ERA_BRADU
ID ERA_BRADU Reviewed; 308 AA.
AC O69162;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 28-FEB-2003, sequence version 3.
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=bll5060;
OS Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS NBRC 14792 / USDA 110).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Bradyrhizobium.
OX NCBI_TaxID=224911;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=USDA 110spc4;
RA Mueller P., Stingel D.;
RT "Extended DNA sequencing in the upstream region of sipF in Bradyrhizobium
RT japonicum.";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT Bradyrhizobium japonicum USDA110.";
RL DNA Res. 9:189-197(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-208.
RC STRAIN=USDA 110spc4;
RX PubMed=9870699; DOI=10.1007/pl00008631;
RA Bairl A., Mueller P.;
RT "A second gene for type I signal peptidase in Bradyrhizobium japonicum,
RT sipF, is located near genes involved in RNA processing and cell division.";
RL Mol. Gen. Genet. 260:346-356(1998).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF065159; AAD02940.2; -; Genomic_DNA.
DR EMBL; BA000040; BAC50325.1; -; Genomic_DNA.
DR RefSeq; NP_771700.1; NC_004463.1.
DR RefSeq; WP_011087821.1; NZ_CP011360.1.
DR AlphaFoldDB; O69162; -.
DR SMR; O69162; -.
DR STRING; 224911.27353325; -.
DR EnsemblBacteria; BAC50325; BAC50325; BAC50325.
DR GeneID; 64024824; -.
DR KEGG; bja:bll5060; -.
DR PATRIC; fig|224911.44.peg.4928; -.
DR eggNOG; COG1159; Bacteria.
DR HOGENOM; CLU_038009_1_1_5; -.
DR InParanoid; O69162; -.
DR OMA; WAEVDVI; -.
DR PhylomeDB; O69162; -.
DR Proteomes; UP000002526; 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 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..308
FT /note="GTPase Era"
FT /id="PRO_0000179999"
FT DOMAIN 14..181
FT /note="Era-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT DOMAIN 212..289
FT /note="KH type-2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00367"
FT REGION 22..29
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT REGION 48..52
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT REGION 69..72
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT REGION 131..134
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 22..29
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00367"
FT BINDING 69..73
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00367"
FT BINDING 131..134
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00367"
FT CONFLICT 225
FT /note="D -> AR (in Ref. 1; AAD02940)"
FT /evidence="ECO:0000305"
FT CONFLICT 229
FT /note="E -> A (in Ref. 1; AAD02940)"
FT /evidence="ECO:0000305"
FT CONFLICT 232
FT /note="D -> A (in Ref. 1; AAD02940)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 308 AA; 33969 MW; 7F0F8638BFE6A572 CRC64;
MTVEASGEAP AATRCGFVAL IGAPNVGKST LVNALVGAKV TIVSRKVQTT RALIRGIVIE
NNAQIILVDT PGIFSPKRRL DRAMVSTAWS GAHDADLVCV LLDAKTGIDE EAEAILAKAA
SVNHDKILVI NKVDLVQREK LLALAQAANE RMPFAKTFMI AAISGDGVDD LRSTLAEMVP
PGPFLYPEDQ MSDAPMRHLA AEITREKIYR KLHQELPYQS TVETDKWEER KDKSVRIEQT
IFVERESQRK IVLGKGGATI KSIGADSRKE ISEILGVPVH LFLFVKVREN WGDDPDRYRE
MGLEFPKE
