ID A0A316AA12_9ACTN Unreviewed; 319 AA.
AC A0A316AA12;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
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=BXY45_109120 {ECO:0000313|EMBL:PWJ54038.1};
OS Quadrisphaera granulorum.
OC Bacteria; Actinomycetota; Actinomycetes; Kineosporiales; Kineosporiaceae;
OC Quadrisphaera.
OX NCBI_TaxID=317664 {ECO:0000313|EMBL:PWJ54038.1, ECO:0000313|Proteomes:UP000245469};
RN [1] {ECO:0000313|EMBL:PWJ54038.1, ECO:0000313|Proteomes:UP000245469}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44889 {ECO:0000313|EMBL:PWJ54038.1,
RC ECO:0000313|Proteomes:UP000245469};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (MAR-2018) 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:PWJ54038.1}.
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DR EMBL; QGDQ01000009; PWJ54038.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A316AA12; -.
DR Proteomes; UP000245469; 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 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:UP000245469};
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 17..191
FT /note="Era-type G"
FT /evidence="ECO:0000259|PROSITE:PS51713"
FT DOMAIN 222..305
FT /note="KH type-2"
FT /evidence="ECO:0000259|PROSITE:PS50823"
FT REGION 25..32
FT /note="G1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01050"
FT REGION 51..55
FT /note="G2"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01050"
FT REGION 72..75
FT /note="G3"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01050"
FT REGION 135..138
FT /note="G4"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01050"
FT REGION 170..172
FT /note="G5"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01050"
FT BINDING 25..32
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00367"
FT BINDING 72..76
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00367"
FT BINDING 135..138
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00367"
SQ SEQUENCE 319 AA; 34481 MW; 124C42A5A60DA072 CRC64;
MITDNSSPTE RGPDEHRSGF ACLVGRPNAG KSTLTNALVG EKVAITSSRP QTTRHTVRGV
VHRPDAQLVL VDTPGLHRPR TLLGQRLNDL VLATLSEVDV IAFCLPADER AGPGDRWIAA
QLAEVRRTPV VAVVTKTDKV DRGRLAERLL EVTAMGEEDG HRPFADVVPV SATGDFQVGA
VADVLCSHLP PGPPLYPEGE LTDEPEAVMV AELVREAALE GVRDELPHSL AVVVDEMTPR
LGEDGEPTGL LEVHVLLYVE RDSQKGIVIG RGGARLKEVG TTARQGIEAL LGTRVHLDLR
VKVAKDWQRD PRQLARLGF
//