ID   ERA_CAMJ8               Reviewed;         291 AA.
AC   A8FL79;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=GTPase Era {ECO:0000255|HAMAP-Rule:MF_00367};
GN   Name=era {ECO:0000255|HAMAP-Rule:MF_00367}; OrderedLocusNames=C8J_0617;
OS   Campylobacter jejuni subsp. jejuni serotype O:6 (strain 81116 / NCTC
OS   11828).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=407148;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=81116 / NCTC 11828;
RX   PubMed=17873037; DOI=10.1128/jb.01404-07;
RA   Pearson B.M., Gaskin D.J.H., Segers R.P.A.M., Wells J.M., Nuijten P.J.M.,
RA   van Vliet A.H.M.;
RT   "The complete genome sequence of Campylobacter jejuni strain 81116
RT   (NCTC11828).";
RL   J. Bacteriol. 189:8402-8403(2007).
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; CP000814; ABV52216.1; -; Genomic_DNA.
DR   RefSeq; WP_002866516.1; NC_009839.1.
DR   AlphaFoldDB; A8FL79; -.
DR   SMR; A8FL79; -.
DR   KEGG; cju:C8J_0617; -.
DR   HOGENOM; CLU_038009_1_0_7; -.
DR   OMA; WAEVDVI; -.
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..291
FT                   /note="GTPase Era"
FT                   /id="PRO_1000079666"
FT   DOMAIN          2..167
FT                   /note="Era-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT   DOMAIN          186..274
FT                   /note="KH type-2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00367"
FT   REGION          10..17
FT                   /note="G1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT   REGION          36..40
FT                   /note="G2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT   REGION          57..60
FT                   /note="G3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT   REGION          116..119
FT                   /note="G4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT   REGION          146..148
FT                   /note="G5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT   BINDING         10..17
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00367"
FT   BINDING         57..61
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00367"
FT   BINDING         116..119
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00367"
SQ   SEQUENCE   291 AA;  33140 MW;  D5579FF5B838BD14 CRC64;
     MKSGFVSIIG RTNAGKSTLI NSLLEEKIAL VSHKQNATRR KIKAIVMHEK NQIIFIDTPG
     LHESGATLNQ LLVQSAIKSM GDCDVILFVA SVFDSTKDYE NFLSLNPQVP HIIALNKVDL
     TDNATLLKKL SEYAKFSQHF KAIIPYSSKK KSYKKGLLDE IVKYLDKHEY FYDPEFLSAS
     SEKELYRDFI LESIYENLSD ELPYSSEVLI HRTKDTPNLL ILEANIITDT NSHKGMLIGK
     EGATLKRIGK DARFKISKLA QKKVLLKLFV TVKKNWQKDE EFLKKLLNDE N