ala-X-Ala motif at the C-terminal end of the signal peptide, one amino acid away from the cleavage site
physiological function
signal peptides direct proteins from the cytoplasm to the periplasm. These N-terminal peptides are cleaved upon entry to the periplasm by either signal peptidase I, or signal peptidase II for lipoproteins. Signal peptidase I is a serine protease that has either a serine-lysine or serine-histidine catalytic dyad present in the active site. The recognition site for signal peptide cleavage by signal peptidase I has been defined primarily by an Ala-X-Ala motif at the C-terminal end of the signal peptide, one amino acid away from the cleavage site
physiological function
signal peptides direct proteins from the cytoplasm to the periplasm. These N-terminal peptides are cleaved upon entry to the periplasm by either signal peptidase I, or signal peptidase II for lipoproteins. Signal peptidase I is a serine protease that has either a serine-lysine or serine-histidine catalytic dyad present in the active site. The recognition site for signal peptide cleavage by signal peptidase I has been defined primarily by an Ala-X-Ala motif at the C-terminal end of the signal peptide, one amino acid away from the cleavage site
physiological function
signal peptides direct proteins from the cytoplasm to the periplasm. These N-terminal peptides are cleaved upon entry to the periplasm by either signal peptidase I, or signal peptidase II for lipoproteins. Signal peptidase I is a serine protease that has either a serine-lysine or serine-histidine catalytic dyad present in the active site. The recognition site for signal peptide cleavage by signal peptidase I has been defined primarily by an Ala-X-Ala motif at the C-terminal end of the signal peptide, one amino acid away from the cleavage site
physiological function
type I signal peptidase (SPase I) mediates the final step of bacterial secretion, by cleaving proteins at their signal peptide once they are translocated by the Sec or twin-arginine (Tat) translocon. SPase I is important for viability in multiple bacterial pathogens. SpsB cleavage of the signal (or leader) peptide allows protein release from the membrane. A potential distinct secretion system involving an ABC transporter in Staphylococcus aureus is able to bypass the nominal essentiality of SpsB, overview
physiological function
-
type I signal peptidase (SPase) is an essential part of the secretion apparatus. Its proteolytic activity is required to release proteins from their N-terminal leader sequence, which remain membrane bound after the preprotein translocates across the cytoplasmic membrane. Before the protein achieves its mature form, the Sec machinery recognizes the signal peptide and translocates the pre-protein across the cytoplasmic membrane, during which time the lipophilic region of the signal peptide becomes embedded in the cytoplasmic membrane. SPase then cleaves the signal peptide to release the protein. SPase also functions at the terminal step of the twin-arginine translocase (Tat) pathway. The Tat pathway is functionally similar to the Sec pathway, but it recognizes signal peptides containing a highly conserved R-R motif, and its pre-protein cargo fold prior to translocation across the cytoplasmic membrane. But SPase has also relevant biological functions outside of mediating secretion. SPase is required for virulence. SPase processes components of multimeric secretion systems. SPase plays an essential role in the assembly of multiple secretion systems through the processing of secretins, which are large, multimeric proteins that localize to the outer membrane
physiological function
-
type I signal peptidase (SPase) is an essential part of the secretion apparatus. Its proteolytic activity is required to release proteins from their N-terminal leader sequence, which remain membrane bound after the preprotein translocates across the cytoplasmic membrane. Before the protein achieves its mature form, the Sec machinery recognizes the signal peptide and translocates the pre-protein across the cytoplasmic membrane, during which time the lipophilic region of the signal peptide becomes embedded in the cytoplasmic membrane. SPase then cleaves the signal peptide to release the protein. SPase also functions at the terminal step of the twin-arginine translocase (Tat) pathway. The Tat pathway is functionally similar to the Sec pathway, but it recognizes signal peptides containing a highly conserved R-R motif, and its pre-protein cargo fold prior to translocation across the cytoplasmic membrane. But SPase has also relevant biological functions outside of mediating secretion. SPase is required for virulence. SPase processes components of multimeric secretion systems. SPase plays an essential role in the assembly of multiple secretion systems through the processing of secretins, which are large, multimeric proteins that localize to the outer membrane
physiological function
-
type I signal peptidase (SPase) is an essential part of the secretion apparatus. Its proteolytic activity is required to release proteins from their N-terminal leader sequence, which remain membrane bound after the preprotein translocates across the cytoplasmic membrane. Before the protein achieves its mature form, the Sec machinery recognizes the signal peptide and translocates the pre-protein across the cytoplasmic membrane, during which time the lipophilic region of the signal peptide becomes embedded in the cytoplasmic membrane. SPase then cleaves the signal peptide to release the protein. SPase also functions at the terminal step of the twin-arginine translocase (Tat) pathway. The Tat pathway is functionally similar to the Sec pathway, but it recognizes signal peptides containing a highly conserved R-R motif, and its pre-protein cargo fold prior to translocation across the cytoplasmic membrane. But SPase has also relevant biological functions outside of mediating secretion. SPase is required for virulence. SPase processes components of multimeric secretion systems. SPase plays an essential role in the assembly of multiple secretion systems through the processing of secretins, which are large, multimeric proteins that localize to the outer membrane
