ID   ERA_CORDI               Reviewed;         305 AA.
AC   Q6NG20;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=GTPase Era {ECO:0000255|HAMAP-Rule:MF_00367};
GN   Name=era {ECO:0000255|HAMAP-Rule:MF_00367}; OrderedLocusNames=DIP1714;
OS   Corynebacterium diphtheriae (strain ATCC 700971 / NCTC 13129 / Biotype
OS   gravis).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=257309;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700971 / NCTC 13129 / Biotype gravis;
RX   PubMed=14602910; DOI=10.1093/nar/gkg874;
RA   Cerdeno-Tarraga A.-M., Efstratiou A., Dover L.G., Holden M.T.G.,
RA   Pallen M.J., Bentley S.D., Besra G.S., Churcher C.M., James K.D.,
RA   De Zoysa A., Chillingworth T., Cronin A., Dowd L., Feltwell T., Hamlin N.,
RA   Holroyd S., Jagels K., Moule S., Quail M.A., Rabbinowitsch E.,
RA   Rutherford K.M., Thomson N.R., Unwin L., Whitehead S., Barrell B.G.,
RA   Parkhill J.;
RT   "The complete genome sequence and analysis of Corynebacterium diphtheriae
RT   NCTC13129.";
RL   Nucleic Acids Res. 31:6516-6523(2003).
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 membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00367}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC       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; BX248359; CAE50243.1; -; Genomic_DNA.
DR   RefSeq; WP_003852330.1; NC_002935.2.
DR   AlphaFoldDB; Q6NG20; -.
DR   SMR; Q6NG20; -.
DR   STRING; 257309.DIP1714; -.
DR   EnsemblBacteria; CAE50243; CAE50243; DIP1714.
DR   GeneID; 29421643; -.
DR   KEGG; cdi:DIP1714; -.
DR   HOGENOM; CLU_038009_0_2_11; -.
DR   OMA; WAEVDVI; -.
DR   OrthoDB; 984717at2; -.
DR   Proteomes; UP000002198; 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   PRINTS; PR00326; GTP1OBG.
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 membrane; Cytoplasm; GTP-binding; Membrane; Nucleotide-binding;
KW   Reference proteome; Ribosome biogenesis; RNA-binding; rRNA-binding.
FT   CHAIN           1..305
FT                   /note="GTPase Era"
FT                   /id="PRO_1000079679"
FT   DOMAIN          11..181
FT                   /note="Era-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT   DOMAIN          212..291
FT                   /note="KH type-2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00367"
FT   REGION          19..26
FT                   /note="G1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT   REGION          45..49
FT                   /note="G2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT   REGION          66..69
FT                   /note="G3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT   REGION          130..133
FT                   /note="G4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT   REGION          160..162
FT                   /note="G5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT   BINDING         19..26
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00367"
FT   BINDING         66..70
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00367"
FT   BINDING         130..133
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00367"
SQ   SEQUENCE   305 AA;  33742 MW;  88743A85B11668A6 CRC64;
     MSFTDTPEGF RSGFISFVGR PNTGKSTLTN ALVGEKIAIT ANQPETTRHP IRGIVHREDA
     QIIVVDTPGL HKPRTLLGER LNEVVKDTYA DMDLIAITVP ADEKIGPGDR WILDAVKKVA
     PKTPLLGIVT KVDKASRDQV AVQLMELHEL LGGNSEVVPV SAVTGEQRDV LLDVITRLLP
     EGPKFYPDDH ITDDDTETRL SELIREAALS GLKDELPHSV AVQIDEILPN DEREGVLDVH
     AVIYVERPGQ KSILIGKDGR RLGRIIHNAR PEIIKILGSN VYLDLRIKVL KNWQQDPKQL
     GRLGF