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Entry: E3G7V7_ENTLS
LinkDB: E3G7V7_ENTLS
Original site: E3G7V7_ENTLS 
ID   E3G7V7_ENTLS            Unreviewed;       301 AA.
AC   E3G7V7;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 87.
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   OrderedLocusNames=Entcl_1181 {ECO:0000313|EMBL:ADO47448.1};
OS   Enterobacter lignolyticus (strain SCF1).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Pluralibacter.
OX   NCBI_TaxID=701347 {ECO:0000313|EMBL:ADO47448.1, ECO:0000313|Proteomes:UP000006872};
RN   [1] {ECO:0000313|Proteomes:UP000006872}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCF1 {ECO:0000313|Proteomes:UP000006872};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N.,
RA   Mikhailova N., DeAngelis K., Arkin A.P., Chivian D., Edwards B., Woo H.,
RA   Hazen T.C., Woyke T.;
RT   "Complete sequence of Enterobacter cloacae SCF1.";
RL   Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADO47448.1, ECO:0000313|Proteomes:UP000006872}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCF1 {ECO:0000313|EMBL:ADO47448.1,
RC   ECO:0000313|Proteomes:UP000006872};
RX   PubMed=22180812; DOI=10.4056/sigs.2104875;
RA   Deangelis K.M., D'Haeseleer P., Chivian D., Fortney J.L., Khudyakov J.,
RA   Simmons B., Woo H., Arkin A.P., Davenport K.W., Goodwin L., Chen A.,
RA   Ivanova N., Kyrpides N.C., Mavromatis K., Woyke T., Hazen T.C.;
RT   "Complete genome sequence of "Enterobacter lignolyticus" SCF1.";
RL   Stand. Genomic Sci. 5:69-85(2011).
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       inner membrane {ECO:0000256|HAMAP-Rule:MF_00367}; Peripheral membrane
CC       protein {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}.
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DR   EMBL; CP002272; ADO47448.1; -; Genomic_DNA.
DR   RefSeq; WP_013365196.1; NC_014618.1.
DR   AlphaFoldDB; E3G7V7; -.
DR   STRING; 701347.Entcl_1181; -.
DR   KEGG; esc:Entcl_1181; -.
DR   eggNOG; COG1159; Bacteria.
DR   HOGENOM; CLU_038009_1_2_6; -.
DR   Proteomes; UP000006872; 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   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 inner membrane {ECO:0000256|HAMAP-Rule:MF_00367};
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:UP000006872};
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          7..175
FT                   /note="Era-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51713"
FT   DOMAIN          206..283
FT                   /note="KH type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS50823"
FT   REGION          15..22
FT                   /note="G1"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01050"
FT   REGION          41..45
FT                   /note="G2"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01050"
FT   REGION          62..65
FT                   /note="G3"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01050"
FT   REGION          124..127
FT                   /note="G4"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01050"
FT   REGION          154..156
FT                   /note="G5"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01050"
FT   BINDING         15..22
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00367"
FT   BINDING         62..66
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00367"
FT   BINDING         124..127
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00367"
SQ   SEQUENCE   301 AA;  33913 MW;  E24913A4ECF49536 CRC64;
     MSDNKTYCGF IAIVGRPNVG KSTLLNKLLG QKISITSRKA QTTRHRIVGI HTEGEYQAIY
     VDTPGLHMEE KRAINRLMNK AASSSIGDVE LVIFVVEGTR WTPDDEMVLN KLREGKAPVI
     LAVNKVDNVQ EKADLLPHLQ FLASQMNFLD IVPISAETGM NVDTIAGIVR KHLPEAIHHF
     PEDYITDRSQ RFMASEIIRE KLMRFLGAEL PYSVTVEIER FVTNERGGYD INGLILVERE
     GQKKMVIGNK GAKIKTIGIE ARKDMQEMFE APVHLELWVK VKSGWADDER ALRSLGYVDD
     L
//
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