ERA_ECOLI
ID ERA_ECOLI Reviewed; 301 AA.
AC P06616; Q2MAG4;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 2.
DT 03-AUG-2022, entry version 204.
DE RecName: Full=GTPase Era;
DE Short=ERA;
DE AltName: Full=GTP-binding protein Era;
GN Name=era; Synonyms=rbaA, sdgE; OrderedLocusNames=b2566, JW2550;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND GTP-BINDING.
RX PubMed=3097637; DOI=10.1073/pnas.83.23.8849;
RA Ahnn J., March P.E., Takiff H.E., Inouye M.;
RT "A GTP-binding protein of Escherichia coli has homology to yeast RAS
RT proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:8849-8853(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / W3110;
RA Nashimoto H., Saito N.;
RL Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-50.
RC STRAIN=K12 / CS520;
RX PubMed=3895158; DOI=10.1093/nar/13.13.4677;
RA March P.E., Ahnn J., Inouye M.;
RT "The DNA sequence of the gene (rnc) encoding ribonuclease III of
RT Escherichia coli.";
RL Nucleic Acids Res. 13:4677-4685(1985).
RN [6]
RP PROTEIN SEQUENCE OF 2-40, GTP-BINDING, GDP-BINDING, CATALYTIC ACTIVITY,
RP ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=K12 / W3110;
RX PubMed=2105934; DOI=10.1016/s0021-9258(19)39884-9;
RA Chen S.M., Takiff H.E., Barber A.M., Dubois G.C., Bardwell J.C.,
RA Court D.L.;
RT "Expression and characterization of RNase III and Era proteins. Products of
RT the rnc operon of Escherichia coli.";
RL J. Biol. Chem. 265:2888-2895(1990).
RN [7]
RP PROTEIN SEQUENCE OF N-TERMINUS, MASS SPECTROMETRY, GTPASE ACTIVITY,
RP SUBUNIT, AND PRELIMINARY CRYSTALLIZATION.
RC STRAIN=K12 / W3110;
RX PubMed=10094501; DOI=10.1016/s0014-5793(99)00178-7;
RA Chen X., Chen S.M., Powell B.S., Court D.L., Ji X.;
RT "Purification, characterization and crystallization of ERA, an essential
RT GTPase from Escherichia coli.";
RL FEBS Lett. 445:425-430(1999).
RN [8]
RP PARTIAL PROTEIN SEQUENCE, SEQUENCE REVISION TO C-TERMINUS, AND
RP PHOSPHORYLATION AT THR-36 AND SER-37.
RX PubMed=8057845; DOI=10.1111/j.1365-2958.1994.tb01009.x;
RA Sood P., Lerner C.G., Shimamoto T., Lu Q., Inouye M.;
RT "Characterization of the autophosphorylation of Era, an essential
RT Escherichia coli GTPase.";
RL Mol. Microbiol. 12:201-208(1994).
RN [9]
RP DISRUPTION PHENOTYPE, AND OPERON STRUCTURE.
RC STRAIN=K12 / W3110;
RX PubMed=2540151; DOI=10.1128/jb.171.5.2581-2590.1989;
RA Takiff H.E., Chen S.M., Court D.L.;
RT "Genetic analysis of the rnc operon of Escherichia coli.";
RL J. Bacteriol. 171:2581-2590(1989).
RN [10]
RP DISRUPTION PHENOTYPE, MUTAGENESIS OF CYS-8, AND OPERON STRUCTURE.
RC STRAIN=K12;
RX PubMed=2527846; DOI=10.1128/jb.171.9.5017-5024.1989;
RA Inada T., Kawakami K., Chen S.M., Takiff H.E., Court D.L., Nakamura Y.;
RT "Temperature-sensitive lethal mutant of era, a G protein in Escherichia
RT coli.";
RL J. Bacteriol. 171:5017-5024(1989).
