Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 3.4.24.B20 - FtsH protease and Organism(s) Thermotoga maritima and UniProt Accession Q9WZ49

for references in articles please use BRENDA:EC3.4.24.B20
preliminary BRENDA-supplied EC number
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.24 Metalloendopeptidases
                3.4.24.B20 FtsH protease
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Thermotoga maritima
UNIPROT: Q9WZ49
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Thermotoga maritima
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
degradative cleavage of proteins
Synonyms
ftsh protease, ftsh2, ftsh1, ftsh11, ftsh5, ftsh3, ftsh12, ftsh6, atftsh2, atp-dependent zinc metalloprotease, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
the enzyme belongs to the AAA+ protease family
CAS REGISTRY NUMBER
COMMENTARY hide
253850-13-4
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
casein + H2O
?
show the reaction diagram
artificial resorufin-labeled substrate
-
-
?
additional information
?
-
an active-site switch is formed by a substrate-binding beta-strand
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
a metalloprotease with HEXXH motif
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ATP
dependent on
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
membrane-spanning enzyme
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
hexameric assembly consisting of a 6fold symmetric protease disk and a 2fold symmetric AAA ring
additional information
comparison of the apo- and ADP-bound structure visualizes an inward movement of the aromatic pore residues and generates a model of substrate translocation by AAA+ proteases, modelling of the apo- and ADP bound state
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
cytosolic region of apo-FtsH, microbatch method by mixing equal volumes of 20 mg/ml protein with crystallization buffer containing 30% w/v PEG 400, 200 mM CaCl2, 100 mM HEPES, pH 7.5, 200 mM glycine, and 0.1-0.2% w/v low-melt agarose, 20°C, X-ray diffraction structure determination and analysis at 2.6 A resolution
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A359V
homolog of the human pathogenic A510V mutation of paraplegin (SPG7), does not affect the dynamic behavior of the protease but impairs the ATP-coupled domain compaction
G404L
site-directed mutagenesis, the mutant is monomeric and inactive in the ATPase assay and possesses only very low proteolytic activity
K207A
site-directed mutagenesis, crystal structure determination
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant amino acids 147-610 of FtsH with K410L-K415A surface mutations, and recombinant G404L and K207A mutants
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of amino acids 147-610 of FtsH with K410L-K415A surface mutations, and expression of G404L and K207A mutants
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bieniossek, C.; Niederhauser, B.; Baumann, U.M.
The crystal structure of apo-FtsH reveals domain movements necessary for substrate unfolding and translocation
Proc. Natl. Acad. Sci. USA
106
21579-21584
2009
Thermotoga maritima (Q9WZ49)
Manually annotated by BRENDA team
Ruer, M.; Krainer, G.; Groeger, P.; Schlierf, M.
ATPase and protease domain movements in the bacterial AAA+ protease FtsH are driven by thermal fluctuations
J. Mol. Biol.
430
4592-4602
2018
Thermotoga maritima (Q9WZ49), Thermotoga maritima DSM 3109 (Q9WZ49)
Manually annotated by BRENDA team