Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

GTPase Era (ERA) (GTP-binding protein Era)

 ERA_ECOLI               Reviewed;         301 AA.
P06616; Q2MAG4;
01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
01-FEB-1994, sequence version 2.
28-MAR-2018, entry version 179.
RecName: Full=GTPase Era;
Short=ERA;
AltName: Full=GTP-binding protein Era;
Name=era; Synonyms=rbaA, sdgE; OrderedLocusNames=b2566, JW2550;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND GTP-BINDING.
PubMed=3097637; DOI=10.1073/pnas.83.23.8849;
Ahnn J., March P.E., Takiff H.E., Inouye M.;
"A GTP-binding protein of Escherichia coli has homology to yeast RAS
proteins.";
Proc. Natl. Acad. Sci. U.S.A. 83:8849-8853(1986).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12 / W3110;
Nashimoto H., Saito N.;
Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-50.
STRAIN=K12 / CS520;
PubMed=3895158; DOI=10.1093/nar/13.13.4677;
March P.E., Ahnn J., Inouye M.;
"The DNA sequence of the gene (rnc) encoding ribonuclease III of
Escherichia coli.";
Nucleic Acids Res. 13:4677-4685(1985).
[6]
PROTEIN SEQUENCE OF 2-40, GTP-BINDING, GDP-BINDING, CATALYTIC
ACTIVITY, ENZYME REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
STRAIN=K12 / W3110;
PubMed=2105934;
Chen S.M., Takiff H.E., Barber A.M., Dubois G.C., Bardwell J.C.,
Court D.L.;
"Expression and characterization of RNase III and Era proteins.
Products of the rnc operon of Escherichia coli.";
J. Biol. Chem. 265:2888-2895(1990).
[7]
PROTEIN SEQUENCE OF N-TERMINUS, MASS SPECTROMETRY, GTPASE ACTIVITY,
SUBUNIT, AND PRELIMINARY CRYSTALLIZATION.
STRAIN=K12 / W3110;
PubMed=10094501; DOI=10.1016/S0014-5793(99)00178-7;
Chen X., Chen S.M., Powell B.S., Court D.L., Ji X.;
"Purification, characterization and crystallization of ERA, an
essential GTPase from Escherichia coli.";
FEBS Lett. 445:425-430(1999).
[8]
PARTIAL PROTEIN SEQUENCE, SEQUENCE REVISION TO C-TERMINUS, AND
PHOSPHORYLATION AT THR-36 AND SER-37.
PubMed=8057845; DOI=10.1111/j.1365-2958.1994.tb01009.x;
Sood P., Lerner C.G., Shimamoto T., Lu Q., Inouye M.;
"Characterization of the autophosphorylation of Era, an essential
Escherichia coli GTPase.";
Mol. Microbiol. 12:201-208(1994).
[9]
DISRUPTION PHENOTYPE, AND OPERON STRUCTURE.
STRAIN=K12 / W3110;
PubMed=2540151; DOI=10.1128/jb.171.5.2581-2590.1989;
Takiff H.E., Chen S.M., Court D.L.;
"Genetic analysis of the rnc operon of Escherichia coli.";
J. Bacteriol. 171:2581-2590(1989).
[10]
DISRUPTION PHENOTYPE, MUTAGENESIS OF CYS-8, AND OPERON STRUCTURE.
STRAIN=K12;
PubMed=2527846; DOI=10.1128/jb.171.9.5017-5024.1989;
Inada T., Kawakami K., Chen S.M., Takiff H.E., Court D.L.,
Nakamura Y.;
"Temperature-sensitive lethal mutant of era, a G protein in
Escherichia coli.";
J. Bacteriol. 171:5017-5024(1989).
[11]
MUTAGENESIS OF PRO-17.
PubMed=1526446; DOI=10.1016/0378-1097(92)90419-O;
Lerner C.G., Sood P., Ahnn J., Inouye M.;
"Cold-sensitive growth and decreased GTP-hydrolytic activity from
substitution of Pro17 for Val in Era, an essential Escherichia coli
GTPase.";
FEMS Microbiol. Lett. 74:137-142(1992).
