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Information on EC 3.4.21.89 - Signal peptidase I and Organism(s) Bacillus subtilis and UniProt Accession P28628

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.21 Serine endopeptidases
                3.4.21.89 Signal peptidase I
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This record set is specific for:
Bacillus subtilis
UNIPROT: P28628 not found.
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Word Map
The taxonomic range for the selected organisms is: Bacillus subtilis
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Cleavage of hydrophobic, N-terminal signal or leader sequences
Synonyms
signal peptidase, leader peptidase, spase, protease iv, signal peptidase i, spase i, type i signal peptidase, leader proteinase, plsp1, sec11, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SipP (pTA1015)
plasmid-encodes type I signal peptidase
SipP (pTA1040)
plasmid-encodes type I signal peptidase
SipT
chromsomal type I signal peptidase
SipU
chromsomal type I signal peptidase
SipV
chromsomal type I signal peptidase
SipW
chromsomal type I signal peptidase
Bacterial leader peptidase 1
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-
-
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Escherichia coli leader peptidase
-
-
-
-
Eukaryotic signal peptidase
-
-
-
-
Eukaryotic signal proteinase
-
-
-
-
HOSP
-
-
-
-
Leader peptidase
-
-
-
-
Leader peptidase I
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-
-
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Leader peptide hydrolase
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-
-
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Leader proteinase
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-
-
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Peptidase, signal
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-
-
-
Pilin leader peptidase
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-
-
-
Prokaryotic leader peptidase
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-
-
-
Prokaryotic signal peptidase
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-
-
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Prokaryotic signal proteinase
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-
-
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Propeptidase
-
-
-
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Proteinase, eukaryotic signal
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-
-
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Proteinase, signal
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-
-
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PuIO prepilin peptidase
-
-
-
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Signal peptidase
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-
-
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Signal peptide hydrolase
-
-
-
-
Signal peptide peptidase
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-
-
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Signalase
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-
-
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SPC
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
65979-36-4
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
preprotein substrate PONA + H2O
protein substrate PONA + ?
show the reaction diagram
-
-
?
signal peptides from preproteins + H2O
mature proteins
show the reaction diagram
-
-
?
pro-ompA-nuclease + H2O
ompA-nuclease + ?
show the reaction diagram
-
-
-
?
signal peptides from preproteins + H2O
mature proteins
show the reaction diagram
additional information
?
-
signal peptidase I processes secretory signal sequences. Selection for and against specific amino acids occurs at the second position of mature protein. The enzyme shows preference for the presence of acidic residues at second position of the mature protein (P2'), and a complete absence of aromatic amino acids at the same position. Substrate specificity and in silico prediction of signal peptidase I cleavage sites, overview
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
signal peptides from preproteins + H2O
mature proteins
show the reaction diagram
-
-
?
signal peptides from preproteins + H2O
mature proteins
show the reaction diagram
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
not inhibited by any commercially available peptidase inhibitor including o-phenanthroline, ethylenediamine tetraacetic acid, phosphoramidon, 2,6-pyridine dicarboxylic acid, bestatin, tosyl-amido-2-phenylethyl chloromethyl ketone, 1-chloro-3-tosylamido-7-amino-2-heptanone hydrochloride, phenylmethylsulfonyl fluoride, 4-(amidinophenyl)methanesulfonyl fluoride, N-carbobenzyloxy-L-phenylalanyl chloromethyl ketone, dichloroisocoumarin, elastatinal, aprotinin, chymostatin, leupeptin, antipain dihydrochloride, iodoacetamide, N-ethylmaleimide, L-trans-epoxysuccinyl-leucylamido (4-guanidino) butane, 1,2-epoxy-3-(p nitrophenoxy)propane, pepstatin, and diaxoacetyl-DL-norleucine methyl ester
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0166 - 0.044
preprotein substrate PONA
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.014 - 0.034
preprotein substrate PONA
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60000
recombinant fusion protein MBP-SipS-P2
63000
recombinant fusion protein MBP-SipS
21000
-
deduced from DNA sequence
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
MBP-SipS fusion protein, SipS, SipS-P2
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloning of the WT and P2 domain of SipS, MBP-SipS fusion protein expressed in Escherichia coli
gene SppA similar to Escherichia coli signal peptide peptidase A
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pharmacology
possible targets for the design of novel antibiotics
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bolhuis, A.; Matzen, A.; Hyyrylainen, H.L.; Kontinen, V.P.; Meima, R.; Chapuis, J.; Venema, G.; Bron, S.; Freudl, R.; van Dijl, J.M.
Signal peptide peptidase- and ClpP-like proteins of Bacillus subtilis required for efficient translocation and processing of secretory proteins
J. Biol. Chem.
274
24585-24592
1999
Bacillus subtilis
Manually annotated by BRENDA team
Carlos, J.L.; Paetzel, M.; Brubaker, G.; Karla, A.; Ashwell, C.M.; Lively, M.O.; Cao, G.; Bullinger, P.; Dalbey, R.E.
The role of the membrane-spanning domain of type I signal peptidases in substrate cleavage site selection
J. Biol. Chem.
275
38813-38822
2000
Escherichia coli (P00803), Escherichia coli, Bacillus subtilis (P28628), Bacillus subtilis
Manually annotated by BRENDA team
Dalbey, R.E.; Lively, M.O.; Bron,S.; Van Diijl, J.M.
The chemistry and enzymology of the type I signal peptidases
Protein Sci.
6
1129-1138
1997
Bacillus amyloliquefaciens, [Bacillus] caldolyticus, Bacillus subtilis, Bacillus licheniformis, Bradyrhizobium japonicum, Saccharomyces cerevisiae, Canis lupus familiaris, Gallus gallus, Escherichia coli, Haemophilus influenzae, Methanocaldococcus jannaschii, Staphylococcus aureus, Mycobacterium tuberculosis, no activity in Mycoplasma genitalium, Phormidium laminosum, Pseudomonas fluorescens, Rana sp., Rattus norvegicus, Salmonella enterica subsp. enterica serovar Typhimurium, Caenorhabditis elegans (P34525), Schizosaccharomyces pombe (Q10259), Homo sapiens (Q15005), Rhodobacter capsulatus (Q52697)
Manually annotated by BRENDA team
Zalucki, Y.M.; Jennings, M.P.
Signal peptidase I processed secretory signal sequences selection for and against specific amino acids at the second position of mature protein
Biochem. Biophys. Res. Commun.
483
972-977
2017
Methanococcus voltae, Sulfurisphaera tokodaii, Escherichia coli (P00803), Saccharomyces cerevisiae (P15367), Saccharomyces cerevisiae, Bacillus subtilis (P28628), Bacillus subtilis 168 (P28628), Sulfurisphaera tokodaii 7, Methanococcus voltae A3, Saccharomyces cerevisiae ATCC 204508 (P15367)
Manually annotated by BRENDA team