3.6.5.4: signal-recognition-particle GTPase
This is an abbreviated version!
For detailed information about signal-recognition-particle GTPase, go to the full flat file.
Word Map on EC 3.6.5.4
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3.6.5.4
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gtpases
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ribonucleoprotein
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co-translational
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translocons
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srp-dependent
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thylakoids
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sec
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exit
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light-harvesting
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myopathy
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secyeg
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cotranslationally
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universally
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gtp-binding
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myositis
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translocase
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presecretory
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tetraloops
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insertase
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polytopic
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anti-srp
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methionine-rich
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ribosome-associated
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rna-protein
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preproteins
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protein-targeting
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signal-anchor
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m-domain
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ribosome-bound
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chromodomains
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medicine
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polymyositis
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protein-conducting
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anti-signal
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protein-rna
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chlorophyll-binding
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gtp-bound
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walter
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multispanning
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imnms
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sequence-binding
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myositis-specific
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tail-anchored
- 3.6.5.4
- gtpases
- ribonucleoprotein
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co-translational
-
translocons
-
srp-dependent
- thylakoids
-
sec
-
exit
-
light-harvesting
- myopathy
-
secyeg
-
cotranslationally
-
universally
-
gtp-binding
- myositis
- translocase
-
presecretory
- tetraloops
-
insertase
-
polytopic
-
anti-srp
-
methionine-rich
-
ribosome-associated
-
rna-protein
- preproteins
-
protein-targeting
-
signal-anchor
-
m-domain
-
ribosome-bound
-
chromodomains
- medicine
- polymyositis
-
protein-conducting
-
anti-signal
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protein-rna
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chlorophyll-binding
-
gtp-bound
-
walter
-
multispanning
-
imnms
-
sequence-binding
-
myositis-specific
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tail-anchored
Reaction
Synonyms
54-kDa GTPase, chloroplast signal recognition particle, chloroplast signal recognition particle protein, chloroplast signal recognition particle receptor, chloroplast SRP, cpFtsY, cpSRP, cpSRP43, cpSRP54, CtSR, EC 3.6.1.49, Ffh, FlhF, FtsH, FtsY, FtsY GTPase, GTPase, guanine triphosphatase, guanosine 5'-triphosphatase, guanosine triphosphatase, PAB0955, ribosomal GTPase, signal recognition particle, signal recognition particle 54 kDa protein, signal recognition particle receptor, signal recognition particle receptor beta subunit, signal recognition particle receptor subunit alpha, signal recognition particle receptor subunit beta, signal recognition particle-like GTPase, signal-recognition-particle GTPase, SR, SR GTPase, SRalpha, SRbeta, SRbeta GTPase, SRP, SRP GTPase, SRP GTPase Ffh, SRP receptor, SRP receptor GTPase, SRP14, SRP19, SRP21, SRP54, SRP54 GTPase, Srp72p, SRP:SR GTPase, SRP:SR guanine triphosphatase, SRPRA, SRPRB
ECTree
3.6.5.4 signal-recognition-particle GTPaseAdvanced search results
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Engineering on EC 3.6.5.4 - signal-recognition-particle GTPase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Thr112Ala
A142W
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site-directed mutagenesis, the mutant cpSRP54 exhibits the same GTP-dependent complex assembly kinetics as wild-type cpSRP54
A143L
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site-directed mutagenesis, mutant cpSRP54 GTP-dependent complex assembly kinetics compared to the wild-type cpSRP54, overview
A143W
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site-directed mutagenesis, mutant cpSRP54 GTP-dependent complex assembly kinetics compared to the wild-type cpSRP54, overview
A168W
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site-directed mutagenesis, mutant cpSRP54 GTP-dependent complex assembly kinetics compared to the wild-type cpSRP54, overview
A169L
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site-directed mutagenesis, mutant cpSRP54 GTP-dependent complex assembly kinetics compared to the wild-type cpSRP54, overview
A169W
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site-directed mutagenesis, mutant cpSRP54 GTP-dependent complex assembly kinetics compared to the wild-type cpSRP54, overview
D137A
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site-directed mutagenesis, mutant cpSRP54 GTP-dependent complex assembly kinetics compared to the wild-type cpSRP54, overview