[12]
SUBCELLULAR LOCATION.
STRAIN=K12 / SB221;
PubMed=8282709; DOI=10.1128/jb.176.1.44-49.1994;
Lin Y.P., Sharer J.D., March P.E.;
"GTPase-dependent signaling in bacteria: characterization of a
membrane-binding site for era in Escherichia coli.";
J. Bacteriol. 176:44-49(1994).
[13]
MUTAGENESIS OF ASN-26; ALA-156 AND GLU-200.
PubMed=7729673; DOI=10.1111/j.1574-6968.1995.tb07432.x;
Lerner C.G., Gulati P.S., Inouye M.;
"Cold-sensitive conditional mutations in Era, an essential Escherichia
coli GTPase, isolated by localized random polymerase chain reaction
mutagenesis.";
FEMS Microbiol. Lett. 126:291-298(1995).
[14]
BIOPHYSICOCHEMICAL PROPERTIES, AUTOPHOSPHORYLATION, AND MUTAGENESIS OF
40-ALA--GLY-49 AND 42-THR-THR-43.
STRAIN=K12 / ATCC 35607 / JM83;
PubMed=8919456; DOI=10.1111/j.1574-6968.1996.tb08025.x;
Shimamoto T., Inouye M.;
"Mutational analysis of Era, an essential GTP-binding protein of
Escherichia coli.";
FEMS Microbiol. Lett. 136:57-62(1996).
[15]
IDENTIFICATION BY 2D-GEL.
PubMed=9298644; DOI=10.1002/elps.1150180805;
VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R.,
Neidhardt F.C.;
"Escherichia coli proteome analysis using the gene-protein database.";
Electrophoresis 18:1243-1251(1997).
[16]
SUPPRESSION OF DNA PRIMASE MUTATIONS.
PubMed=9093842;
Britton R.A., Lupski J.R.;
"Isolation and characterization of suppressors of two Escherichia coli
dnaG mutations, dnaG2903 and parB.";
Genetics 145:867-875(1997).
[17]
COLD-SENSITIVITY MUTANT SUPPRESSED BY RSMA.
STRAIN=K12 / ATCC 35607 / JM83;
PubMed=9748462;
Lu Q., Inouye M.;
"The gene for 16S rRNA methyltransferase (ksgA) functions as a
multicopy suppressor for a cold-sensitive mutant of era, an essential
RAS-like GTP-binding protein in Escherichia coli.";
J. Bacteriol. 180:5243-5246(1998).
[18]
FUNCTION IN CELL CYCLE, SUPPRESSION OF CELL CYCLE MUTATIONS,
MUTAGENESIS OF PRO-17, INDUCTION, AND DISRUPTION PHENOTYPE.
STRAIN=K12 / W3110;
PubMed=9515700; DOI=10.1046/j.1365-2958.1998.00719.x;
Britton R.A., Powell B.S., Dasgupta S., Sun Q., Margolin W.,
Lupski J.R., Court D.L.;
"Cell cycle arrest in Era GTPase mutants: a potential growth rate-
regulated checkpoint in Escherichia coli.";
Mol. Microbiol. 27:739-750(1998).
[19]
SMALL RRNA-BINDING, AND INTERACTION WITH 30S RIBOSOMAL SUBUNIT.
PubMed=10527840; DOI=10.1006/bbrc.1999.1471;
Sayed A., Matsuyama S., Inouye M.;
"Era, an essential Escherichia coli small G-protein, binds to the 30S
ribosomal subunit.";
Biochem. Biophys. Res. Commun. 264:51-54(1999).
[20]
GTP-BINDING, GDP-BINDING, AND GUANINE NUCLEOTIDE EXCHANGE RATES.
STRAIN=K12 / W3110;
PubMed=10852878; DOI=10.1128/JB.182.12.3460-3466.2000;
Sullivan S.M., Mishra R., Neubig R.R., Maddock J.R.;
"Analysis of guanine nucleotide binding and exchange kinetics of the
Escherichia coli GTPase Era.";
J. Bacteriol. 182:3460-3466(2000).
[21]
INTERACTION WITH MAZG.