RN [11]
RP MUTAGENESIS OF PRO-17.
RX PubMed=1526446; DOI=10.1016/0378-1097(92)90419-o;
RA Lerner C.G., Sood P., Ahnn J., Inouye M.;
RT "Cold-sensitive growth and decreased GTP-hydrolytic activity from
RT substitution of Pro17 for Val in Era, an essential Escherichia coli
RT GTPase.";
RL FEMS Microbiol. Lett. 74:137-142(1992).
RN [12]
RP SUBCELLULAR LOCATION.
RC STRAIN=K12 / SB221;
RX PubMed=8282709; DOI=10.1128/jb.176.1.44-49.1994;
RA Lin Y.P., Sharer J.D., March P.E.;
RT "GTPase-dependent signaling in bacteria: characterization of a membrane-
RT binding site for era in Escherichia coli.";
RL J. Bacteriol. 176:44-49(1994).
RN [13]
RP MUTAGENESIS OF ASN-26; ALA-156 AND GLU-200.
RX PubMed=7729673; DOI=10.1111/j.1574-6968.1995.tb07432.x;
RA Lerner C.G., Gulati P.S., Inouye M.;
RT "Cold-sensitive conditional mutations in Era, an essential Escherichia coli
RT GTPase, isolated by localized random polymerase chain reaction
RT mutagenesis.";
RL FEMS Microbiol. Lett. 126:291-298(1995).
RN [14]
RP BIOPHYSICOCHEMICAL PROPERTIES, AUTOPHOSPHORYLATION, AND MUTAGENESIS OF
RP 40-ALA--GLY-49 AND 42-THR-THR-43.
RC STRAIN=K12 / ATCC 35607 / JM83;
RX PubMed=8919456; DOI=10.1111/j.1574-6968.1996.tb08025.x;
RA Shimamoto T., Inouye M.;
RT "Mutational analysis of Era, an essential GTP-binding protein of
RT Escherichia coli.";
RL FEMS Microbiol. Lett. 136:57-62(1996).
RN [15]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [16]
RP SUPPRESSION OF DNA PRIMASE MUTATIONS.
RX PubMed=9093842; DOI=10.1093/genetics/145.4.867;
RA Britton R.A., Lupski J.R.;
RT "Isolation and characterization of suppressors of two Escherichia coli dnaG
RT mutations, dnaG2903 and parB.";
RL Genetics 145:867-875(1997).
RN [17]
RP COLD-SENSITIVITY MUTANT SUPPRESSED BY RSMA.
RC STRAIN=K12 / ATCC 35607 / JM83;
RX PubMed=9748462; DOI=10.1128/jb.180.19.5243-5246.1998;
RA Lu Q., Inouye M.;
RT "The gene for 16S rRNA methyltransferase (ksgA) functions as a multicopy
RT suppressor for a cold-sensitive mutant of era, an essential RAS-like GTP-
RT binding protein in Escherichia coli.";
RL J. Bacteriol. 180:5243-5246(1998).
RN [18]
RP FUNCTION IN CELL CYCLE, SUPPRESSION OF CELL CYCLE MUTATIONS, MUTAGENESIS OF
RP PRO-17, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / W3110;
RX PubMed=9515700; DOI=10.1046/j.1365-2958.1998.00719.x;
RA Britton R.A., Powell B.S., Dasgupta S., Sun Q., Margolin W., Lupski J.R.,
RA Court D.L.;
RT "Cell cycle arrest in Era GTPase mutants: a potential growth rate-regulated
RT checkpoint in Escherichia coli.";
RL Mol. Microbiol. 27:739-750(1998).
RN [19]
RP SMALL RRNA-BINDING, AND INTERACTION WITH 30S RIBOSOMAL SUBUNIT.