physiological function
-
type I signal peptidase (SPase) is an essential part of the secretion apparatus. Its proteolytic activity is required to release proteins from their N-terminal leader sequence, which remain membrane bound after the preprotein translocates across the cytoplasmic membrane. Before the protein achieves its mature form, the Sec machinery recognizes the signal peptide and translocates the pre-protein across the cytoplasmic membrane, during which time the lipophilic region of the signal peptide becomes embedded in the cytoplasmic membrane. SPase then cleaves the signal peptide to release the protein. SPase also functions at the terminal step of the twin-arginine translocase (Tat) pathway. The Tat pathway is functionally similar to the Sec pathway, but it recognizes signal peptides containing a highly conserved R-R motif, and its pre-protein cargo fold prior to translocation across the cytoplasmic membrane. But SPase has also relevant biological functions outside of mediating secretion. SPase is required for virulence. SPase processes components of multimeric secretion systems. SPase plays an essential role in the assembly of multiple secretion systems through the processing of secretins, which are large, multimeric proteins that localize to the outer membrane
physiological function
-
type I signal peptidase (SPase) is an essential part of the secretion apparatus. Its proteolytic activity is required to release proteins from their N-terminal leader sequence, which remain membrane bound after the preprotein translocates across the cytoplasmic membrane. Before the protein achieves its mature form, the Sec machinery recognizes the signal peptide and translocates the pre-protein across the cytoplasmic membrane, during which time the lipophilic region of the signal peptide becomes embedded in the cytoplasmic membrane. SPase then cleaves the signal peptide to release the protein. SPase also functions at the terminal step of the twin-arginine translocase (Tat) pathway. The Tat pathway is functionally similar to the Sec pathway, but it recognizes signal peptides containing a highly conserved R-R motif, and its pre-protein cargo fold prior to translocation across the cytoplasmic membrane. But SPase has also relevant biological functions outside of mediating secretion. SPase is required for virulence. SPase processes components of multimeric secretion systems. SPase plays an essential role in the assembly of multiple secretion systems through the processing of secretins, which are large, multimeric proteins that localize to the outer membrane
physiological function
type I signal peptidase (SPase) is an essential part of the secretion apparatus. Its proteolytic activity is required to release proteins from their N-terminal leader sequence, which remain membrane bound after the preprotein translocates across the cytoplasmic membrane. Before the protein achieves its mature form, the Sec machinery recognizes the signal peptide and translocates the pre-protein across the cytoplasmic membrane, during which time the lipophilic region of the signal peptide becomes embedded in the cytoplasmic membrane. SPase then cleaves the signal peptide to release the protein. SPase also functions at the terminal step of the twin-arginine translocase (Tat) pathway. The Tat pathway is functionally similar to the Sec pathway, but it recognizes signal peptides containing a highly conserved R-R motif, and its pre-protein cargo fold prior to translocation across the cytoplasmic membrane. But SPase has also relevant biological functions outside of mediating secretion. SPase is required for virulence. SPase processes components of multimeric secretion systems. SPase plays an essential role in the assembly of multiple secretion systems through the processing of secretins, which are large, multimeric proteins that localize to the outer membrane
physiological function
-
type I signal peptidase (SPase) is an essential part of the secretion apparatus. Its proteolytic activity is required to release proteins from their N-terminal leader sequence, which remain membrane bound after the preprotein translocates across the cytoplasmic membrane. Before the protein achieves its mature form, the Sec machinery recognizes the signal peptide and translocates the pre-protein across the cytoplasmic membrane, during which time the lipophilic region of the signal peptide becomes embedded in the cytoplasmic membrane. SPase then cleaves the signal peptide to release the protein. SPase also functions at the terminal step of the twin-arginine translocase (Tat) pathway. The Tat pathway is functionally similar to the Sec pathway, but it recognizes signal peptides containing a highly conserved R-R motif, and its pre-protein cargo fold prior to translocation across the cytoplasmic membrane. But SPase has also relevant biological functions outside of mediating secretion. SPase is required for virulence. SPase processes components of multimeric secretion systems. SPase plays an essential role in the assembly of multiple secretion systems through the processing of secretins, which are large, multimeric proteins that localize to the outer membrane
physiological function
