ID ERA_DINSH Reviewed; 308 AA.
AC A8LLE0;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE RecName: Full=GTPase Era {ECO:0000255|HAMAP-Rule:MF_00367};
GN Name=era {ECO:0000255|HAMAP-Rule:MF_00367}; OrderedLocusNames=Dshi_0201;
OS Dinoroseobacter shibae (strain DSM 16493 / NCIMB 14021 / DFL 12).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Dinoroseobacter.
OX NCBI_TaxID=398580;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16493 / NCIMB 14021 / DFL 12;
RX PubMed=19741735; DOI=10.1038/ismej.2009.94;
RA Wagner-Dobler I., Ballhausen B., Berger M., Brinkhoff T., Buchholz I.,
RA Bunk B., Cypionka H., Daniel R., Drepper T., Gerdts G., Hahnke S., Han C.,
RA Jahn D., Kalhoefer D., Kiss H., Klenk H.P., Kyrpides N., Liebl W.,
RA Liesegang H., Meincke L., Pati A., Petersen J., Piekarski T.,
RA Pommerenke C., Pradella S., Pukall R., Rabus R., Stackebrandt E., Thole S.,
RA Thompson L., Tielen P., Tomasch J., von Jan M., Wanphrut N., Wichels A.,
RA Zech H., Simon M.;
RT "The complete genome sequence of the algal symbiont Dinoroseobacter shibae:
RT a hitchhiker's guide to life in the sea.";
RL ISME J. 4:61-77(2010).
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; CP000830; ABV91950.1; -; Genomic_DNA.
DR RefSeq; WP_012176883.1; NC_009952.1.
DR AlphaFoldDB; A8LLE0; -.
DR SMR; A8LLE0; -.
DR STRING; 398580.Dshi_0201; -.
DR KEGG; dsh:Dshi_0201; -.
DR eggNOG; COG1159; Bacteria.
DR HOGENOM; CLU_038009_1_1_5; -.
DR OrthoDB; 9805918at2; -.
DR Proteomes; UP000006833; 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 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 inner membrane; Cell membrane; Cytoplasm; GTP-binding; Membrane;
KW Nucleotide-binding; Reference proteome; Ribosome biogenesis; RNA-binding;
KW rRNA-binding.
FT CHAIN 1..308
FT /note="GTPase Era"
FT /id="PRO_1000079685"
FT DOMAIN 9..179
FT /note="Era-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT DOMAIN 210..287
FT /note="KH type-2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00367"
FT REGION 17..24
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT REGION 43..47
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT REGION 64..67
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT REGION 129..132
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT REGION 158..160
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT BINDING 17..24
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00367"
FT BINDING 64..68
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00367"
FT BINDING 129..132
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00367"
SQ SEQUENCE 308 AA; 34262 MW; 8722AF8358AFCEE8 CRC64;
MTENAAPTRA GFVALIGEPN AGKSTLTNAM VGAKVSIVTH KVQTTRARIR GVALEGAAQI
VFVDTPGLFR PRRRLDRAMV AAAWGGAADA DIVVLMVEAH RGMTDGVRAI LETLNERRDP
KQIVALAINK IDRVKSEVLL KLTQDLNAAY PFAETFMISA EKGYGVADLR AWLGASLPEG
PWMYPEDQIA DVPLRMIAAE ITREKLTLRL HQELPYQLTV ETENWEERKD GSVRIDQVVY
VMRDGHKGIL LGHKGETAKA VSKAAREELV EFLGRKVHLF LQVKVRPNWL EEKERFDEMG
LDFRDGNA
//