RX PubMed=10527840; DOI=10.1006/bbrc.1999.1471;
RA Sayed A., Matsuyama S., Inouye M.;
RT "Era, an essential Escherichia coli small G-protein, binds to the 30S
RT ribosomal subunit.";
RL Biochem. Biophys. Res. Commun. 264:51-54(1999).
RN [20]
RP GTP-BINDING, GDP-BINDING, AND GUANINE NUCLEOTIDE EXCHANGE RATES.
RC STRAIN=K12 / W3110;
RX PubMed=10852878; DOI=10.1128/jb.182.12.3460-3466.2000;
RA Sullivan S.M., Mishra R., Neubig R.R., Maddock J.R.;
RT "Analysis of guanine nucleotide binding and exchange kinetics of the
RT Escherichia coli GTPase Era.";
RL J. Bacteriol. 182:3460-3466(2000).
RN [21]
RP INTERACTION WITH MAZG.
RX PubMed=12218018; DOI=10.1128/jb.184.19.5323-5329.2002;
RA Zhang J., Inouye M.;
RT "MazG, a nucleoside triphosphate pyrophosphohydrolase, interacts with Era,
RT an essential GTPase in Escherichia coli.";
RL J. Bacteriol. 184:5323-5329(2002).
RN [22]
RP PROBABLE FUNCTION IN ENERGY METABOLISM.
RC STRAIN=K12 / DH5-alpha;
RX PubMed=12125819;
RA Inoue K., Chen J., Kato I., Inouye M.;
RT "Specific growth inhibition by acetate of an Escherichia coli strain
RT expressing Era-dE, a dominant negative Era mutant.";
RL J. Mol. Microbiol. Biotechnol. 4:379-388(2002).
RN [23]
RP FUNCTION IN RIBOSOME ASSEMBLY, FUNCTION IN RRNA PROCESSING, DEPLETION
RP STUDIES, MUTAGENESIS OF 39-LYS--GLY-49; 42-THR-THR-43 AND GLU-200, AND
RP SUPPRESSION OF RBFA DISRUPTION MUTANTS.
RC STRAIN=K12 / ATCC 35607 / JM83, and K12 / MC4100;
RX PubMed=12753192; DOI=10.1046/j.1365-2958.2003.03475.x;
RA Inoue K., Alsina J., Chen J., Inouye M.;
RT "Suppression of defective ribosome assembly in a rbfA deletion mutant by
RT overexpression of Era, an essential GTPase in Escherichia coli.";
RL Mol. Microbiol. 48:1005-1016(2003).
RN [24]
RP FUNCTION IN 30S RIBOSOMAL SUBUNIT BIOGENESIS, AND FUNCTION IN RRNA
RP PROCESSING.
RC STRAIN=K12 / ATCC 35607 / JM83, and K12 / MC4100;
RX PubMed=16825789; DOI=10.1159/000092818;
RA Inoue K., Chen J., Tan Q., Inouye M.;
RT "Era and RbfA have overlapping function in ribosome biogenesis in
RT Escherichia coli.";
RL J. Mol. Microbiol. Biotechnol. 11:41-52(2006).
RN [25]
RP PARTIALLY SUPPRESSES A RSGA MUTANT.
RC STRAIN=K12;
RX PubMed=18223068; DOI=10.1128/jb.01744-07;
RA Campbell T.L., Brown E.D.;
RT "Genetic interaction screens with ordered overexpression and deletion clone
RT sets implicate the Escherichia coli GTPase YjeQ in late ribosome
RT biogenesis.";
RL J. Bacteriol. 190:2537-2545(2008).
RN [26]
RP FUNCTION IN 30S SUBUNIT PROTEIN ASSEMBLY.
RX PubMed=20188109; DOI=10.1016/j.jmb.2010.02.036;
RA Bunner A.E., Nord S., Wikstrom P.M., Williamson J.R.;
RT "The effect of ribosome assembly cofactors on in vitro 30S subunit
RT reconstitution.";
RL J. Mol. Biol. 398:1-7(2010).