type I signal peptidase (SPase) is an essential part of the secretion apparatus. Its proteolytic activity is required to release proteins from their N-terminal leader sequence, which remain membrane bound after the preprotein translocates across the cytoplasmic membrane. Before the protein achieves its mature form, the Sec machinery recognizes the signal peptide and translocates the pre-protein across the cytoplasmic membrane, during which time the lipophilic region of the signal peptide becomes embedded in the cytoplasmic membrane. SPase then cleaves the signal peptide to release the protein. SPase also functions at the terminal step of the twin-arginine translocase (Tat) pathway. The Tat pathway is functionally similar to the Sec pathway, but it recognizes signal peptides containing a highly conserved R-R motif, and its pre-protein cargo fold prior to translocation across the cytoplasmic membrane. But SPase has also relevant biological functions outside of mediating secretion. SPase is required for virulence. SPase processes components of multimeric secretion systems. SPase plays an essential role in the assembly of multiple secretion systems through the processing of secretins, which are large, multimeric proteins that localize to the outer membrane
physiological function
type I signal peptidase (SPase) is an essential part of the secretion apparatus. Its proteolytic activity is required to release proteins from their N-terminal leader sequence, which remain membrane bound after the preprotein translocates across the cytoplasmic membrane. Before the protein achieves its mature form, the Sec machinery recognizes the signal peptide and translocates the pre-protein across the cytoplasmic membrane, during which time the lipophilic region of the signal peptide becomes embedded in the cytoplasmic membrane. SPase then cleaves the signal peptide to release the protein. SPase also functions at the terminal step of the twin-arginine translocase (Tat) pathway. The Tat pathway is functionally similar to the Sec pathway, but it recognizes signal peptides containing a highly conserved R-R motif, and its pre-protein cargo fold prior to translocation across the cytoplasmic membrane. But SPase has also relevant biological functions outside of mediating secretion. SPase is required for virulence. SPase processes components of multimeric secretion systems. SPase plays an essential role in the assembly of multiple secretion systems through the processing of secretins, which are large, multimeric proteins that localize to the outer membrane
physiological function
type I signal peptidase (SPase) is an essential part of the secretion apparatus. Its proteolytic activity is required to release proteins from their N-terminal leader sequence, which remain membrane bound after the preprotein translocates across the cytoplasmic membrane. Before the protein achieves its mature form, the Sec machinery recognizes the signal peptide and translocates the pre-protein across the cytoplasmic membrane, during which time the lipophilic region of the signal peptide becomes embedded in the cytoplasmic membrane. SPase then cleaves the signal peptide to release the protein. SPase also functions at the terminal step of the twin-arginine translocase (Tat) pathway. The Tat pathway is functionally similar to the Sec pathway, but it recognizes signal peptides containing a highly conserved R-R motif, and its pre-protein cargo fold prior to translocation across the cytoplasmic membrane. But SPase has also relevant biological functions outside of mediating secretion. SPase is required for virulence. SPase processes components of multimeric secretion systems. SPase plays an essential role in the assembly of multiple secretion systems through the processing of secretins, which are large, multimeric proteins that localize to the outer membrane
physiological function
type I signal peptidase (SPase) is an essential part of the secretion apparatus. Its proteolytic activity is required to release proteins from their N-terminal leader sequence, which remain membrane bound after the preprotein translocates across the cytoplasmic membrane. Before the protein achieves its mature form, the Sec machinery recognizes the signal peptide and translocates the pre-protein across the cytoplasmic membrane, during which time the lipophilic region of the signal peptide becomes embedded in the cytoplasmic membrane. SPase then cleaves the signal peptide to release the protein. SPase also functions at the terminal step of the twin-arginine translocase (Tat) pathway. The Tat pathway is functionally similar to the Sec pathway, but it recognizes signal peptides containing a highly conserved R-R motif, and its pre-protein cargo fold prior to translocation across the cytoplasmic membrane. But SPase has also relevant biological functions outside of mediating secretion. SPase is required for virulence. SPase processes components of multimeric secretion systems. SPase plays an essential role in the assembly of multiple secretion systems through the processing of secretins, which are large, multimeric proteins that localize to the outer membrane
physiological function
type I signal peptidase (SPase) is an essential part of the secretion apparatus. Its proteolytic activity is required to release proteins from their N-terminal leader sequence, which remain membrane bound after the preprotein translocates across the cytoplasmic membrane. Before the protein achieves its mature form, the Sec machinery recognizes the signal peptide and translocates the pre-protein across the cytoplasmic membrane, during which time the lipophilic region of the signal peptide becomes embedded in the cytoplasmic membrane. SPase then cleaves the signal peptide to release the protein. SPase also functions at the terminal step of the twin-arginine translocase (Tat) pathway. The Tat pathway is functionally similar to the Sec pathway, but it recognizes signal peptides containing a highly conserved R-R motif, and its pre-protein cargo fold prior to translocation across the cytoplasmic membrane. But SPase has also relevant biological functions outside of mediating secretion. SPase is required for virulence. SPase processes components of multimeric secretion systems. SPase plays an essential role in the assembly of multiple secretion systems through the processing of secretins, which are large, multimeric proteins that localize to the outer membrane
