ID A0A1Q4YM63_9ACTN Unreviewed; 321 AA.
AC A0A1Q4YM63;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=A6A29_11955 {ECO:0000313|EMBL:OKI35620.1};
OS Streptomyces sp. TSRI0281.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1718998 {ECO:0000313|EMBL:OKI35620.1, ECO:0000313|Proteomes:UP000186952};
RN [1] {ECO:0000313|EMBL:OKI35620.1, ECO:0000313|Proteomes:UP000186952}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TSRI0281 {ECO:0000313|EMBL:OKI35620.1,
RC ECO:0000313|Proteomes:UP000186952};
RX PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL MBio 7:e02104-e02116(2016).
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:OKI35620.1}.
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DR EMBL; LWLE01000033; OKI35620.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q4YM63; -.
DR STRING; 1718998.A6A29_11955; -.
DR OrthoDB; 9805918at2; -.
DR Proteomes; UP000186952; 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:UP000186952};
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..194
FT /note="Era-type G"
FT /evidence="ECO:0000259|PROSITE:PS51713"
FT DOMAIN 225..307
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 139..142
FT /note="G4"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01050"
FT REGION 173..175
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 139..142
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00367"
SQ SEQUENCE 321 AA; 35216 MW; DCECFB6229624135 CRC64;
MSARPNPEAA AQQAENNAPH RAGFACFVGR PNAGKSTLTN ALVGQKVAIT SNRPQTTRHT
VRGIVHRDDA QLILVDTPGL HKPRTLLGER LNDVVRTTWA EVDVIGFCLP ADQKLGPGDK
FIIKELAGIK KTPKIAIITK TDLVDSKALA EQLLAVSRLG EELGFEWAEI VPVSAVKDQQ
VSLLADLIAP LLPESPPLYP EGDLTDEPEM VMVAELIREA ALEGVRDELP HSIAVVVEEM
LPREDRPADK PLLDIHANVY IERPSQKGII IGPKGKRLKE VGTKSRKHIE ALLGTPVFLD
LHVKVAKDWQ RDPKQLRKLG F
//