PubMed=12218018; DOI=10.1128/JB.184.19.5323-5329.2002;
Zhang J., Inouye M.;
"MazG, a nucleoside triphosphate pyrophosphohydrolase, interacts with
Era, an essential GTPase in Escherichia coli.";
J. Bacteriol. 184:5323-5329(2002).
[22]
PROBABLE FUNCTION IN ENERGY METABOLISM.
STRAIN=K12 / DH5-alpha;
PubMed=12125819;
Inoue K., Chen J., Kato I., Inouye M.;
"Specific growth inhibition by acetate of an Escherichia coli strain
expressing Era-dE, a dominant negative Era mutant.";
J. Mol. Microbiol. Biotechnol. 4:379-388(2002).
[23]
FUNCTION IN RIBOSOME ASSEMBLY, FUNCTION IN RRNA PROCESSING, DEPLETION
STUDIES, MUTAGENESIS OF 39-LYS--GLY-49; 42-THR-THR-43 AND GLU-200, AND
SUPPRESSION OF RBFA DISRUPTION MUTANTS.
STRAIN=K12 / ATCC 35607 / JM83, and K12 / MC4100;
PubMed=12753192; DOI=10.1046/j.1365-2958.2003.03475.x;
Inoue K., Alsina J., Chen J., Inouye M.;
"Suppression of defective ribosome assembly in a rbfA deletion mutant
by overexpression of Era, an essential GTPase in Escherichia coli.";
Mol. Microbiol. 48:1005-1016(2003).
[24]
FUNCTION IN 30S RIBOSOMAL SUBUNIT BIOGENESIS, AND FUNCTION IN RRNA
PROCESSING.
STRAIN=K12 / ATCC 35607 / JM83, and K12 / MC4100;
PubMed=16825789; DOI=10.1159/000092818;
Inoue K., Chen J., Tan Q., Inouye M.;
"Era and RbfA have overlapping function in ribosome biogenesis in
Escherichia coli.";
J. Mol. Microbiol. Biotechnol. 11:41-52(2006).
[25]
PARTIALLY SUPPRESSES A RSGA MUTANT.
STRAIN=K12;
PubMed=18223068; DOI=10.1128/JB.01744-07;
Campbell T.L., Brown E.D.;
"Genetic interaction screens with ordered overexpression and deletion
clone sets implicate the Escherichia coli GTPase YjeQ in late ribosome
biogenesis.";
J. Bacteriol. 190:2537-2545(2008).
[26]
FUNCTION IN 30S SUBUNIT PROTEIN ASSEMBLY.
PubMed=20188109; DOI=10.1016/j.jmb.2010.02.036;
Bunner A.E., Nord S., Wikstrom P.M., Williamson J.R.;
"The effect of ribosome assembly cofactors on in vitro 30S subunit
reconstitution.";
J. Mol. Biol. 398:1-7(2010).
[27]
SUBUNIT.
STRAIN=K12 / BW25113;
PubMed=27382067; DOI=10.1093/nar/gkw613;
Thurlow B., Davis J.H., Leong V., Moraes T.F., Williamson J.R.,
Ortega J.;
"Binding properties of YjeQ (RsgA), RbfA, RimM and Era to assembly
intermediates of the 30S subunit.";
Nucleic Acids Res. 44:9918-9932(2016).
[28]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
STRAIN=K12 / W3110;
PubMed=10411886; DOI=10.1073/pnas.96.15.8396;
Chen X., Court D.L., Ji X.;
"Crystal structure of ERA: a GTPase-dependent cell cycle regulator
containing an RNA binding motif.";
Proc. Natl. Acad. Sci. U.S.A. 96:8396-8401(1999).
[29]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH GDP.
PubMed=19706445; DOI=10.1073/pnas.0904032106;
Tu C., Zhou X., Tropea J.E., Austin B.P., Waugh D.S., Court D.L.,
Ji X.;
"Structure of ERA in complex with the 3' end of 16S rRNA: implications
for ribosome biogenesis.";
Proc. Natl. Acad. Sci. U.S.A. 106:14843-14848(2009).