physiological function
type I signal peptidase (SPase) is an essential part of the secretion apparatus. Its proteolytic activity is required to release proteins from their N-terminal leader sequence, which remain membrane bound after the preprotein translocates across the cytoplasmic membrane. Before the protein achieves its mature form, the Sec machinery recognizes the signal peptide and translocates the pre-protein across the cytoplasmic membrane, during which time the lipophilic region of the signal peptide becomes embedded in the cytoplasmic membrane. SPase then cleaves the signal peptide to release the protein. SPase also functions at the terminal step of the twin-arginine translocase (Tat) pathway. The Tat pathway is functionally similar to the Sec pathway, but it recognizes signal peptides containing a highly conserved R-R motif, and its pre-protein cargo fold prior to translocation across the cytoplasmic membrane. But SPase has also relevant biological functions outside of mediating secretion. SPase is required for virulence. SPase processes components of multimeric secretion systems. SPase plays an essential role in the assembly of multiple secretion systems through the processing of secretins, which are large, multimeric proteins that localize to the outer membrane
physiological function
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type I signal peptidase (SPase) is an essential part of the secretion apparatus. Its proteolytic activity is required to release proteins from their N-terminal leader sequence, which remain membrane bound after the preprotein translocates across the cytoplasmic membrane. Before the protein achieves its mature form, the Sec machinery recognizes the signal peptide and translocates the pre-protein across the cytoplasmic membrane, during which time the lipophilic region of the signal peptide becomes embedded in the cytoplasmic membrane. SPase then cleaves the signal peptide to release the protein. SPase also functions at the terminal step of the twin-arginine translocase (Tat) pathway. The Tat pathway is functionally similar to the Sec pathway, but it recognizes signal peptides containing a highly conserved R-R motif, and its pre-protein cargo fold prior to translocation across the cytoplasmic membrane. But SPase has also relevant biological functions outside of mediating secretion. SPase is required for virulence. As is common with Gram-positive bacteria, the genome of Listeria monocytogenes includes three separate SPase genes (SipX, SipY, and SipZ) that each play distinct roles in virulence. SPase processes components of multimeric secretion systems. SPase plays an essential role in the assembly of multiple secretion systems through the processing of secretins, which are large, multimeric proteins that localize to the outer membrane
physiological function
type I signal peptidase (SPase) is an essential part of the secretion apparatus. Its proteolytic activity is required to release proteins from their N-terminal leader sequence, which remain membrane bound after the preprotein translocates across the cytoplasmic membrane. Before the protein achieves its mature form, the Sec machinery recognizes the signal peptide and translocates the pre-protein across the cytoplasmic membrane, during which time the lipophilic region of the signal peptide becomes embedded in the cytoplasmic membrane. SPase then cleaves the signal peptide to release the protein. SPase also functions at the terminal step of the twin-arginine translocase (Tat) pathway. The Tat pathway is functionally similar to the Sec pathway, but it recognizes signal peptides containing a highly conserved R-R motif, and its pre-protein cargo fold prior to translocation across the cytoplasmic membrane. But SPase has also relevant biological functions outside of mediating secretion. SPase is required for virulence. The pathogenicity of Staphylococcus epidermidis relies almost solely on its ability to form biofilms. SPase processes components of multimeric secretion systems. SPase plays an essential role in the assembly of multiple secretion systems through the processing of secretins, which are large, multimeric proteins that localize to the outer membrane
physiological function
A0A1S0QR24
type I signal peptidase (SPase) is an essential part of the secretion apparatus. Its proteolytic activity is required to release proteins from their N-terminal leader sequence, which remain membrane bound after the preprotein translocates across the cytoplasmic membrane. Before the protein achieves its mature form, the Sec machinery recognizes the signal peptide and translocates the pre-protein across the cytoplasmic membrane, during which time the lipophilic region of the signal peptide becomes embedded in the cytoplasmic membrane. SPase then cleaves the signal peptide to release the protein. SPase also functions at the terminal step of the twin-arginine translocase (Tat) pathway. The Tat pathway is functionally similar to the Sec pathway, but it recognizes signal peptides containing a highly conserved R-R motif, and its pre-protein cargo fold prior to translocation across the cytoplasmic membrane. But SPase has also relevant biological functions outside of mediating secretion. SPase is required for virulence. SPase is involved in the formation of the S-layer which is a crystalline-like array of proteins, glycoprotein, or both that coat the surface of the cell. SPase processes components of multimeric secretion systems. SPase plays an essential role in the assembly of multiple secretion systems through the processing of secretins, which are large, multimeric proteins that localize to the outer membrane
