ERA_SHIF8
ID ERA_SHIF8 Reviewed; 301 AA.
AC Q0T1T9;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=GTPase Era {ECO:0000255|HAMAP-Rule:MF_00367};
GN Name=era {ECO:0000255|HAMAP-Rule:MF_00367}; OrderedLocusNames=SFV_2629;
OS Shigella flexneri serotype 5b (strain 8401).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=373384;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=8401;
RX PubMed=16822325; DOI=10.1186/1471-2164-7-173;
RA Nie H., Yang F., Zhang X., Yang J., Chen L., Wang J., Xiong Z., Peng J.,
RA Sun L., Dong J., Xue Y., Xu X., Chen S., Yao Z., Shen Y., Jin Q.;
RT "Complete genome sequence of Shigella flexneri 5b and comparison with
RT Shigella flexneri 2a.";
RL BMC Genomics 7:173-173(2006).
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; CP000266; ABF04726.1; -; Genomic_DNA.
DR RefSeq; WP_000020745.1; NC_008258.1.
DR AlphaFoldDB; Q0T1T9; -.
DR SMR; Q0T1T9; -.
DR EnsemblBacteria; ABF04726; ABF04726; SFV_2629.
DR KEGG; sfv:SFV_2629; -.
DR HOGENOM; CLU_038009_1_2_6; -.
DR OMA; WAEVDVI; -.
DR BioCyc; SFLE373384:SFV_RS14620-MON; -.
DR Proteomes; UP000000659; 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 inner membrane; Cell membrane; Cytoplasm; GTP-binding; Membrane;
KW Nucleotide-binding; Ribosome biogenesis; RNA-binding; rRNA-binding.
FT CHAIN 1..301
FT /note="GTPase Era"
FT /id="PRO_1000079736"
FT DOMAIN 7..175
FT /note="Era-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT DOMAIN 206..283
FT /note="KH type-2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00367"
FT REGION 15..22
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT REGION 41..45
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT REGION 62..65
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT REGION 124..127
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT REGION 154..156
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT BINDING 15..22
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00367"
FT BINDING 62..66
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00367"
FT BINDING 124..127
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00367"
SQ SEQUENCE 301 AA; 33757 MW; F3FEC336A0B75355 CRC64;
MSIDKSYCGF IAIVGRPNVG KSTLLNKLLG QKISITSRKA QTTRHRIVGI HTEGAYQAIY
VDTPGLHMEE KRAINRLMNK AASSSIGDVE LVIFVVEGTR WTPDDEMVLN KLREGKAPVI
LAVNKVDNVQ EKADLLPHLQ FLASQMNFLD IVPISAETGL NVDTIAAIVR KHLPEATHHF
PEDYITDCSQ RFMASEIIRE KLMRFLGAEL PYSVTVEIER FVSNERGGYD INGLILVERE
GQKKMVIGNK GAKIKTIGIE ARKDMQEMFE APVHLELWVK VKSGWADDER ALRSLGYVDD
L