D163A
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site-directed mutagenesis, mutant cpSRP54 GTP-dependent complex assembly kinetics compared to the wild-type cpSRP54, overview
F33L
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mutation in the N-domain modulates the interaction kinetic between cpSRP54 and cpFtsY
F71V
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mutation in the N-domain modulates the interaction kinetic between cpSRP54 and cpFtsY
R140A
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site-directed mutagenesis, mutant cpSRP54 GTP-dependent complex assembly kinetics compared to the wild-type cpSRP54, overview
R166A
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site-directed mutagenesis, mutant cpSRP54 GTP-dependent complex assembly kinetics compared to the wild-type cpSRP54, overview
S54C/K407C
site-directed mutagenesis, mutations S54C in the N-domain and K407C in the M-domain of cpSRP54r resulting in mutant cpSRP54S54C/K407C
V339N/L370N
site-directed mutagenesis, mutant cpSRP54V339N/L370N of the mature enyme
DELTAflhF1
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flhF fragment from bp +282 to +1071 relative to the translational initiation site
DELTAflhF2
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flhF fragment from bp +210 to +685 relative to the translational initiation site
D181N
G118L
G118L/D181N
H119L
K75I
K75I/H119L
P61010; P06625
site-directed mutagenesis of SRP54 (or SRbeta), the mutant shows a null mutant phenotype and no binding of SRalpha
N178K
C86A
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mutations at C86 yield a more complex pattern: whereas C86A and C86U completely abolish GTPase activation by the RNA, C86 and C86G reduce GTPase activity by only 50%
C86G
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mutations at C86 yield a more complex pattern: whereas C86A and C86U completely abolish GTPase activation by the RNA, DELTAC86 and C86G reduce GTPase activity by only 50%. Despite defective GTP hydrolysis, the G83A mutant shows any detectable defect in the efficiency of GTPase docking at the distal end
C86U
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mutations at C86 yield a more complex pattern: whereas C86A and C86U completely abolish GTPase activation by the RNA, C86 and C86G reduce GTPase activity by only 50%
C87A/C97U
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site-directed mutagenesis, combining C97U with C87A generates a superactive SRP RNA double mutant that hydrolyzes GTP 5.5fold faster than wild-type SRP RNA
C97U
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site-directed mutagenesis, the mutant prolongs GTPase docking at the distal end, which correlates with its faster GTP hydrolysis rate
C97U/G99A
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site-directed mutagenesis, combining G99A with C87A generate s a superactive SRP RNA double mutant that hydrolyzes GTP 4.6fold faster than wild-type SRP RNA
F240V
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mutation in the N-domain modulates the interaction kinetic between Ffh and FtsY
G257A
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residue resides at the N-GTPase domain interface, mutation produces a lethal phenotype, it does not significantly affect Ffh function, but severely reduces interaction with FtsY
G455W
G83A
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deletion or substitution of G83 by any other nucleotide completely abolishes the stimulatory effect of the SRP RNA on GTP hydrolysis. Despite defective GTP hydrolysis, the G83A mutant shows any detectable defect in the efficiency of GTPase docking at the distal end
G99A
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site-directed mutagenesis, the mutant prolongs GTPase docking at the distal end, which correlates with its faster GTP hydrolysis rate
L199F
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mutation in the N-domain modulates the interaction kinetic between Ffh and FtsY
G257A
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residue resides at the N-GTPase domain interface, mutation produces a lethal phenotype, it does not significantly affect Ffh function, but severely reduces interaction with FtsY
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F48A
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the cpFtsY mutant exhibits a GTP hydrolysis rate 4times greater than wild type cpFtsY in the absence of liposomes, the mutation reduces light-harvesting chlorophyll-binding protein integration efficiency by nearly 80%
F49A
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the mutation reduces light-harvesting chlorophyll-binding protein integration efficiency by nearly 40%
A145S
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substitution introduced into the putative GTP binding motif GXXGXGK
G141V
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substitution introduced into the putative GTP binding motif GXXGXGK
G222V
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substitution introduced into the putative GTP binding motif GXXGXGK
GAK-VSG
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substitution introduced into the putative GTP binding motif GXXGXGK
GTK-VSG
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substitution introduced into the putative GTP binding motif GXXGXGK
K147G
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substitution introduced into the putative GTP binding motif GXXGXGK
K228G
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substitution introduced into the putative GTP binding motif GXXGXGK
T226S
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substitution introduced into the putative GTP binding motif GXXGXGK
additional information
D181N
P61010; P06625
site-directed mutagenesis of SRP54 (or SRbeta), the mutant shows the wild-type phenotype and binding of SRalpha at wild-type level, but no binding in absence of GTP. SRalpha binding to D181N can be restored to some level by adding back nucleotide, i.e. GTP, GDP, XTP or XDP, but not with ATP
G118L
P61010; P06625
site-directed mutagenesis of SRP54 (or SRbeta), the mutant shows a temperature-sensitive phenotype and binding of SRalpha at wild-type level
G118L/D181N
P61010; P06625
site-directed mutagenesis of SRP54 (or SRbeta) and weak binding of SRalpha
