ID A0A2Z5T0C8_9CYAN Unreviewed; 314 AA.
AC A0A2Z5T0C8;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
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 ECO:0000313|EMBL:BBA80001.1};
GN ORFNames=RGRSB_1586 {ECO:0000313|EMBL:BBA80001.1};
OS cyanobacterium endosymbiont of Rhopalodia gibberula.
OC Bacteria; Cyanobacteriota.
OX NCBI_TaxID=1763363 {ECO:0000313|EMBL:BBA80001.1, ECO:0000313|Proteomes:UP000264686};
RN [1] {ECO:0000313|EMBL:BBA80001.1, ECO:0000313|Proteomes:UP000264686}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RgSB {ECO:0000313|EMBL:BBA80001.1};
RX PubMed=29026213; DOI=10.1038/s41598-017-13578-8;
RA Nakayama T., Inagaki Y.;
RT "Genomic divergence within non-photosynthetic cyanobacterial endosymbionts
RT in rhopalodiacean diatoms.";
RL Sci. Rep. 7:13075-13075(2017).
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}.
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DR EMBL; AP018341; BBA80001.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2Z5T0C8; -.
DR KEGG; cer:RGRSB_1586; -.
DR OrthoDB; 9805918at2; -.
DR Proteomes; UP000264686; 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 PRINTS; PR00326; GTP1OBG.
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:UP000264686};
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 21..190
FT /note="Era-type G"
FT /evidence="ECO:0000259|PROSITE:PS51713"
FT DOMAIN 212..296
FT /note="KH type-2"
FT /evidence="ECO:0000259|PROSITE:PS50823"
FT REGION 29..36
FT /note="G1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01050"
FT REGION 55..59
FT /note="G2"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01050"
FT REGION 76..79
FT /note="G3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01050"
FT REGION 138..141
FT /note="G4"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01050"
FT REGION 168..170
FT /note="G5"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01050"
FT BINDING 29..36
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00367"
FT BINDING 76..80
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00367"
FT BINDING 138..141
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00367"
SQ SEQUENCE 314 AA; 34563 MW; 4FA092BAF11BA0D4 CRC64;
MSHESELISL STVPTAPAGF KSGFVGIIGR PNVGKSTLMN QLVGQKIAIT SPISQTTRNR
LRGILTTEEA QIILIDTPGI HKPHHQLGKI LVRNAKSAIN SVDIVLFIVD SSVPAGGGDH
YVSELLGTST NPVILGLNKT DQQPSDYYSL DKSYSILARP YNWPVIKFSA LTGEGLDLLQ
KALINNLAPG PYYYPPNLVT DQPEHFIMGE LIREQILKQT SQEIPHSVAI FIEKVEETSN
LTCVFAAINV ERDSQKGIII GKKGNMLKAI GSAAREQIQK LIMGEVYLKL FVKVKPKWRQ
SSLYLSEFGY HIES
//
