ERA_MYCSJ
ID ERA_MYCSJ Reviewed; 299 AA.
AC A3Q264;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=GTPase Era {ECO:0000255|HAMAP-Rule:MF_00367};
GN Name=era {ECO:0000255|HAMAP-Rule:MF_00367}; OrderedLocusNames=Mjls_3463;
OS Mycobacterium sp. (strain JLS).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; unclassified Mycobacterium.
OX NCBI_TaxID=164757;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JLS;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Miller C.D., Anderson A.J.,
RA Sims R.C., Richardson P.;
RT "Complete sequence of Mycobacterium sp. JLS.";
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000580; ABN99241.1; -; Genomic_DNA.
DR AlphaFoldDB; A3Q264; -.
DR SMR; A3Q264; -.
DR STRING; 164757.Mjls_3463; -.
DR KEGG; mjl:Mjls_3463; -.
DR HOGENOM; CLU_038009_0_2_11; -.
DR OMA; WAEVDVI; -.
DR BioCyc; MSP164757:G1G8C-3493-MON; -.
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 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 membrane; Cytoplasm; GTP-binding; Membrane; Nucleotide-binding;
KW Ribosome biogenesis; RNA-binding; rRNA-binding.
FT CHAIN 1..299
FT /note="GTPase Era"
FT /id="PRO_1000079712"
FT DOMAIN 5..175
FT /note="Era-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT DOMAIN 206..285
FT /note="KH type-2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00367"
FT REGION 13..20
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT REGION 39..43
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT REGION 60..63
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 13..20
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00367"
FT BINDING 60..64
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 299 AA; 32848 MW; 4CFBF02EA8D51FA3 CRC64;
MSEFRSGFVC FVGRPNTGKS TLTNALVGTK VAITSNRPQT TRHTIRGIVH RDEFQIILVD
TPGLHRPRTL LGQRLNDLVK TTYSEVDVIG LCIPADEAIG PGDRWIHEQI RAVAPRTTLV
VIVTKIDKVP KDRVAAQLMA VSELIGPDAE IVPVSATTGE QLDVLTDVLA GKLPPGPAFY
PDGELTDEPE ETLMAELIRE AALEGVRDEL PHSLAVVIDE VSPREDRDDL IDVHAILYVE
RDSQKGIVIG KGGARLREVG TAARLQIEKL LGTKVYLDLR VKIAKNWQRD PKQLGRLGF