ID   ERA_NEIMF               Reviewed;         307 AA.
AC   A1KSV0;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=GTPase Era {ECO:0000255|HAMAP-Rule:MF_00367};
GN   Name=era {ECO:0000255|HAMAP-Rule:MF_00367}; OrderedLocusNames=NMC0638;
OS   Neisseria meningitidis serogroup C / serotype 2a (strain ATCC 700532 / DSM
OS   15464 / FAM18).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=272831;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700532 / DSM 15464 / FAM18;
RX   PubMed=17305430; DOI=10.1371/journal.pgen.0030023;
RA   Bentley S.D., Vernikos G.S., Snyder L.A.S., Churcher C., Arrowsmith C.,
RA   Chillingworth T., Cronin A., Davis P.H., Holroyd N.E., Jagels K.,
RA   Maddison M., Moule S., Rabbinowitsch E., Sharp S., Unwin L., Whitehead S.,
RA   Quail M.A., Achtman M., Barrell B.G., Saunders N.J., Parkhill J.;
RT   "Meningococcal genetic variation mechanisms viewed through comparative
RT   analysis of serogroup C strain FAM18.";
RL   PLoS Genet. 3:230-240(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; AM421808; CAM09931.1; -; Genomic_DNA.
DR   RefSeq; WP_002222780.1; NC_008767.1.
DR   AlphaFoldDB; A1KSV0; -.
DR   SMR; A1KSV0; -.
DR   PRIDE; A1KSV0; -.
DR   EnsemblBacteria; CAM09931; CAM09931; NMC0638.
DR   KEGG; nmc:NMC0638; -.
DR   HOGENOM; CLU_038009_1_2_4; -.
DR   OMA; WAEVDVI; -.
DR   OrthoDB; 984717at2; -.
DR   Proteomes; UP000002286; 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; Ribosome biogenesis; RNA-binding; rRNA-binding.
FT   CHAIN           1..307
FT                   /note="GTPase Era"
FT                   /id="PRO_1000079716"
FT   DOMAIN          17..186
FT                   /note="Era-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT   DOMAIN          217..293
FT                   /note="KH type-2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00367"
FT   REGION          25..32
FT                   /note="G1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT   REGION          51..55
FT                   /note="G2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT   REGION          72..75
FT                   /note="G3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT   REGION          133..136
FT                   /note="G4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT   REGION          165..167
FT                   /note="G5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT   BINDING         25..32
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00367"
FT   BINDING         72..76
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00367"
FT   BINDING         133..136
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00367"
SQ   SEQUENCE   307 AA;  34617 MW;  ABD7C680C6DDED28 CRC64;
     MDIETFLAGE RAAGGYRCGF VAIVGRPNVG KSTLMNHLIG QKISITSKKA QTTRNRVTGI
     YTDDTAQFVF VDTPGFQTDH RNALNDRLNQ NVTEALGGVD VVVFVVEAMR FTDADRVVLK
     QLPKHTPVIL VVNKIDKDKA KDRYALEAFV AQVRAEFEFA AAEAVSAKHG LRIANLLELL
     KPYLPESVPM YPEDMVTDKS ARFLAMEIVR EKLFRYLGEE LPYAMNVEVE QFEEEDGLNR
     IYIAVLVDKE SQKAILIGKG GERLKKISTE ARLDMEKLFD TKVFLKVWVK VKSGWADDIR
     FLRELGL