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Database: UniProt
Entry: E7RVC2_9BURK
LinkDB: E7RVC2_9BURK
Original site: E7RVC2_9BURK 
ID   E7RVC2_9BURK            Unreviewed;       309 AA.
AC   E7RVC2;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 72.
DE   RecName: Full=GTPase Era {ECO:0000256|ARBA:ARBA00020484, ECO:0000256|HAMAP-Rule:MF_00367};
GN   Name=era {ECO:0000256|HAMAP-Rule:MF_00367,
GN   ECO:0000313|EMBL:EFV95726.1};
GN   ORFNames=HMPREF0551_0634 {ECO:0000313|EMBL:EFV95726.1};
OS   Lautropia mirabilis ATCC 51599.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Lautropia.
OX   NCBI_TaxID=887898 {ECO:0000313|EMBL:EFV95726.1, ECO:0000313|Proteomes:UP000011021};
RN   [1] {ECO:0000313|EMBL:EFV95726.1, ECO:0000313|Proteomes:UP000011021}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51599 {ECO:0000313|EMBL:EFV95726.1,
RC   ECO:0000313|Proteomes:UP000011021};
RA   Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA   Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA   Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA   Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA   Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA   Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA   Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA   Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA   Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA   Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA   Petrosino J., Highlander S., Gibbs R.;
RL   Submitted (DEC-2010) 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:0000256|HAMAP-Rule:MF_00367}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00367}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00367}. Cell
CC       membrane {ECO:0000256|HAMAP-Rule:MF_00367}; Peripheral membrane protein
CC       {ECO:0000256|HAMAP-Rule:MF_00367}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC       GTPase superfamily. Era GTPase family. {ECO:0000256|ARBA:ARBA00007921,
CC       ECO:0000256|HAMAP-Rule:MF_00367, ECO:0000256|PROSITE-ProRule:PRU01050,
CC       ECO:0000256|RuleBase:RU003761}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00367}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EFV95726.1}.
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DR   EMBL; AEQP01000002; EFV95726.1; -; Genomic_DNA.
DR   RefSeq; WP_005672717.1; NZ_GL636062.1.
DR   AlphaFoldDB; E7RVC2; -.
DR   STRING; 887898.HMPREF0551_0634; -.
DR   eggNOG; COG1159; Bacteria.
DR   HOGENOM; CLU_038009_1_2_4; -.
DR   Proteomes; UP000011021; Unassembled WGS sequence.
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   CDD; cd22534; KH-II_Era; 1.
DR   Gene3D; 3.30.300.20; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   HAMAP; MF_00367; GTPase_Era; 1.
DR   InterPro; IPR030388; G_ERA_dom.
DR   InterPro; IPR006073; GTP-bd.
DR   InterPro; IPR005662; GTPase_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   NCBIfam; TIGR00436; era; 1.
DR   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR42698; GTPASE ERA; 1.
DR   PANTHER; PTHR42698:SF2; GTPASE ERA-LIKE, CHLOROPLASTIC; 1.
DR   Pfam; PF07650; KH_2; 1.
DR   Pfam; PF01926; MMR_HSR1; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF54814; Prokaryotic type KH domain (KH-domain type II); 1.
DR   PROSITE; PS51713; G_ERA; 1.
DR   PROSITE; PS50823; KH_TYPE_2; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_00367};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00367};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW   Rule:MF_00367}; Membrane {ECO:0000256|HAMAP-Rule:MF_00367};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00367}; Reference proteome {ECO:0000313|Proteomes:UP000011021};
KW   Ribosome biogenesis {ECO:0000256|HAMAP-Rule:MF_00367};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW   Rule:MF_00367}; rRNA-binding {ECO:0000256|HAMAP-Rule:MF_00367}.
FT   DOMAIN          19..187
FT                   /note="Era-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51713"
FT   DOMAIN          210..294
FT                   /note="KH type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS50823"
FT   REGION          27..34
FT                   /note="G1"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01050"
FT   REGION          53..57
FT                   /note="G2"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01050"
FT   REGION          74..77
FT                   /note="G3"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01050"
FT   REGION          135..138
FT                   /note="G4"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01050"
FT   REGION          166..168
FT                   /note="G5"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01050"
FT   BINDING         27..34
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00367"
FT   BINDING         135..138
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00367"
SQ   SEQUENCE   309 AA;  34404 MW;  65D5AE16794712E2 CRC64;
     MPHDPSASPS PVAEGTPFRC GYVALVGRPN TGKSTLLNQL LGQMLSITAD RAQTTRHRIQ
     GVLSRPHAQL ILVDSPGYQT QRINPLNKIL NRTAQSVGQQ ADVVVLVTEA GRWRRQDDEI
     LGWLKGDAPV IVALNKIDQL RNVNEVLPLI AQVHEAHPGL AAIVPICARN GQGIEALLDA
     IESNLPEGEA IYGEDELTDR PERFFAAEIV REKLFRLLGE ELPYESTVVI DRFEEEGNLR
     RIAATIIVER RAHKPIVLGH GGERIKRIAS EARQDMERMF DGKVFLTLWV QVRSGWAKDA
     AHLRSYGYE
//
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