-!- FUNCTION: An essential GTPase that binds both GDP and GTP, with
nucleotide exchange occurring on the order of seconds whereas
hydrolysis occurs on the order of minutes. Plays a role in
numerous processes, including cell cycle regulation, energy
metabolism, as a chaperone for 16S rRNA processing and 30S
ribosomal subunit biogenesis. One of at least 4 proteins (Era,
RbfA, RimM and RsgA/YjeQ) that assist in the late assembly stage
of the 30S ribosomal subunit. Its presence in the 30S subunit may
prevent translation initiation. Seems to be critical for
maintaining cell growth and cell divison rates; a dramatic
reduction in Era protein levels temporarily arrests cell growth
just before cytokinesis (at the predivisional two-cell stage) and
delays cell division. Era mutant era1 suppresses some temperature-
sensitive mutations that affect DNA replication and chromosome
partitioning and segregation. The dominant-negative Era-de mutant
which is missing residues in a putative effector region, is unable
to complement the disruption mutant; upon overproduction it shows
a significant decrease in cell viability and a synthetic lethal
phenotype in the presence of acetate. Era function probably
overlaps RbfA (PubMed:16825789). Binds to the pre-30S ribosomal
subunit through several stages of protein assembly
(PubMed:20188109). {ECO:0000269|PubMed:12753192,
ECO:0000269|PubMed:16825789, ECO:0000269|PubMed:20188109,
ECO:0000269|PubMed:9515700}.
-!- ENZYME REGULATION: GTPase is competitively inhibited by GDP but
not by ADP, ATP, CTP or UTP. {ECO:0000269|PubMed:2105934}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=15.4 uM for GTP (for His-tagged protein at pH 8.0, 5 mM
MgCl(2)) {ECO:0000269|PubMed:2105934,
ECO:0000269|PubMed:8919456};
KM=9.0 uM for GTP (for overexpressed protein at pH 8.0, 5 mM
MgCl(2)) {ECO:0000269|PubMed:2105934,
ECO:0000269|PubMed:8919456};
-!- SUBUNIT: Monomer. Binds both 16S rRNA and 30S ribosomal subunits;
binding is inhibited by GDP and GTP (PubMed:10094501). Bind
preferentially to mature 30S ribosomal subunits over immature
subunits in the presence of GMP-PNP (PubMed:27382067). Binds to
MazG; GDP-bound Era binds more tightly to MazG than GTP-bound Era
(PubMed:19706445). {ECO:0000269|PubMed:10094501,
ECO:0000269|PubMed:19706445}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8282709}. Cell
inner membrane {ECO:0000269|PubMed:8282709}; Peripheral membrane
protein {ECO:0000269|PubMed:8282709}; Cytoplasmic side
{ECO:0000269|PubMed:8282709}. Note=Binding is GDP or GTP-
dependent, slightly more protein is bound in the presence of GTP
than GDP.
-!- INDUCTION: Expression increases as the growth rate increases.
Encoded in the rnc-era-recO operon. {ECO:0000269|PubMed:9515700}.
-!- PTM: Autophosphorylated. {ECO:0000269|PubMed:8919456}.
-!- MASS SPECTROMETRY: Mass=33682; Mass_error=5; Method=Electrospray;
Range=2-301; Evidence={ECO:0000269|PubMed:10094501};
-!- DISRUPTION PHENOTYPE: Lethality. In the presence of 1% protein
cells grow extremely slowly and are blocked at the predivisional
two-cell stage of the cell cycle. In the absence of Era and Rnc
there is an additional defect in chromosome partitioning. In
depletion experiments cells grow normally for 2 hours when protein
levels fall. After 4 hours 16S rRNA levels decrease with a
concomitant rise in the 17S precursor rRNA molecule (extra
sequences at both the 5' and 3' end compared to mature 16S rRNA)
and a loss of 70S ribosome assembly. {ECO:0000269|PubMed:2527846,
ECO:0000269|PubMed:2540151, ECO:0000269|PubMed:9515700}.