RN [27]
RP SUBUNIT.
RC STRAIN=K12 / BW25113;
RX PubMed=27382067; DOI=10.1093/nar/gkw613;
RA Thurlow B., Davis J.H., Leong V., Moraes T.F., Williamson J.R., Ortega J.;
RT "Binding properties of YjeQ (RsgA), RbfA, RimM and Era to assembly
RT intermediates of the 30S subunit.";
RL Nucleic Acids Res. 44:9918-9932(2016).
RN [28]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RC STRAIN=K12 / W3110;
RX PubMed=10411886; DOI=10.1073/pnas.96.15.8396;
RA Chen X., Court D.L., Ji X.;
RT "Crystal structure of ERA: a GTPase-dependent cell cycle regulator
RT containing an RNA binding motif.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:8396-8401(1999).
RN [29]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH GDP.
RX PubMed=19706445; DOI=10.1073/pnas.0904032106;
RA Tu C., Zhou X., Tropea J.E., Austin B.P., Waugh D.S., Court D.L., Ji X.;
RT "Structure of ERA in complex with the 3' end of 16S rRNA: implications for
RT ribosome biogenesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:14843-14848(2009).
CC -!- FUNCTION: An essential GTPase that binds both GDP and GTP, with
CC nucleotide exchange occurring on the order of seconds whereas
CC hydrolysis occurs on the order of minutes. Plays a role in numerous
CC processes, including cell cycle regulation, energy metabolism, as a
CC chaperone for 16S rRNA processing and 30S ribosomal subunit biogenesis.
CC One of at least 4 proteins (Era, RbfA, RimM and RsgA/YjeQ) that assist
CC in the late assembly stage of the 30S ribosomal subunit. Its presence
CC in the 30S subunit may prevent translation initiation. Seems to be
CC critical for maintaining cell growth and cell divison rates; a dramatic
CC reduction in Era protein levels temporarily arrests cell growth just
CC before cytokinesis (at the predivisional two-cell stage) and delays
CC cell division. Era mutant era1 suppresses some temperature-sensitive
CC mutations that affect DNA replication and chromosome partitioning and
CC segregation. The dominant-negative Era-de mutant which is missing
CC residues in a putative effector region, is unable to complement the
CC disruption mutant; upon overproduction it shows a significant decrease
CC in cell viability and a synthetic lethal phenotype in the presence of
CC acetate. Era function probably overlaps RbfA (PubMed:16825789). Binds
CC to the pre-30S ribosomal subunit through several stages of protein
CC assembly (PubMed:20188109). {ECO:0000269|PubMed:12753192,
CC ECO:0000269|PubMed:16825789, ECO:0000269|PubMed:20188109,
CC ECO:0000269|PubMed:9515700}.
CC -!- ACTIVITY REGULATION: GTPase is competitively inhibited by GDP but not
CC by ADP, ATP, CTP or UTP. {ECO:0000269|PubMed:2105934}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=15.4 uM for GTP (for His-tagged protein at pH 8.0, 5 mM MgCl(2))
CC {ECO:0000269|PubMed:2105934, ECO:0000269|PubMed:8919456};
CC KM=9.0 uM for GTP (for overexpressed protein at pH 8.0, 5 mM MgCl(2))
CC {ECO:0000269|PubMed:2105934, ECO:0000269|PubMed:8919456};
CC -!- SUBUNIT: Monomer. Binds both 16S rRNA and 30S ribosomal subunits;
CC binding is inhibited by GDP and GTP (PubMed:10094501). Bind
CC preferentially to mature 30S ribosomal subunits over immature subunits
CC in the presence of GMP-PNP (PubMed:27382067). Binds to MazG; GDP-bound
CC Era binds more tightly to MazG than GTP-bound Era (PubMed:19706445).
