ERA_STRSV
ID ERA_STRSV Reviewed; 299 AA.
AC A3CP94;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=GTPase Era {ECO:0000255|HAMAP-Rule:MF_00367};
GN Name=era {ECO:0000255|HAMAP-Rule:MF_00367}; OrderedLocusNames=SSA_1611;
OS Streptococcus sanguinis (strain SK36).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=388919;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK36;
RX PubMed=17277061; DOI=10.1128/jb.01808-06;
RA Xu P., Alves J.M., Kitten T., Brown A., Chen Z., Ozaki L.S., Manque P.,
RA Ge X., Serrano M.G., Puiu D., Hendricks S., Wang Y., Chaplin M.D., Akan D.,
RA Paik S., Peterson D.L., Macrina F.L., Buck G.A.;
RT "Genome of the opportunistic pathogen Streptococcus sanguinis.";
RL J. Bacteriol. 189:3166-3175(2007).
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 membrane {ECO:0000255|HAMAP-
CC Rule:MF_00367}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC 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; CP000387; ABN44999.1; -; Genomic_DNA.
DR RefSeq; WP_002894867.1; NC_009009.1.
DR RefSeq; YP_001035549.1; NC_009009.1.
DR AlphaFoldDB; A3CP94; -.
DR SMR; A3CP94; -.
DR STRING; 388919.SSA_1611; -.
DR EnsemblBacteria; ABN44999; ABN44999; SSA_1611.
DR KEGG; ssa:SSA_1611; -.
DR PATRIC; fig|388919.9.peg.1529; -.
DR eggNOG; COG1159; Bacteria.
DR HOGENOM; CLU_038009_1_0_9; -.
DR OMA; WAEVDVI; -.
DR OrthoDB; 984717at2; -.
DR Proteomes; UP000002148; Chromosome.
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 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 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 membrane; Cytoplasm; GTP-binding; Membrane; Nucleotide-binding;
KW Reference proteome; Ribosome biogenesis; RNA-binding; rRNA-binding.
FT CHAIN 1..299
FT /note="GTPase Era"
FT /id="PRO_1000079758"
FT DOMAIN 4..171
FT /note="Era-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT DOMAIN 202..280
FT /note="KH type-2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00367"
FT REGION 12..19
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT REGION 38..42
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT REGION 59..62
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT REGION 121..124
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT REGION 150..152
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT BINDING 12..19
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00367"
FT BINDING 59..63
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00367"
FT BINDING 121..124
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00367"
SQ SEQUENCE 299 AA; 34065 MW; 79E63980742B6048 CRC64;
MTFKSGFVAI LGRPNVGKST FLNHVMGQKI AIMSDKAQTT RNKIMGIYTT DKEQIVFIDT
PGIHKPKTAL GDFMVEAAYS TLREVDTVLF MVPADEPRGK GDDMIIERLK AAKVPVILVV
NKIDKVHPDQ LLAQIDDFRQ QMDFKEIVPI SALQGNNVSH LIDILSENLE EGFQYFPEDQ
ITDHPERFLV SEMIREKVLM LTREEIPHSV AVVVDSMKRD EETDKVHIRA TIMVERDSQK
GIIIGKGGSM LKKIGSMARR DIELMLGDKV FLETWVKVKK NWRDKKLDLA DFGYNKKEY