-!- MISCELLANEOUS: When overexpressed partially suppresses the slow
growth and decreased 70S ribosome phenotype of an rsgA knockout;
RsgA may be involved in 30S ribosomal subunit biogenesis
(PubMed:18223068). When overexpressed partially suppresses the 30S
ribosomal subunit assembly defects and cold-sensitivity of an rbfA
knockout; an era mutant missing residues 39-49 fully suppresses
these phenotypes (PubMed:12753192). Overexpression is not able to
suppress a rimM disruption phenotype nor a C23U mutation in 16S
rRNA. Also suppresses temperature-sensitive mutations in DNA
primase (PubMed:9093842). {ECO:0000269|PubMed:12753192,
ECO:0000269|PubMed:18223068, ECO:0000269|PubMed:9093842}.
-!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-
like GTPase superfamily. Era GTPase family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M14658; AAA03242.1; -; Unassigned_DNA.
EMBL; D64044; BAA10913.1; -; Genomic_DNA.
EMBL; U36841; AAA79828.1; -; Genomic_DNA.
EMBL; U00096; AAC75619.1; -; Genomic_DNA.
EMBL; AP009048; BAE76742.1; -; Genomic_DNA.
EMBL; X02673; CAA26505.1; -; Genomic_DNA.
PIR; S44713; RGECGT.
RefSeq; NP_417061.1; NC_000913.3.
RefSeq; WP_000020749.1; NZ_LN832404.1.
PDB; 1EGA; X-ray; 2.40 A; A/B=1-301.
PDB; 3IEU; X-ray; 2.80 A; A/B=1-301.
PDBsum; 1EGA; -.
PDBsum; 3IEU; -.
ProteinModelPortal; P06616; -.
SMR; P06616; -.
BioGrid; 4263220; 465.
DIP; DIP-9521N; -.
IntAct; P06616; 29.
STRING; 316385.ECDH10B_2734; -.
iPTMnet; P06616; -.
PaxDb; P06616; -.
PRIDE; P06616; -.
EnsemblBacteria; AAC75619; AAC75619; b2566.
EnsemblBacteria; BAE76742; BAE76742; BAE76742.
GeneID; 947036; -.
KEGG; ecj:JW2550; -.
KEGG; eco:b2566; -.
PATRIC; fig|1411691.4.peg.4168; -.
EchoBASE; EB0266; -.
EcoGene; EG10270; era.
eggNOG; ENOG4105CWT; Bacteria.
eggNOG; COG1159; LUCA.
HOGENOM; HOG000245597; -.
InParanoid; P06616; -.
KO; K03595; -.
OMA; KVAKDWQ; -.
PhylomeDB; P06616; -.
BioCyc; EcoCyc:EG10270-MONOMER; -.
BioCyc; MetaCyc:EG10270-MONOMER; -.
EvolutionaryTrace; P06616; -.
PRO; PR:P06616; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005737; C:cytoplasm; TAS:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:EcoCyc.
GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IDA:EcoCyc.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
GO; GO:0043024; F:ribosomal small subunit binding; IDA:UniProtKB.
GO; GO:0003723; F:RNA binding; IDA:EcoCyc.
GO; GO:0070181; F:small ribosomal subunit rRNA binding; IDA:UniProtKB.
GO; GO:0046777; P:protein autophosphorylation; IDA:EcoCyc.
GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
GO; GO:0042274; P:ribosomal small subunit biogenesis; IDA:EcoCyc.
CDD; cd04163; Era; 1.
Gene3D; 3.30.300.20; -; 1.
HAMAP; MF_00367; GTPase_Era; 1.
InterPro; IPR030388; G_ERA_dom.
InterPro; IPR005662; GTP-bd_Era.
InterPro; IPR006073; GTP_binding_domain.
InterPro; IPR015946; KH_dom-like_a/b.
InterPro; IPR004044; KH_dom_type_2.
InterPro; IPR009019; KH_sf_prok-type.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR005225; Small_GTP-bd_dom.
Pfam; PF07650; KH_2; 1.
Pfam; PF01926; MMR_HSR1; 1.
SUPFAM; SSF52540; SSF52540; 1.
SUPFAM; SSF54814; SSF54814; 1.
TIGRFAMs; TIGR00436; era; 1.
TIGRFAMs; TIGR00231; small_GTP; 1.