physiological function
type I signal peptidase (SPase) is an essential part of the secretion apparatus. Its proteolytic activity is required to release proteins from their N-terminal leader sequence, which remain membrane bound after the preprotein translocates across the cytoplasmic membrane. Before the protein achieves its mature form, the Sec machinery recognizes the signal peptide and translocates the pre-protein across the cytoplasmic membrane, during which time the lipophilic region of the signal peptide becomes embedded in the cytoplasmic membrane. SPase then cleaves the signal peptide to release the protein. SPase also functions at the terminal step of the twin-arginine translocase (Tat) pathway. The Tat pathway is functionally similar to the Sec pathway, but it recognizes signal peptides containing a highly conserved R-R motif, and its pre-protein cargo fold prior to translocation across the cytoplasmic membrane. But SPase has also relevant biological functions outside of mediating secretion. SPase is required for virulence. SPase is involved in the formation of the S-layer which is a crystalline-like array of proteins, glycoprotein, or both that coat the surface of the cell. SPase processes components of multimeric secretion systems. SPase plays an essential role in the assembly of multiple secretion systems through the processing of secretins, which are large, multimeric proteins that localize to the outer membrane
physiological function
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type I signal peptidase (SPase) is an essential part of the secretion apparatus. Its proteolytic activity is required to release proteins from their N-terminal leader sequence, which remain membrane bound after the preprotein translocates across the cytoplasmic membrane. Before the protein achieves its mature form, the Sec machinery recognizes the signal peptide and translocates the pre-protein across the cytoplasmic membrane, during which time the lipophilic region of the signal peptide becomes embedded in the cytoplasmic membrane. SPase then cleaves the signal peptide to release the protein. SPase also functions at the terminal step of the twin-arginine translocase (Tat) pathway. The Tat pathway is functionally similar to the Sec pathway, but it recognizes signal peptides containing a highly conserved R-R motif, and its pre-protein cargo fold prior to translocation across the cytoplasmic membrane. But SPase has also relevant biological functions outside of mediating secretion. SPase is required for virulence. SPase processes components of multimeric secretion systems. SPase plays an essential role in the assembly of multiple secretion systems through the processing of secretins, which are large, multimeric proteins that localize to the outer membrane
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physiological function
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signal peptides direct proteins from the cytoplasm to the periplasm. These N-terminal peptides are cleaved upon entry to the periplasm by either signal peptidase I, or signal peptidase II for lipoproteins. Signal peptidase I is a serine protease that has either a serine-lysine or serine-histidine catalytic dyad present in the active site. The recognition site for signal peptide cleavage by signal peptidase I has been defined primarily by an Ala-X-Ala motif at the C-terminal end of the signal peptide, one amino acid away from the cleavage site
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physiological function
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involvement of signal peptidase I in Streptococcus sanguinis biofilm formation. Streptococcus sanguinis, a Gram-positive bacterium, is one of the most abundant species of the oral microbiota and it contributes to biofilm development in the oral cavity
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physiological function
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type I signal peptidase (SPase) is an essential part of the secretion apparatus. Its proteolytic activity is required to release proteins from their N-terminal leader sequence, which remain membrane bound after the preprotein translocates across the cytoplasmic membrane. Before the protein achieves its mature form, the Sec machinery recognizes the signal peptide and translocates the pre-protein across the cytoplasmic membrane, during which time the lipophilic region of the signal peptide becomes embedded in the cytoplasmic membrane. SPase then cleaves the signal peptide to release the protein. SPase also functions at the terminal step of the twin-arginine translocase (Tat) pathway. The Tat pathway is functionally similar to the Sec pathway, but it recognizes signal peptides containing a highly conserved R-R motif, and its pre-protein cargo fold prior to translocation across the cytoplasmic membrane. But SPase has also relevant biological functions outside of mediating secretion. SPase is required for virulence. SPase processes components of multimeric secretion systems. SPase plays an essential role in the assembly of multiple secretion systems through the processing of secretins, which are large, multimeric proteins that localize to the outer membrane
