ID   ERA_THEP1               Reviewed;         300 AA.
AC   A5IIT6;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=GTPase Era {ECO:0000255|HAMAP-Rule:MF_00367};
GN   Name=era {ECO:0000255|HAMAP-Rule:MF_00367}; OrderedLocusNames=Tpet_0080;
OS   Thermotoga petrophila (strain ATCC BAA-488 / DSM 13995 / JCM 10881 /
OS   RKU-1).
OC   Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX   NCBI_TaxID=390874;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-488 / DSM 13995 / JCM 10881 / RKU-1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Detter J.C., Han C.,
RA   Tapia R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Nelson K., Gogarten J.P., Noll K., Richardson P.;
RT   "Complete sequence of Thermotoga petrophila RKU-1.";
RL   Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: An essential GTPase that binds both GDP and GTP, with rapid
CC       nucleotide exchange. Plays a role in 16S rRNA processing and 30S
CC       ribosomal subunit biogenesis and possibly also in cell cycle regulation
CC       and energy metabolism. {ECO:0000255|HAMAP-Rule:MF_00367}.
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00367}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cell inner membrane
CC       {ECO:0000255|HAMAP-Rule:MF_00367}; Peripheral membrane protein
CC       {ECO:0000255|HAMAP-Rule:MF_00367}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC       GTPase superfamily. Era GTPase family. {ECO:0000255|HAMAP-
CC       Rule:MF_00367, ECO:0000255|PROSITE-ProRule:PRU01050}.
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DR   EMBL; CP000702; ABQ46109.1; -; Genomic_DNA.
DR   RefSeq; WP_011942783.1; NC_009486.1.
DR   AlphaFoldDB; A5IIT6; -.
DR   SMR; A5IIT6; -.
DR   STRING; 390874.Tpet_0080; -.
DR   EnsemblBacteria; ABQ46109; ABQ46109; Tpet_0080.
DR   KEGG; tpt:Tpet_0080; -.
DR   eggNOG; COG1159; Bacteria.
DR   HOGENOM; CLU_038009_1_0_0; -.
DR   OMA; WAEVDVI; -.
DR   Proteomes; UP000006558; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0070181; F:small ribosomal subunit rRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0042274; P:ribosomal small subunit biogenesis; IEA:UniProtKB-UniRule.
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   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Cytoplasm; GTP-binding; Membrane;
KW   Nucleotide-binding; Ribosome biogenesis; RNA-binding; rRNA-binding.
FT   CHAIN           1..300
FT                   /note="GTPase Era"
FT                   /id="PRO_1000079763"
FT   DOMAIN          4..172
FT                   /note="Era-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT   DOMAIN          195..280
FT                   /note="KH type-2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00367"
FT   REGION          12..19
FT                   /note="G1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT   REGION          38..42
FT                   /note="G2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT   REGION          59..62
FT                   /note="G3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT   REGION          121..124
FT                   /note="G4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT   REGION          151..153
FT                   /note="G5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT   BINDING         12..19
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00367"
FT   BINDING         59..63
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00367"
FT   BINDING         121..124
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00367"
SQ   SEQUENCE   300 AA;  33563 MW;  3F37A6F94B21F22A CRC64;
     MSIKSGFVAL AGKPNVGKST FINVVMGRKV VIVSDKPQTT RNRINCIYTD RDSQIIFVDT
     PGIHKPLHRL GEYMVKAAVQ ALKGVDLILF MLDAADGFTK TDEHVAKIVS ESGTKTIIAV
     NKIDVAGEEK AKAVGQLAKS MVENVVSVHY ISALKGEGVF EVLEKIKEEL PEGPQYYPED
     MVTDRPLSFM AAEIIREKIF HLTRQEVPHS TAVVIEEIKD RPNGVLYIRA NIYVERDSQK
     GILIGKNGSM IKKIGTLARE ELEFLVGRKV YLDLNVKVKE NWREKDFIIL QEIGLKDDIK