PROSITE; PS51713; G_ERA; 1.
PROSITE; PS50823; KH_TYPE_2; 1.
1: Evidence at protein level;
3D-structure; Cell inner membrane; Cell membrane; Complete proteome;
Cytoplasm; Direct protein sequencing; GTP-binding; Membrane;
Nucleotide-binding; Phosphoprotein; Reference proteome;
Ribosome biogenesis; RNA-binding; rRNA-binding.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:2105934}.
CHAIN 2 301 GTPase Era.
/FTId=PRO_0000180012.
DOMAIN 7 175 Era-type G.
DOMAIN 206 283 KH type-2.
NP_BIND 15 22 GTP.
NP_BIND 62 66 GTP.
NP_BIND 124 127 GTP.
MOD_RES 36 36 Phosphothreonine; by autocatalysis.
{ECO:0000269|PubMed:8057845}.
MOD_RES 37 37 Phosphoserine; by autocatalysis.
{ECO:0000269|PubMed:8057845}.
MUTAGEN 8 8 C->A: In era770; 20-fold reduction in
GTP-binding. Confers growth sensitivity
at 42 degrees Celsius; when associated
with an unpublished 22 residue
replacement in the C-terminus.
{ECO:0000269|PubMed:2527846}.
MUTAGEN 17 17 P->R: In era1; suppresses a number of
temperature-sensitive mutations affecting
cell cycle. {ECO:0000269|PubMed:1526446,
ECO:0000269|PubMed:9515700}.
MUTAGEN 17 17 P->V: Confers sensitivity to cold.
{ECO:0000269|PubMed:1526446,
ECO:0000269|PubMed:9515700}.
MUTAGEN 26 26 N->S: Confers sensitivity to cold;
overexpression does not suppress an rbfA
disruption. {ECO:0000269|PubMed:7729673}.
MUTAGEN 39 49 KAQTTRHRIVG->R: In Era-de; does not
complement a disruption mutant,
overexpression in a wt cells inhibits
growth. Binds GTP poorly, Km for GTP
increases 5-fold, Vmax for GTPase is 55%
that of wt. Does not autophosphorylate.
Complements cold-sensitivity and 16S rRNA
processing in an rbfA disruption mutant.
{ECO:0000269|PubMed:12753192}.
MUTAGEN 42 43 TT->AA: Does not complement a disruption
mutant, Km for GTP increases 12-fold,
Vmax for GTPase is 49% that of wt.
Overexpression partially suppresses an
rbfA disruption.
{ECO:0000269|PubMed:12753192,
ECO:0000269|PubMed:8919456}.
MUTAGEN 156 156 A->D: Confers sensitivity to cold;
overexpression partially suppresses an
rbfA disruption.
{ECO:0000269|PubMed:7729673}.
MUTAGEN 200 200 E->K: Confers sensitivity to cold, cells
do not divide properly but do replicate
DNA and segregate nucleoids normally. 16S
rRNA processing is decreased, ribosome
assembly is defective. Suppressed by
overexpression of RsmA. Overexpression
does not suppress an rbfA disruption,
while at 37 degrees Celsius the rbfA/era
E220K mutant grows very poorly, a
dominant-negative effect. This mutant
still binds 30S ribosomes.
{ECO:0000269|PubMed:12753192,
ECO:0000269|PubMed:7729673}.
STRAND 7 14 {ECO:0000244|PDB:1EGA}.
STRAND 16 20 {ECO:0000244|PDB:1EGA}.
HELIX 21 29 {ECO:0000244|PDB:1EGA}.
STRAND 32 35 {ECO:0000244|PDB:1EGA}.
STRAND 47 53 {ECO:0000244|PDB:1EGA}.
STRAND 56 65 {ECO:0000244|PDB:1EGA}.
HELIX 68 78 {ECO:0000244|PDB:1EGA}.
STRAND 89 97 {ECO:0000244|PDB:1EGA}.
HELIX 103 113 {ECO:0000244|PDB:1EGA}.
STRAND 114 117 {ECO:0000244|PDB:1EGA}.
STRAND 119 125 {ECO:0000244|PDB:1EGA}.