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physiological function
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type I signal peptidase (SPase) is an essential part of the secretion apparatus. Its proteolytic activity is required to release proteins from their N-terminal leader sequence, which remain membrane bound after the preprotein translocates across the cytoplasmic membrane. Before the protein achieves its mature form, the Sec machinery recognizes the signal peptide and translocates the pre-protein across the cytoplasmic membrane, during which time the lipophilic region of the signal peptide becomes embedded in the cytoplasmic membrane. SPase then cleaves the signal peptide to release the protein. SPase also functions at the terminal step of the twin-arginine translocase (Tat) pathway. The Tat pathway is functionally similar to the Sec pathway, but it recognizes signal peptides containing a highly conserved R-R motif, and its pre-protein cargo fold prior to translocation across the cytoplasmic membrane. But SPase has also relevant biological functions outside of mediating secretion. SPase is required for virulence. The pathogenicity of Staphylococcus epidermidis relies almost solely on its ability to form biofilms. SPase processes components of multimeric secretion systems. SPase plays an essential role in the assembly of multiple secretion systems through the processing of secretins, which are large, multimeric proteins that localize to the outer membrane
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physiological function
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signal peptides direct proteins from the cytoplasm to the periplasm. These N-terminal peptides are cleaved upon entry to the periplasm by either signal peptidase I, or signal peptidase II for lipoproteins. Signal peptidase I is a serine protease that has either a serine-lysine or serine-histidine catalytic dyad present in the active site. The recognition site for signal peptide cleavage by signal peptidase I has been defined primarily by an Ala-X-Ala motif at the C-terminal end of the signal peptide, one amino acid away from the cleavage site
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physiological function
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type I signal peptidase (SPase) is an essential part of the secretion apparatus. Its proteolytic activity is required to release proteins from their N-terminal leader sequence, which remain membrane bound after the preprotein translocates across the cytoplasmic membrane. Before the protein achieves its mature form, the Sec machinery recognizes the signal peptide and translocates the pre-protein across the cytoplasmic membrane, during which time the lipophilic region of the signal peptide becomes embedded in the cytoplasmic membrane. SPase then cleaves the signal peptide to release the protein. SPase also functions at the terminal step of the twin-arginine translocase (Tat) pathway. The Tat pathway is functionally similar to the Sec pathway, but it recognizes signal peptides containing a highly conserved R-R motif, and its pre-protein cargo fold prior to translocation across the cytoplasmic membrane. But SPase has also relevant biological functions outside of mediating secretion. SPase is required for virulence. SPase processes components of multimeric secretion systems. SPase plays an essential role in the assembly of multiple secretion systems through the processing of secretins, which are large, multimeric proteins that localize to the outer membrane
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physiological function
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type I signal peptidase (SPase) is an essential part of the secretion apparatus. Its proteolytic activity is required to release proteins from their N-terminal leader sequence, which remain membrane bound after the preprotein translocates across the cytoplasmic membrane. Before the protein achieves its mature form, the Sec machinery recognizes the signal peptide and translocates the pre-protein across the cytoplasmic membrane, during which time the lipophilic region of the signal peptide becomes embedded in the cytoplasmic membrane. SPase then cleaves the signal peptide to release the protein. SPase also functions at the terminal step of the twin-arginine translocase (Tat) pathway. The Tat pathway is functionally similar to the Sec pathway, but it recognizes signal peptides containing a highly conserved R-R motif, and its pre-protein cargo fold prior to translocation across the cytoplasmic membrane. But SPase has also relevant biological functions outside of mediating secretion. SPase is required for virulence. SPase processes components of multimeric secretion systems. SPase plays an essential role in the assembly of multiple secretion systems through the processing of secretins, which are large, multimeric proteins that localize to the outer membrane
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physiological function
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SPase I is responsible for removing the signal peptide from secretory pre-proteins and releasing mature proteins to cellular or extra-cellular space. SPase I may have an important role in Leishmania infectivity, e.g. in differentiation and survival of amastigotes
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physiological function