CC {ECO:0000269|PubMed:10094501, ECO:0000269|PubMed:19706445}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8282709}. Cell
CC inner membrane {ECO:0000269|PubMed:8282709}; Peripheral membrane
CC protein {ECO:0000269|PubMed:8282709}; Cytoplasmic side
CC {ECO:0000269|PubMed:8282709}. Note=Binding is GDP or GTP-dependent,
CC slightly more protein is bound in the presence of GTP than GDP.
CC -!- INDUCTION: Expression increases as the growth rate increases. Encoded
CC in the rnc-era-recO operon. {ECO:0000269|PubMed:9515700}.
CC -!- PTM: Autophosphorylated. {ECO:0000269|PubMed:8919456}.
CC -!- MASS SPECTROMETRY: Mass=33682; Mass_error=5; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:10094501};
CC -!- DISRUPTION PHENOTYPE: Lethality. In the presence of 1% protein cells
CC grow extremely slowly and are blocked at the predivisional two-cell
CC stage of the cell cycle. In the absence of Era and Rnc there is an
CC additional defect in chromosome partitioning. In depletion experiments
CC cells grow normally for 2 hours when protein levels fall. After 4 hours
CC 16S rRNA levels decrease with a concomitant rise in the 17S precursor
CC rRNA molecule (extra sequences at both the 5' and 3' end compared to
CC mature 16S rRNA) and a loss of 70S ribosome assembly.
CC {ECO:0000269|PubMed:2527846, ECO:0000269|PubMed:2540151,
CC ECO:0000269|PubMed:9515700}.
CC -!- MISCELLANEOUS: When overexpressed partially suppresses the slow growth
CC and decreased 70S ribosome phenotype of an rsgA knockout; RsgA may be
CC involved in 30S ribosomal subunit biogenesis (PubMed:18223068). When
CC overexpressed partially suppresses the 30S ribosomal subunit assembly
CC defects and cold-sensitivity of an rbfA knockout; an era mutant missing
CC residues 39-49 fully suppresses these phenotypes (PubMed:12753192).
CC Overexpression is not able to suppress a rimM disruption phenotype nor
CC a C23U mutation in 16S rRNA. Also suppresses temperature-sensitive
CC mutations in DNA primase (PubMed:9093842).
CC {ECO:0000269|PubMed:12753192, ECO:0000269|PubMed:18223068,
CC ECO:0000269|PubMed:9093842}.
CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC GTPase superfamily. Era GTPase family. {ECO:0000255|PROSITE-
CC ProRule:PRU01050, ECO:0000305}.
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DR EMBL; M14658; AAA03242.1; -; Unassigned_DNA.
DR EMBL; D64044; BAA10913.1; -; Genomic_DNA.
DR EMBL; U36841; AAA79828.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75619.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76742.1; -; Genomic_DNA.
DR EMBL; X02673; CAA26505.1; -; Genomic_DNA.
DR PIR; S44713; RGECGT.
DR RefSeq; NP_417061.1; NC_000913.3.
DR RefSeq; WP_000020749.1; NZ_STEB01000011.1.
DR PDB; 1EGA; X-ray; 2.40 A; A/B=1-301.
DR PDB; 3IEU; X-ray; 2.80 A; A/B=1-301.
DR PDBsum; 1EGA; -.
DR PDBsum; 3IEU; -.
DR AlphaFoldDB; P06616; -.
DR SMR; P06616; -.
DR BioGRID; 4263220; 465.
DR BioGRID; 851375; 7.
DR DIP; DIP-9521N; -.
DR IntAct; P06616; 29.
DR STRING; 511145.b2566; -.
DR iPTMnet; P06616; -.
DR jPOST; P06616; -.
DR PaxDb; P06616; -.
DR PRIDE; P06616; -.
DR EnsemblBacteria; AAC75619; AAC75619; b2566.
DR EnsemblBacteria; BAE76742; BAE76742; BAE76742.
DR GeneID; 58391288; -.
DR GeneID; 947036; -.