TURN 126 128 {ECO:0000244|PDB:1EGA}.
HELIX 132 143 {ECO:0000244|PDB:1EGA}.
STRAND 149 153 {ECO:0000244|PDB:1EGA}.
TURN 156 161 {ECO:0000244|PDB:1EGA}.
HELIX 162 170 {ECO:0000244|PDB:1EGA}.
HELIX 190 206 {ECO:0000244|PDB:1EGA}.
HELIX 207 209 {ECO:0000244|PDB:1EGA}.
STRAND 214 222 {ECO:0000244|PDB:1EGA}.
STRAND 228 239 {ECO:0000244|PDB:1EGA}.
HELIX 240 247 {ECO:0000244|PDB:1EGA}.
HELIX 249 251 {ECO:0000244|PDB:1EGA}.
HELIX 252 268 {ECO:0000244|PDB:1EGA}.
STRAND 273 281 {ECO:0000244|PDB:1EGA}.
HELIX 287 292 {ECO:0000244|PDB:1EGA}.
SEQUENCE 301 AA; 33810 MW; 53F275F07BDAE593 CRC64;
MSIDKSYCGF IAIVGRPNVG KSTLLNKLLG QKISITSRKA QTTRHRIVGI HTEGAYQAIY
VDTPGLHMEE KRAINRLMNK AASSSIGDVE LVIFVVEGTR WTPDDEMVLN KLREGKAPVI
LAVNKVDNVQ EKADLLPHLQ FLASQMNFLD IVPISAETGL NVDTIAAIVR KHLPEATHHF
PEDYITDRSQ RFMASEIIRE KLMRFLGAEL PYSVTVEIER FVSNERGGYD INGLILVERE
GQKKMVIGNK GAKIKTIGIE ARKDMQEMFE APVHLELWVK VKSGWADDER ALRSLGYVDD
L


Related products :

Catalog number Product name Quantity
EIAAB34770 ARHU,CDC42L1,CDC42-like GTPase 1,G28K,GTP-binding protein-like 1,Homo sapiens,Human,Rho GTPase-like protein ARHU,Rho-related GTP-binding protein RhoU,RHOU,Ryu GTPase,SB128,Wnt-1 responsive Cdc42 homol
EIAAB34774 ARHV,CDC42-like GTPase 2,GTP-binding protein-like 2,Homo sapiens,Human,Rho GTPase-like protein ARHV,Rho-related GTP-binding protein RhoV,RHOV,Wnt-1 responsive Cdc42 homolog 2,WRCH2,WRCH-2
EIAAB34654 ARHGAP1,CDC42 GTPase-activating protein,CDC42GAP,GTPase-activating protein rhoOGAP,Homo sapiens,Human,p50-RhoGAP,Rho GTPase-activating protein 1,RHOGAP1,Rho-related small GTPase protein activator,Rho-
30-409 SEPT10 is a member of the septin family of cytoskeletal proteins with GTPase activity. This protein localizes to the cytoplasm and nucleus and displays GTP-binding and GTPase activity.This gene encode 0.1 mg
EIAAB34669 ARHGAP10,GRAF2,Graf-related protein 2,GTPase regulator associated with focal adhesion kinase 2,Homo sapiens,Human,Rho GTPase-activating protein 10,Rho-type GTPase-activating protein 10
EIAAB34700 ARHGAP26,GRAF,GTPase regulator associated with focal adhesion kinase,Homo sapiens,Human,KIAA0621,Oligophrenin-1-like protein,OPHN1L,Rho GTPase-activating protein 26,Rho-type GTPase-activating protein
EIAAB34250 GES,GTPase-regulating endothelial cell sprouting,GTP-binding protein REM 1,Homo sapiens,Human,Rad and Gem-like GTP-binding protein 1,REM,REM1
EIAAB34717 Arhgap32,Brain-specific Rho GTPase-activating protein,GAB-associated Cdc42_Rac GTPase-activating protein,GC-GAP,Grit,Kiaa0712,Mouse,Mus musculus,p200RhoGAP,p250GAP,Rho GTPase-activating protein 32,Rho
EIAAB34719 ARHGAP33,Homo sapiens,Human,Rho GTPase-activating protein 33,Rho-type GTPase-activating protein 33,SNX26,Sorting nexin-26,Tc10_CDC42 GTPase-activating protein,TCGAP