H119L
P61010; P06625
site-directed mutagenesis of SRP54 (or SRbeta), the mutant shows the wild-type phenotype and binding of SRalpha at wild-type level
K75I
P61010; P06625
site-directed mutagenesis of SRP54 (or SRbeta), the mutant shows a temperature-sensitive phenotype and no binding of SRalpha
N178K
P61010; P06625
site-directed mutagenesis of SRP54 (or SRbeta), the mutant shows a temperature-sensitive phenotype and weak binding of SRalpha
G455W
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mutant, exhibits no significant GTP hydrolysis and defective in SRP-FtsY complex formation
additional information
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binding kinetics and competing inhibitions with several bacterial cpFtsY mutants, affinities of mutant bacterial cpFtsYs for cpSRP54, and complex formations, overview
additional information
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flhF::cat mutant strain assembles flagella and is motile
additional information
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flhF::cat mutant strain assembles flagella and is motile
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additional information
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SRbetaC1-deltaTM, hydrolysis of XTP favored over GTP
additional information
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SRbeta-deltaloop, hydrolysis of XTP favored over GTP
additional information
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SRbeta-deltaTM, hydrolysis of XTP favored over GTP
additional information
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Srbeta-loop2, hydrolysis of XTP favored over GTP
additional information
P61010; P06625
construction of several deletion mutants: SRbeta-DELTATM, SRbetaDELTA4, SRbetaDELTA5, SRbeta1C1-DELTATM, SRbeta-DELTAloop, and SRbeta-loop2, phenotypes, altered SRalpha binding of the truncated mutants, overview. Deletion of the last 6 amino-acids from the carboxyl-terminus of the SRbeta GTPase domain results in a molecule (SRbetaC1) with primarily type I topology, similar to SRbeta
additional information
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FtsY mutated in the 4th GTP-binding consensus element displays reduced GTP-binding and -hydrolysis which correlates with a reduced ability to interact with SRP
additional information
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4.5S RNA tetraloop mutants UUCG, UUUU, CUUC, GUAA and GAAA
additional information
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several mutants show higher GTPase activity than wild-type SRP RNA, most notably mutations at G99, U12, and C97. By modifying the GTPase docking interface, the efficiency of activation of the Ffh-FtsY GTPase complex can be specifically tuned. When G83 is mutated, substitution of C86 with guanine rescues the SRP RNA-mediated stimulation of GTPase activity to 50% of wild-type rate. Despite defective GTP hydrolysis, neither the G83A nor C86G mutant shows any detectable defect in the efficiency of GTPase docking at the distal end
additional information
construction of the FtsYDELTAN1 mutant, and creation of a fusion construct comprising two FtsYDELTAN1 molecules linked via a 31-amino-acid GS linker, similar to the situation for the FtsY/Ffh heterodimer (FtsYDELTAN12)
additional information
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construction of the FtsYDELTAN1 mutant, and creation of a fusion construct comprising two FtsYDELTAN1 molecules linked via a 31-amino-acid GS linker, similar to the situation for the FtsY/Ffh heterodimer (FtsYDELTAN12)
additional information
P08240; Q9Y5M8
construction of a bi-cistronic construct containing human SRalpha subunit and murine SRbeta subunit lacking the transmembrane domain and cloning in the pET16b vector. Linker deletion variants of SR are created using the same construct
additional information
P08240; Q9Y5M8
two-site binding analysis of the SRP54DELTAC-ribosome interaction. Having a signal sequence fused to SRP54 or presented by the ribosome does not seem to significantly change SRP binding to the ribosome
additional information
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two-site binding analysis of the SRP54DELTAC-ribosome interaction. Having a signal sequence fused to SRP54 or presented by the ribosome does not seem to significantly change SRP binding to the ribosome
additional information
Q9DBG7; P47758
construction of a bi-cistronic construct containing human SRalpha subunit and murine SRbeta subunit lacking the transmembrane domain and cloning in the pET16b vector. Linker deletion variants of SR are created using the same construct
additional information
Thermochaetoides thermophila
while CtSRalpha complexed with SRbetaDELTAN can bind ribosomes, both CtSRbetaDELTAN alone and the minimal CtSRalpha138/SRbetaDELTAN complex are unable to bind ribosomes. Full-length CtSRalpha alone readily binds to the ribosomes in a sedimentation assay, as well as to canine ribosomes
additional information
Thermochaetoides thermophila CBS 144.50
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while CtSRalpha complexed with SRbetaDELTAN can bind ribosomes, both CtSRbetaDELTAN alone and the minimal CtSRalpha138/SRbetaDELTAN complex are unable to bind ribosomes. Full-length CtSRalpha alone readily binds to the ribosomes in a sedimentation assay, as well as to canine ribosomes
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additional information
Thermochaetoides thermophila DSM 1495
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while CtSRalpha complexed with SRbetaDELTAN can bind ribosomes, both CtSRbetaDELTAN alone and the minimal CtSRalpha138/SRbetaDELTAN complex are unable to bind ribosomes. Full-length CtSRalpha alone readily binds to the ribosomes in a sedimentation assay, as well as to canine ribosomes
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additional information
Thermochaetoides thermophila IMI 039719
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while CtSRalpha complexed with SRbetaDELTAN can bind ribosomes, both CtSRbetaDELTAN alone and the minimal CtSRalpha138/SRbetaDELTAN complex are unable to bind ribosomes. Full-length CtSRalpha alone readily binds to the ribosomes in a sedimentation assay, as well as to canine ribosomes
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