DR KEGG; ecj:JW2550; -.
DR KEGG; eco:b2566; -.
DR PATRIC; fig|1411691.4.peg.4168; -.
DR EchoBASE; EB0266; -.
DR eggNOG; COG1159; Bacteria.
DR HOGENOM; CLU_038009_1_2_6; -.
DR InParanoid; P06616; -.
DR OMA; WAEVDVI; -.
DR PhylomeDB; P06616; -.
DR BioCyc; EcoCyc:EG10270-MON; -.
DR BioCyc; MetaCyc:EG10270-MON; -.
DR SABIO-RK; P06616; -.
DR EvolutionaryTrace; P06616; -.
DR PRO; PR:P06616; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; TAS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IDA:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
DR GO; GO:0097216; F:guanosine tetraphosphate binding; IDA:EcoCyc.
DR GO; GO:0043024; F:ribosomal small subunit binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IDA:EcoCyc.
DR GO; GO:0019843; F:rRNA binding; IBA:GO_Central.
DR GO; GO:0070181; F:small ribosomal subunit rRNA binding; IDA:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:EcoCyc.
DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0000028; P:ribosomal small subunit assembly; IDA:EcoCyc.
DR GO; GO:0042274; P:ribosomal small subunit biogenesis; IDA:EcoCyc.
DR CDD; cd04163; Era; 1.
DR Gene3D; 3.30.300.20; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00367; GTPase_Era; 1.
DR InterPro; IPR030388; G_ERA_dom.
DR InterPro; IPR006073; GTP-bd.
DR InterPro; IPR005662; GTP-bd_Era.
DR InterPro; IPR015946; KH_dom-like_a/b.
DR InterPro; IPR004044; KH_dom_type_2.
DR InterPro; IPR009019; KH_sf_prok-type.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR PANTHER; PTHR42698; PTHR42698; 1.
DR Pfam; PF07650; KH_2; 1.
DR Pfam; PF01926; MMR_HSR1; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54814; SSF54814; 1.
DR TIGRFAMs; TIGR00436; era; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51713; G_ERA; 1.
DR PROSITE; PS50823; KH_TYPE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Cytoplasm;
KW Direct protein sequencing; GTP-binding; Membrane; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Ribosome biogenesis; RNA-binding;
KW rRNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2105934"
FT CHAIN 2..301
FT /note="GTPase Era"
FT /id="PRO_0000180012"
FT DOMAIN 7..175
FT /note="Era-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT DOMAIN 206..283
FT /note="KH type-2"
FT REGION 15..22
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT REGION 41..45
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT REGION 62..65
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT REGION 124..127
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT REGION 154..156
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT BINDING 15..22
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT BINDING 62..66
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT BINDING 124..127
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT MOD_RES 36
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:8057845"
FT MOD_RES 37
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:8057845"
FT MUTAGEN 8
FT /note="C->A: In era770; 20-fold reduction in GTP-binding.
FT Confers growth sensitivity at 42 degrees Celsius; when
FT associated with an unpublished 22 residue replacement in
FT the C-terminus."
FT /evidence="ECO:0000269|PubMed:2527846"
FT MUTAGEN 17
FT /note="P->R: In era1; suppresses a number of temperature-
FT sensitive mutations affecting cell cycle."
FT /evidence="ECO:0000269|PubMed:1526446,
FT ECO:0000269|PubMed:9515700"
FT MUTAGEN 17
FT /note="P->V: Confers sensitivity to cold."
FT /evidence="ECO:0000269|PubMed:1526446,
FT ECO:0000269|PubMed:9515700"
FT MUTAGEN 26
FT /note="N->S: Confers sensitivity to cold; overexpression
FT does not suppress an rbfA disruption."