EIAAB34718 Arhgap33,Mouse,Mus musculus,Rho GTPase-activating protein 33,Rho-type GTPase-activating protein 33,Snx26,Sorting nexin-26,Tc10_CDC42 GTPase-activating protein,Tcgap
EIAAB34716 ARHGAP32,Brain-specific Rho GTPase-activating protein,GAB-associated Cdc42_Rac GTPase-activating protein,GC-GAP,GRIT,GTPase regulator interacting with TrkA,Homo sapiens,Human,KIAA0712,p200RhoGAP,p250G
15-288-22382A Ras-GTPase-activating protein-binding protein 1 - EC 3.6.1.-; ATP-dependent DNA helicase VIII; GAP SH3-domain-binding protein 1; G3BP-1; HDH-VIII Polyclonal 0.05 mg
15-288-22382A Ras-GTPase-activating protein-binding protein 1 - EC 3.6.1.-; ATP-dependent DNA helicase VIII; GAP SH3-domain-binding protein 1; G3BP-1; HDH-VIII Polyclonal 0.1 mg
18-003-42840 Ras-GTPase-activating protein-binding protein 1 - EC 3.6.1.-; ATP-dependent DNA helicase VIII; GAP SH3-domain-binding protein 1; G3BP-1; HDH-VIII Polyclonal 0.1 mg Protein A
EIAAB34705 Arhgap27,Camgap1,CIN85-associated multi-domain-containing Rho GTPase-activating protein 1,Rat,Rattus norvegicus,Rho GTPase-activating protein 27,Rho-type GTPase-activating protein 27
EIAAB34703 Arhgap27,Camgap1,CIN85-associated multi-domain-containing Rho GTPase-activating protein 1,Mouse,Mus musculus,Rho GTPase-activating protein 27,Rho-type GTPase-activating protein 27
10-288-22382F Ras-GTPase-activating protein-binding protein 1 - EC 3.6.1.-; ATP-dependent DNA helicase VIII; GAP SH3-domain-binding protein 1; G3BP-1; HDH-VIII 0.1 mg
10-288-22382F Ras-GTPase-activating protein-binding protein 1 - EC 3.6.1.-; ATP-dependent DNA helicase VIII; GAP SH3-domain-binding protein 1; G3BP-1; HDH-VIII 0.05 mg
EIAAB34690 ARHGAP10,ARHGAP21,Homo sapiens,Human,KIAA1424,Rho GTPase-activating protein 10,Rho GTPase-activating protein 21,Rho-type GTPase-activating protein 21
EIAAB34689 Arhgap10,Arhgap21,Kiaa1424,Mouse,Mus musculus,Rho GTPase-activating protein 10,Rho GTPase-activating protein 21,Rho-type GTPase-activating protein 21
EIAAB34704 ARHGAP27,CAMGAP1,CIN85-associated multi-domain-containing Rho GTPase-activating protein 1,Homo sapiens,Human,PP905,Rho GTPase-activating protein 27,Rho-type GTPase-activating protein 27,SH3 domain-con
EIAAB34702 ARHGAP26,Chicken,Gallus gallus,GRAF,GTPase regulator associated with focal adhesion kinase,Rho GTPase-activating protein 26,Rho-type GTPase-activating protein 26
18-661-15189 Centaurin-gamma 1 - ARF-GAP with GTP-binding protein-like. ankyrin repeat and pleckstrin homology domains 2; AGAP-2; Phosphatidylinositol-3-kinase enhancer; PIKE; GTP-binding and GTPase-activating pro 0.1 mg
EIAAB34731 ARHGAP42,Homo sapiens,Human,Rho GTPase-activating protein 10-like,Rho GTPase-activating protein 42,Rho-type GTPase-activating protein 42
G3BP2-4826H Protein: Recombinant Human GTPase Activating Protein (SH3 Domain) Binding Protein 2, His-tagged 0.5mg


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur