ERA_PSEAE
ID ERA_PSEAE Reviewed; 305 AA.
AC Q9XCX8;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 08-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=GTPase Era {ECO:0000255|HAMAP-Rule:MF_00367};
GN Name=era {ECO:0000255|HAMAP-Rule:MF_00367}; OrderedLocusNames=PA0771;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=PAK;
RX PubMed=10438789; DOI=10.1128/jb.181.16.5111-5113.1999;
RA Powell B.S., Peters H.K. III, Nakamura Y., Court D.L.;
RT "Cloning and analysis of the rnc-era-recO operon from Pseudomonas
RT aeruginosa.";
RL J. Bacteriol. 181:5111-5113(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
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:0000255|HAMAP-Rule:MF_00367}.
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00367}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cell inner membrane
CC {ECO:0000255|HAMAP-Rule:MF_00367}; Peripheral membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_00367}.
CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC GTPase superfamily. Era GTPase family. {ECO:0000255|HAMAP-
CC Rule:MF_00367, ECO:0000255|PROSITE-ProRule:PRU01050}.
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DR EMBL; AF123492; AAD40230.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG04160.1; -; Genomic_DNA.
DR PIR; F83548; F83548.
DR RefSeq; NP_249462.1; NC_002516.2.
DR RefSeq; WP_003085566.1; NZ_QZGE01000007.1.
DR AlphaFoldDB; Q9XCX8; -.
DR SMR; Q9XCX8; -.
DR STRING; 287.DR97_1212; -.
DR PaxDb; Q9XCX8; -.
DR PRIDE; Q9XCX8; -.
DR EnsemblBacteria; AAG04160; AAG04160; PA0771.
DR GeneID; 879487; -.
DR KEGG; pae:PA0771; -.
DR PATRIC; fig|208964.12.peg.801; -.
DR PseudoCAP; PA0771; -.
DR HOGENOM; CLU_038009_1_2_6; -.
DR InParanoid; Q9XCX8; -.
DR OMA; WAEVDVI; -.
DR PhylomeDB; Q9XCX8; -.
DR BioCyc; PAER208964:G1FZ6-784-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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:0043024; F:ribosomal small subunit binding; IBA:GO_Central.
DR GO; GO:0019843; F:rRNA binding; IBA:GO_Central.
DR GO; GO:0070181; F:small ribosomal subunit rRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000028; P:ribosomal small subunit assembly; IBA:GO_Central.
DR CDD; cd04163; Era; 1.
DR Gene3D; 3.30.300.20; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00367; GTPase_Era; 1.
DR InterPro; IPR030388; G_ERA_dom.
DR InterPro; IPR006073; GTP-bd.
DR InterPro; IPR005662; GTP-bd_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 PANTHER; PTHR42698; PTHR42698; 1.
DR Pfam; PF07650; KH_2; 1.
DR Pfam; PF01926; MMR_HSR1; 1.
DR PRINTS; PR00326; GTP1OBG.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54814; SSF54814; 1.
DR TIGRFAMs; TIGR00436; era; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51713; G_ERA; 1.
DR PROSITE; PS50823; KH_TYPE_2; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Cytoplasm; GTP-binding; Membrane;
KW Nucleotide-binding; Reference proteome; Ribosome biogenesis; RNA-binding;
KW rRNA-binding.
FT CHAIN 1..305
FT /note="GTPase Era"
FT /id="PRO_0000180036"
FT DOMAIN 13..181
FT /note="Era-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT DOMAIN 204..288
FT /note="KH type-2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00367"
FT REGION 21..28
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT REGION 47..51
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT REGION 68..71
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT REGION 130..133
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT REGION 160..162
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT BINDING 21..28
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00367"
FT BINDING 68..72
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00367"
FT BINDING 130..133
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00367"
FT CONFLICT 162..164
FT /note="AQH -> GQD (in Ref. 1; AAD40230)"
FT /evidence="ECO:0000305"
FT CONFLICT 178
FT /note="R -> C (in Ref. 1; AAD40230)"
FT /evidence="ECO:0000305"
FT CONFLICT 184
FT /note="H -> Y (in Ref. 1; AAD40230)"
FT /evidence="ECO:0000305"
FT CONFLICT 193
FT /note="D -> E (in Ref. 1; AAD40230)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 305 AA; 34550 MW; B1900660CD41D32A CRC64;
MTDMHDDIPA GSRCGYVAIV GRPNVGKSTL LNHILGQKLA ITSRKPQTTR HNMLGIKTEG
EVQAVYVDTP GLHKSGEKAL NRYMNRTASA ALKDVDVVIF VVDRTRWTEE DQMVLERVQY
VSCPVLIAVN KTDRIEEKAD LLPHLEWLTQ QLPKAEVVPI SAQHGTNLDV LEKLVAERLP
ESEHFFPEDQ ITDRSSRFLA AELVREKIMR QLGAELPYQI TVEIEEFKQE GRILHIHALI
LVEREGQKKI IIGDKGERIK SIGQNARKDM EVLFDSKVML NLWVKVKGGW SDDERALRSL
GYGDL