FT /evidence="ECO:0000269|PubMed:7729673"
FT MUTAGEN 39..49
FT /note="KAQTTRHRIVG->R: In Era-de; does not complement a
FT disruption mutant, overexpression in a wt cells inhibits
FT growth. Binds GTP poorly, Km for GTP increases 5-fold, Vmax
FT for GTPase is 55% that of wt. Does not autophosphorylate.
FT Complements cold-sensitivity and 16S rRNA processing in an
FT rbfA disruption mutant."
FT /evidence="ECO:0000269|PubMed:12753192"
FT MUTAGEN 42..43
FT /note="TT->AA: Does not complement a disruption mutant, Km
FT for GTP increases 12-fold, Vmax for GTPase is 49% that of
FT wt. Overexpression partially suppresses an rbfA
FT disruption."
FT /evidence="ECO:0000269|PubMed:12753192,
FT ECO:0000269|PubMed:8919456"
FT MUTAGEN 156
FT /note="A->D: Confers sensitivity to cold; overexpression
FT partially suppresses an rbfA disruption."
FT /evidence="ECO:0000269|PubMed:7729673"
FT MUTAGEN 200
FT /note="E->K: Confers sensitivity to cold, cells do not
FT divide properly but do replicate DNA and segregate
FT nucleoids normally. 16S rRNA processing is decreased,
FT ribosome assembly is defective. Suppressed by
FT overexpression of RsmA. Overexpression does not suppress an
FT rbfA disruption, while at 37 degrees Celsius the rbfA/era
FT E220K mutant grows very poorly, a dominant-negative effect.
FT This mutant still binds 30S ribosomes."
FT /evidence="ECO:0000269|PubMed:12753192,
FT ECO:0000269|PubMed:7729673"
FT STRAND 7..14
FT /evidence="ECO:0007829|PDB:1EGA"
FT STRAND 16..20
FT /evidence="ECO:0007829|PDB:1EGA"
FT HELIX 21..29
FT /evidence="ECO:0007829|PDB:1EGA"
FT STRAND 32..35
FT /evidence="ECO:0007829|PDB:1EGA"
FT STRAND 47..53
FT /evidence="ECO:0007829|PDB:1EGA"
FT STRAND 56..65
FT /evidence="ECO:0007829|PDB:1EGA"
FT HELIX 68..78
FT /evidence="ECO:0007829|PDB:1EGA"
FT STRAND 89..97
FT /evidence="ECO:0007829|PDB:1EGA"
FT HELIX 103..113
FT /evidence="ECO:0007829|PDB:1EGA"
FT STRAND 114..117
FT /evidence="ECO:0007829|PDB:1EGA"
FT STRAND 119..125
FT /evidence="ECO:0007829|PDB:1EGA"
FT TURN 126..128
FT /evidence="ECO:0007829|PDB:1EGA"
FT HELIX 132..143
FT /evidence="ECO:0007829|PDB:1EGA"
FT STRAND 149..153
FT /evidence="ECO:0007829|PDB:1EGA"
FT TURN 156..161
FT /evidence="ECO:0007829|PDB:1EGA"
FT HELIX 162..170
FT /evidence="ECO:0007829|PDB:1EGA"
FT HELIX 190..206
FT /evidence="ECO:0007829|PDB:1EGA"
FT HELIX 207..209
FT /evidence="ECO:0007829|PDB:1EGA"
FT STRAND 214..222
FT /evidence="ECO:0007829|PDB:1EGA"
FT STRAND 228..239
FT /evidence="ECO:0007829|PDB:1EGA"
FT HELIX 240..247
FT /evidence="ECO:0007829|PDB:1EGA"
FT HELIX 249..251
FT /evidence="ECO:0007829|PDB:1EGA"
FT HELIX 252..268
FT /evidence="ECO:0007829|PDB:1EGA"
FT STRAND 273..281
FT /evidence="ECO:0007829|PDB:1EGA"
FT HELIX 287..292
FT /evidence="ECO:0007829|PDB:1EGA"
SQ 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