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type I signal peptidase (SPase) is an essential part of the secretion apparatus. Its proteolytic activity is required to release proteins from their N-terminal leader sequence, which remain membrane bound after the preprotein translocates across the cytoplasmic membrane. Before the protein achieves its mature form, the Sec machinery recognizes the signal peptide and translocates the pre-protein across the cytoplasmic membrane, during which time the lipophilic region of the signal peptide becomes embedded in the cytoplasmic membrane. SPase then cleaves the signal peptide to release the protein. SPase also functions at the terminal step of the twin-arginine translocase (Tat) pathway. The Tat pathway is functionally similar to the Sec pathway, but it recognizes signal peptides containing a highly conserved R-R motif, and its pre-protein cargo fold prior to translocation across the cytoplasmic membrane. But SPase has also relevant biological functions outside of mediating secretion. SPase is required for virulence. SPase processes components of multimeric secretion systems. SPase plays an essential role in the assembly of multiple secretion systems through the processing of secretins, which are large, multimeric proteins that localize to the outer membrane
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physiological function
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signal peptides direct proteins from the cytoplasm to the periplasm. These N-terminal peptides are cleaved upon entry to the periplasm by either signal peptidase I, or signal peptidase II for lipoproteins. Signal peptidase I is a serine protease that has either a serine-lysine or serine-histidine catalytic dyad present in the active site. The recognition site for signal peptide cleavage by signal peptidase I has been defined primarily by an Ala-X-Ala motif at the C-terminal end of the signal peptide, one amino acid away from the cleavage site
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physiological function
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type I signal peptidase (SPase) is an essential part of the secretion apparatus. Its proteolytic activity is required to release proteins from their N-terminal leader sequence, which remain membrane bound after the preprotein translocates across the cytoplasmic membrane. Before the protein achieves its mature form, the Sec machinery recognizes the signal peptide and translocates the pre-protein across the cytoplasmic membrane, during which time the lipophilic region of the signal peptide becomes embedded in the cytoplasmic membrane. SPase then cleaves the signal peptide to release the protein. SPase also functions at the terminal step of the twin-arginine translocase (Tat) pathway. The Tat pathway is functionally similar to the Sec pathway, but it recognizes signal peptides containing a highly conserved R-R motif, and its pre-protein cargo fold prior to translocation across the cytoplasmic membrane. But SPase has also relevant biological functions outside of mediating secretion. SPase is required for virulence. SPase processes components of multimeric secretion systems. SPase plays an essential role in the assembly of multiple secretion systems through the processing of secretins, which are large, multimeric proteins that localize to the outer membrane
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physiological function
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type I signal peptidase (SPase) is an essential part of the secretion apparatus. Its proteolytic activity is required to release proteins from their N-terminal leader sequence, which remain membrane bound after the preprotein translocates across the cytoplasmic membrane. Before the protein achieves its mature form, the Sec machinery recognizes the signal peptide and translocates the pre-protein across the cytoplasmic membrane, during which time the lipophilic region of the signal peptide becomes embedded in the cytoplasmic membrane. SPase then cleaves the signal peptide to release the protein. SPase also functions at the terminal step of the twin-arginine translocase (Tat) pathway. The Tat pathway is functionally similar to the Sec pathway, but it recognizes signal peptides containing a highly conserved R-R motif, and its pre-protein cargo fold prior to translocation across the cytoplasmic membrane. But SPase has also relevant biological functions outside of mediating secretion. SPase is required for virulence. SPase processes components of multimeric secretion systems. SPase plays an essential role in the assembly of multiple secretion systems through the processing of secretins, which are large, multimeric proteins that localize to the outer membrane
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physiological function
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signal peptides direct proteins from the cytoplasm to the periplasm. These N-terminal peptides are cleaved upon entry to the periplasm by either signal peptidase I, or signal peptidase II for lipoproteins. Signal peptidase I is a serine protease that has either a serine-lysine or serine-histidine catalytic dyad present in the active site. The recognition site for signal peptide cleavage by signal peptidase I has been defined primarily by an Ala-X-Ala motif at the C-terminal end of the signal peptide, one amino acid away from the cleavage site
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physiological function
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gene is essential, and reduced lepB expression is detrimental to growth
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physiological function
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proteins that carry a type I signal peptide are released from their membrane anchored signal peptide by signal peptidase I (SPI). They can then remain in the periplasm, or be transported further. In Bacteroidetes, signal peptide cleavage exposes N-terminal glutamine residues in most signal peptidase I (SPI) substrates. The newly exposed glutamines are cyclized to pyroglutamate (also termed 5-oxoproline) residues. Porphyromonas gingivalis SPI substrates typically have a glutamine residue downstream of the SPI cleavage site. A Gln residue downstream of the SPI cleavage site affects RgpA, but not RgpB and Kgp gingipains secretion
