ERA_AQUAE
ID ERA_AQUAE Reviewed; 301 AA.
AC O67800;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=GTPase Era;
GN Name=era; Synonyms=era1; OrderedLocusNames=aq_1994;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN TERNARY COMPLEX WITH A GTP ANALOG
RP AND RNA, RRNA-BINDING, AND GTPASE ACTIVITY.
RX PubMed=19706445; DOI=10.1073/pnas.0904032106;
RA Tu C., Zhou X., Tropea J.E., Austin B.P., Waugh D.S., Court D.L., Ji X.;
RT "Structure of ERA in complex with the 3' end of 16S rRNA: implications for
RT ribosome biogenesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:14843-14848(2009).
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 (By similarity). The GTPase is stimulated about
CC 6-fold in the presence of a 12 nucleotide 16S rRNA C-terminal fragment.
CC Mutations in the rRNA sequence obviate stimulation. RNA-binding depends
CC on GTP-binding by the GTPase domain. May function as a checkpoint for
CC assembly of the 30S ribosomal subunit. {ECO:0000250}.
CC -!- SUBUNIT: Monomer. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cell inner membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC GTPase superfamily. Era GTPase family. {ECO:0000255|PROSITE-
CC ProRule:PRU01050, ECO:0000305}.
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DR EMBL; AE000657; AAC07768.1; -; Genomic_DNA.
DR PIR; D70471; D70471.
DR RefSeq; NP_214369.1; NC_000918.1.
DR RefSeq; WP_010881305.1; NC_000918.1.
DR PDB; 3IEV; X-ray; 1.90 A; A=1-301.
DR PDB; 3R9W; X-ray; 2.05 A; A=1-301.
DR PDB; 3R9X; X-ray; 2.80 A; A=1-301.
DR PDB; 7C1O; X-ray; 2.18 A; A=1-301.
DR PDBsum; 3IEV; -.
DR PDBsum; 3R9W; -.
DR PDBsum; 3R9X; -.
DR PDBsum; 7C1O; -.
DR AlphaFoldDB; O67800; -.
DR SMR; O67800; -.
DR STRING; 224324.aq_1994; -.
DR EnsemblBacteria; AAC07768; AAC07768; aq_1994.
DR KEGG; aae:aq_1994; -.
DR PATRIC; fig|224324.8.peg.1542; -.
DR eggNOG; COG1159; Bacteria.
DR HOGENOM; CLU_038009_1_0_0; -.
DR InParanoid; O67800; -.
DR OMA; WAEVDVI; -.
DR OrthoDB; 984717at2; -.
DR EvolutionaryTrace; O67800; -.
DR Proteomes; UP000000798; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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:0043024; F:ribosomal small subunit binding; IBA:GO_Central.
DR GO; GO:0019843; F:rRNA binding; IBA:GO_Central.
DR GO; GO:0070181; F:small ribosomal subunit rRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000028; P:ribosomal small subunit assembly; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Cytoplasm; GTP-binding;
KW Membrane; Nucleotide-binding; Reference proteome; Ribosome biogenesis;
KW RNA-binding; rRNA-binding.
FT CHAIN 1..301
FT /note="GTPase Era"
FT /id="PRO_0000179995"
FT DOMAIN 2..175
FT /note="Era-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT DOMAIN 206..285
FT /note="KH type-2"
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 58..61
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT REGION 123..126
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT REGION 154..156
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"
FT BINDING 58..62
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 123..126
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT STRAND 2..9
FT /evidence="ECO:0007829|PDB:3IEV"
FT HELIX 16..24
FT /evidence="ECO:0007829|PDB:3IEV"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:3IEV"
FT STRAND 42..48
FT /evidence="ECO:0007829|PDB:3IEV"
FT TURN 49..51
FT /evidence="ECO:0007829|PDB:3IEV"
FT STRAND 52..58
FT /evidence="ECO:0007829|PDB:3IEV"
FT HELIX 70..85
FT /evidence="ECO:0007829|PDB:3IEV"
FT STRAND 87..94
FT /evidence="ECO:0007829|PDB:3IEV"
FT TURN 95..97
FT /evidence="ECO:0007829|PDB:3IEV"
FT HELIX 101..110
FT /evidence="ECO:0007829|PDB:3IEV"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:3IEV"
FT STRAND 118..123
FT /evidence="ECO:0007829|PDB:3IEV"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:3IEV"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:3IEV"
FT HELIX 131..134
FT /evidence="ECO:0007829|PDB:3IEV"
FT HELIX 135..144
FT /evidence="ECO:0007829|PDB:3IEV"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:3IEV"
FT TURN 156..159
FT /evidence="ECO:0007829|PDB:3IEV"
FT HELIX 162..172
FT /evidence="ECO:0007829|PDB:3IEV"
FT HELIX 190..204
FT /evidence="ECO:0007829|PDB:3IEV"
FT HELIX 210..213
FT /evidence="ECO:0007829|PDB:3IEV"
FT STRAND 215..223
FT /evidence="ECO:0007829|PDB:3IEV"
FT STRAND 230..241
FT /evidence="ECO:0007829|PDB:3IEV"
FT HELIX 242..244
FT /evidence="ECO:0007829|PDB:3IEV"
FT HELIX 245..249
FT /evidence="ECO:0007829|PDB:3IEV"
FT HELIX 251..253
FT /evidence="ECO:0007829|PDB:3IEV"
FT HELIX 254..271
FT /evidence="ECO:0007829|PDB:3IEV"
FT STRAND 275..283
FT /evidence="ECO:0007829|PDB:3IEV"
FT HELIX 287..289
FT /evidence="ECO:0007829|PDB:3IEV"
FT HELIX 291..296
FT /evidence="ECO:0007829|PDB:3IEV"
SQ SEQUENCE 301 AA; 33888 MW; 7E32D92D744345B3 CRC64;
MKVGYVAIVG KPNVGKSTLL NNLLGTKVSI ISPKAGTTRM RVLGVKNIPN EAQIIFLDTP
GIYEPKKSDV LGHSMVEIAK QSLEEADVIL FMIDATEGWR PRDEEIYQNF IKPLNKPVIV
VINKIDKIGP AKNVLPLIDE IHKKHPELTE IVPISALKGA NLDELVKTIL KYLPEGEPLF
PEDMITDLPL RLLAAEIVRE KAMMLTREEV PTSIAVKINE IKPGDANPNM LVIKGEIIVD
RENLKPIIIG KKGQRLKEIG KRARQELELI LGRPVYLELW VKVVPDWRRR PEYVRLFGYA
L
