ID A0A239I340_9RHOB Unreviewed; 302 AA.
AC A0A239I340;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=GTPase Era {ECO:0000256|ARBA:ARBA00020484, ECO:0000256|HAMAP-Rule:MF_00367};
GN Name=era {ECO:0000256|HAMAP-Rule:MF_00367};
GN ORFNames=SAMN05421757_104180 {ECO:0000313|EMBL:SNS88007.1};
OS Tropicimonas sediminicola.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Tropicimonas.
OX NCBI_TaxID=1031541 {ECO:0000313|EMBL:SNS88007.1, ECO:0000313|Proteomes:UP000198426};
RN [1] {ECO:0000313|EMBL:SNS88007.1, ECO:0000313|Proteomes:UP000198426}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 29339 {ECO:0000313|EMBL:SNS88007.1,
RC ECO:0000313|Proteomes:UP000198426};
RA Kim H.J., Triplett B.A.;
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-Rule:MF_00367}.
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00367}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00367}. Cell
CC membrane {ECO:0000256|HAMAP-Rule:MF_00367}; Peripheral membrane protein
CC {ECO:0000256|HAMAP-Rule:MF_00367}.
CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC GTPase superfamily. Era GTPase family. {ECO:0000256|ARBA:ARBA00007921,
CC ECO:0000256|HAMAP-Rule:MF_00367, ECO:0000256|PROSITE-ProRule:PRU01050,
CC ECO:0000256|RuleBase:RU003761}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FZOY01000004; SNS88007.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A239I340; -.
DR OrthoDB; 9805918at2; -.
DR Proteomes; UP000198426; Unassembled WGS sequence.
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 CDD; cd22534; KH-II_Era; 1.
DR Gene3D; 3.30.300.20; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_00367; GTPase_Era; 1.
DR InterPro; IPR030388; G_ERA_dom.
DR InterPro; IPR006073; GTP-bd.
DR InterPro; IPR005662; GTPase_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 NCBIfam; TIGR00436; era; 1.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR42698; GTPASE ERA; 1.
DR PANTHER; PTHR42698:SF2; GTPASE ERA-LIKE, CHLOROPLASTIC; 1.
DR Pfam; PF07650; KH_2; 1.
DR Pfam; PF01926; MMR_HSR1; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF54814; Prokaryotic type KH domain (KH-domain type II); 1.
DR PROSITE; PS51713; G_ERA; 1.
DR PROSITE; PS50823; KH_TYPE_2; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_00367};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00367};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW Rule:MF_00367}; Membrane {ECO:0000256|HAMAP-Rule:MF_00367};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00367}; Reference proteome {ECO:0000313|Proteomes:UP000198426};
KW Ribosome biogenesis {ECO:0000256|HAMAP-Rule:MF_00367};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_00367}; rRNA-binding {ECO:0000256|HAMAP-Rule:MF_00367}.
FT DOMAIN 4..173
FT /note="Era-type G"
FT /evidence="ECO:0000259|PROSITE:PS51713"
FT DOMAIN 204..281
FT /note="KH type-2"
FT /evidence="ECO:0000259|PROSITE:PS50823"
FT REGION 12..19
FT /note="G1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01050"
FT REGION 38..42
FT /note="G2"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01050"
FT REGION 59..62
FT /note="G3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01050"
FT REGION 123..126
FT /note="G4"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01050"
FT REGION 152..154
FT /note="G5"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01050"
FT BINDING 12..19
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00367"
FT BINDING 59..63
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00367"
FT BINDING 123..126
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00367"
SQ SEQUENCE 302 AA; 33542 MW; B9F496AEB6E5DB37 CRC64;
MSTRCGFVAL IGEPNAGKST LLNAMVGAKV SIVTHKVQTT RARIRGVALE GESQIVFVDT
PGLFRPRRRL DRAMVAAAWG GAADADIVVL LIEAHRGLTE GVKAILEALK ERGSGQTVAL
AINKIDRVKS ETLLALTKEM NEAYPFVETY LISAEKGYGV DDLREWLAGA LPEGPWLYPE
DQLSDLPMRM IAAEMTREKL TLRLHQELPY QLTVETENWE ERKDGSARID QVIYVARDGH
KGIVLGKGGE TIKAVSQAAR AELEEFLDRK VHLFLQVKVR PNWLEEAERY SEMGLDFKDG
NS
//