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physiological function
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type I signal peptidase (SPase) is an essential part of the secretion apparatus. Its proteolytic activity is required to release proteins from their N-terminal leader sequence, which remain membrane bound after the preprotein translocates across the cytoplasmic membrane. Before the protein achieves its mature form, the Sec machinery recognizes the signal peptide and translocates the pre-protein across the cytoplasmic membrane, during which time the lipophilic region of the signal peptide becomes embedded in the cytoplasmic membrane. SPase then cleaves the signal peptide to release the protein. SPase also functions at the terminal step of the twin-arginine translocase (Tat) pathway. The Tat pathway is functionally similar to the Sec pathway, but it recognizes signal peptides containing a highly conserved R-R motif, and its pre-protein cargo fold prior to translocation across the cytoplasmic membrane. But SPase has also relevant biological functions outside of mediating secretion. SPase is required for virulence. SPase processes components of multimeric secretion systems. SPase plays an essential role in the assembly of multiple secretion systems through the processing of secretins, which are large, multimeric proteins that localize to the outer membrane
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physiological function
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proteins that carry a type I signal peptide are released from their membrane anchored signal peptide by signal peptidase I (SPI). They can then remain in the periplasm, or be transported further. In Bacteroidetes, signal peptide cleavage exposes N-terminal glutamine residues in most signal peptidase I (SPI) substrates. The newly exposed glutamines are cyclized to pyroglutamate (also termed 5-oxoproline) residues. Porphyromonas gingivalis SPI substrates typically have a glutamine residue downstream of the SPI cleavage site. A Gln residue downstream of the SPI cleavage site affects RgpA, but not RgpB and Kgp gingipains secretion
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additional information
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proper maturation of lumenal proteins may be a key process for correct assembly of thylakoids
additional information
if an N-terminal glutamine residue is exposed as a result of proteolysis, e.g. signal peptide proteolysis by signal peptidase 1, this glutamine residue has a tendency to cyclize to diglutamate, with release of ammonia as a side product. The transamidation reaction is thought to initiate with nucleophilic attack of the alpha-amino group on the carbonyl group of the side chain carboxamide, followed by collapse of the oxyanion intermediate and protonation of the leaving epsilon-amino group. Glutamine cyclization to diglutamate can occur spontaneously. The reaction is facilitated by inorganic catalysts such as phosphate ions serving as the proton shuttle, or can be catalyzed enzymatically by glutaminyl cyclases (QCs)
additional information
the energy requirement of integration of Plsp1 into isolated chloroplast membranes are satified by ATP hydrolysis. The C-terminal portion of Plsp1 including catalytic residues is predicted to form a hydrophobic surface at the trans-side of the membrane
additional information
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the energy requirement of integration of Plsp1 into isolated chloroplast membranes are satified by ATP hydrolysis. The C-terminal portion of Plsp1 including catalytic residues is predicted to form a hydrophobic surface at the trans-side of the membrane
additional information
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if an N-terminal glutamine residue is exposed as a result of proteolysis, e.g. signal peptide proteolysis by signal peptidase 1, this glutamine residue has a tendency to cyclize to diglutamate, with release of ammonia as a side product. The transamidation reaction is thought to initiate with nucleophilic attack of the alpha-amino group on the carbonyl group of the side chain carboxamide, followed by collapse of the oxyanion intermediate and protonation of the leaving epsilon-amino group. Glutamine cyclization to diglutamate can occur spontaneously. The reaction is facilitated by inorganic catalysts such as phosphate ions serving as the proton shuttle, or can be catalyzed enzymatically by glutaminyl cyclases (QCs)
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additional information
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if an N-terminal glutamine residue is exposed as a result of proteolysis, e.g. signal peptide proteolysis by signal peptidase 1, this glutamine residue has a tendency to cyclize to diglutamate, with release of ammonia as a side product. The transamidation reaction is thought to initiate with nucleophilic attack of the alpha-amino group on the carbonyl group of the side chain carboxamide, followed by collapse of the oxyanion intermediate and protonation of the leaving epsilon-amino group. Glutamine cyclization to diglutamate can occur spontaneously. The reaction is facilitated by inorganic catalysts such as phosphate ions serving as the proton shuttle, or can be catalyzed enzymatically by glutaminyl cyclases (QCs)
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