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Database: UniProt
Entry: A0A1I4G9D1_9FIRM
LinkDB: A0A1I4G9D1_9FIRM
Original site: A0A1I4G9D1_9FIRM 
ID   A0A1I4G9D1_9FIRM        Unreviewed;       293 AA.
AC   A0A1I4G9D1;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
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=SAMN02983006_00648 {ECO:0000313|EMBL:SFL26163.1};
OS   Halanaerobium salsuginis.
OC   Bacteria; Bacillota; Clostridia; Halanaerobiales; Halanaerobiaceae;
OC   Halanaerobium.
OX   NCBI_TaxID=29563 {ECO:0000313|EMBL:SFL26163.1, ECO:0000313|Proteomes:UP000199006};
RN   [1] {ECO:0000313|EMBL:SFL26163.1, ECO:0000313|Proteomes:UP000199006}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51327 {ECO:0000313|EMBL:SFL26163.1,
RC   ECO:0000313|Proteomes:UP000199006};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; FOTI01000005; SFL26163.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I4G9D1; -.
DR   STRING; 29563.SAMN02983006_00648; -.
DR   OrthoDB; 9805918at2; -.
DR   Proteomes; UP000199006; 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:SF1; GTPASE ERA, MITOCHONDRIAL; 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};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, 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:UP000199006};
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..170
FT                   /note="Era-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51713"
FT   DOMAIN          201..278
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          121..124
FT                   /note="G4"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01050"
FT   REGION          149..151
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         121..124
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00367"
SQ   SEQUENCE   293 AA;  34023 MW;  E16A27F913F86CEC CRC64;
     MSYKSGFVTI IGRPNVGKST LINQLIGEKI NIISPRPQTT RNSIKAIYTA ENGQVIFIDT
     PGIHQPRNEL DNYMLEAAYN SLEGIDLIIF ILDGSTYWGK NDQLIYDQIK NNSNKIIFVM
     NKIDKLSAQD LVKKQQQYSQ KVGQEVIPIS ALNKKNIDTL LMEVFDFLPE GPQYYPADMI
     TDQIERFVFA EMIREKIFYL TRDEVPYGVA VIVEEVKERQ NDDYYIRANI YVEKKSHKGI
     IIGKNGKMLK KIGQQARKEI ENLLQTKVYL DLWVKILKDW REKDNLLKRM GYK
//
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