ID   ERA_PASMU               Reviewed;         306 AA.
AC   Q9CPH8;
DT   04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT   04-MAY-2001, sequence version 1.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=GTPase Era {ECO:0000255|HAMAP-Rule:MF_00367};
GN   Name=era {ECO:0000255|HAMAP-Rule:MF_00367}; OrderedLocusNames=PM0060;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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; AE004439; AAK02144.1; -; Genomic_DNA.
DR   RefSeq; WP_010906461.1; NC_002663.1.
DR   AlphaFoldDB; Q9CPH8; -.
DR   SMR; Q9CPH8; -.
DR   STRING; 747.DR93_2013; -.
DR   EnsemblBacteria; AAK02144; AAK02144; PM0060.
DR   KEGG; pmu:PM0060; -.
DR   HOGENOM; CLU_038009_1_0_6; -.
DR   OMA; WAEVDVI; -.
DR   Proteomes; UP000000809; 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 inner membrane; Cell membrane; Cytoplasm; GTP-binding; Membrane;
KW   Nucleotide-binding; Reference proteome; Ribosome biogenesis; RNA-binding;
KW   rRNA-binding.
FT   CHAIN           1..306
FT                   /note="GTPase Era"
FT                   /id="PRO_0000180035"
FT   DOMAIN          13..181
FT                   /note="Era-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT   DOMAIN          212..289
FT                   /note="KH type-2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00367"
FT   REGION          21..28
FT                   /note="G1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT   REGION          47..51
FT                   /note="G2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT   REGION          68..71
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         21..28
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00367"
FT   BINDING         68..72
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   306 AA;  34714 MW;  FE86B17655C0C74D CRC64;
     MNEIKTADNA KTYCGFIAIV GRPNVGKSTL LNKILGQKIS ITSRKAQTTR HRIVGIHTDG
     PYQAVYVDTP GLHIEEKRAI NRLMNRAASS AIGDVDLIIF VVDGTHWNED DEMVLNKLRA
     AKAPVVLAIN KIDNIKNKEE MLPFITELTS KFDFAHVVPI SAQGGKNIAE LEKIVRESLH
     EGTHHFPEEY VTDRSQRFMA SEIIREKLMR FTGDELPYSV TVEIEQFKLN ERGTYEINGL
     ILVEREGQKK MVIGNKGQKI KQIGIEARAD MERLFDNKVH LELWVKVKSG WADDERALRS
     LGYMDE