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Database: UniProt
Entry: H0R0T6_9ACTN
LinkDB: H0R0T6_9ACTN
Original site: H0R0T6_9ACTN 
ID   H0R0T6_9ACTN            Unreviewed;       308 AA.
AC   H0R0T6;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 65.
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:GAB18687.1};
GN   ORFNames=GOEFS_061_00260 {ECO:0000313|EMBL:GAB18687.1};
OS   Gordonia effusa NBRC 100432.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC   Gordonia.
OX   NCBI_TaxID=1077974 {ECO:0000313|EMBL:GAB18687.1, ECO:0000313|Proteomes:UP000035034};
RN   [1] {ECO:0000313|EMBL:GAB18687.1, ECO:0000313|Proteomes:UP000035034}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 100432 {ECO:0000313|EMBL:GAB18687.1,
RC   ECO:0000313|Proteomes:UP000035034};
RA   Yoshida I., Takarada H., Hosoyama A., Tsuchikane K., Katsumata H.,
RA   Yamazaki S., Fujita N.;
RT   "Whole genome shotgun sequence of Gordonia effusa NBRC 100432.";
RL   Submitted (DEC-2011) 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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GAB18687.1}.
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DR   EMBL; BAEH01000061; GAB18687.1; -; Genomic_DNA.
DR   RefSeq; WP_007318023.1; NZ_BAEH01000061.1.
DR   AlphaFoldDB; H0R0T6; -.
DR   STRING; 1077974.GOEFS_061_00260; -.
DR   eggNOG; COG1159; Bacteria.
DR   OrthoDB; 9805918at2; -.
DR   Proteomes; UP000035034; 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:UP000035034};
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          10..180
FT                   /note="Era-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51713"
FT   DOMAIN          211..294
FT                   /note="KH type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS50823"
FT   REGION          18..25
FT                   /note="G1"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01050"
FT   REGION          44..48
FT                   /note="G2"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01050"
FT   REGION          65..68
FT                   /note="G3"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01050"
FT   REGION          129..132
FT                   /note="G4"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01050"
FT   REGION          159..161
FT                   /note="G5"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01050"
FT   BINDING         18..25
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00367"
FT   BINDING         65..69
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00367"
FT   BINDING         129..132
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00367"
SQ   SEQUENCE   308 AA;  33698 MW;  0ADE47242706630F CRC64;
     MTDHDTPEFR SGFVCFVGRP NTGKSTLTNA LVGEKIAITS NRPQTTRHTI RGIVNRPDAQ
     LILVDTPGLH RPRTLLGQRL NDLVRDTYSE VDVIGVCIPA DEAIGPGDRW IVEQVRTMAP
     STTVIGVLTK IDKVAPPSVA KQLLALSNLL GPEAEVVPVS AKSGAQLDVL ADVLVGLMAP
     GPAFYPDGEL TDEPEQVLMA EFIREAALEG VRDELPHSLA VTIDEVIPRE DRREDQAPMV
     DVHAILYVER DSQKGIVIGH KGSRLKHVGT VARGQIEALL GTKVFLDLRV KVAKDWQRDP
     KQLRRMGF
//
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