OBG_ELUMP
ID OBG_ELUMP Reviewed; 458 AA.
AC B2KAW2;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=GTPase Obg {ECO:0000255|HAMAP-Rule:MF_01454};
DE EC=3.6.5.- {ECO:0000255|HAMAP-Rule:MF_01454};
DE AltName: Full=GTP-binding protein Obg {ECO:0000255|HAMAP-Rule:MF_01454};
GN Name=obg {ECO:0000255|HAMAP-Rule:MF_01454}; OrderedLocusNames=Emin_0092;
OS Elusimicrobium minutum (strain Pei191).
OC Bacteria; Elusimicrobia; Elusimicrobia; Elusimicrobiales;
OC Elusimicrobiaceae; Elusimicrobium.
OX NCBI_TaxID=445932;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pei191;
RX PubMed=19270133; DOI=10.1128/aem.02698-08;
RA Herlemann D.P.R., Geissinger O., Ikeda-Ohtsubo W., Kunin V., Sun H.,
RA Lapidus A., Hugenholtz P., Brune A.;
RT "Genomic analysis of 'Elusimicrobium minutum,' the first cultivated
RT representative of the phylum 'Elusimicrobia' (formerly termite group 1).";
RL Appl. Environ. Microbiol. 75:2841-2849(2009).
CC -!- FUNCTION: An essential GTPase which binds GTP, GDP and possibly
CC (p)ppGpp with moderate affinity, with high nucleotide exchange rates
CC and a fairly low GTP hydrolysis rate. Plays a role in control of the
CC cell cycle, stress response, ribosome biogenesis and in those bacteria
CC that undergo differentiation, in morphogenesis control.
CC {ECO:0000255|HAMAP-Rule:MF_01454}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01454};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01454}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01454}.
CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase
CC superfamily. OBG GTPase family. {ECO:0000255|HAMAP-Rule:MF_01454}.
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DR EMBL; CP001055; ACC97658.1; -; Genomic_DNA.
DR AlphaFoldDB; B2KAW2; -.
DR SMR; B2KAW2; -.
DR STRING; 445932.Emin_0092; -.
DR EnsemblBacteria; ACC97658; ACC97658; Emin_0092.
DR KEGG; emi:Emin_0092; -.
DR HOGENOM; CLU_011747_2_1_0; -.
DR OMA; VVFDWEP; -.
DR Proteomes; UP000001029; Chromosome.
DR GO; GO:0005737; C:cytoplasm; 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:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-UniRule.
DR CDD; cd01898; Obg; 1.
DR Gene3D; 2.70.210.12; -; 1.
DR Gene3D; 3.30.300.350; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_01454; GTPase_Obg; 1.
DR InterPro; IPR031167; G_OBG.
DR InterPro; IPR006073; GTP-bd.
DR InterPro; IPR014100; GTP-bd_Obg/CgtA.
DR InterPro; IPR036346; GTP-bd_prot_GTP1/OBG_C_sf.
DR InterPro; IPR006074; GTP1-OBG_CS.
DR InterPro; IPR006169; GTP1_OBG_dom.
DR InterPro; IPR036726; GTP1_OBG_dom_sf.
DR InterPro; IPR045086; OBG_GTPase.
DR InterPro; IPR015349; OCT_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR PANTHER; PTHR11702; PTHR11702; 1.
DR Pfam; PF09269; DUF1967; 1.
DR Pfam; PF01018; GTP1_OBG; 1.
DR Pfam; PF01926; MMR_HSR1; 1.
DR PRINTS; PR00326; GTP1OBG.
DR SUPFAM; SSF102741; SSF102741; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF82051; SSF82051; 1.
DR TIGRFAMs; TIGR02729; Obg_CgtA; 1.
DR TIGRFAMs; TIGR03595; Obg_CgtA_exten; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51710; G_OBG; 1.
DR PROSITE; PS00905; GTP1_OBG; 1.
DR PROSITE; PS51883; OBG; 1.
DR PROSITE; PS51881; OCT; 1.
PE 3: Inferred from homology;
KW Cytoplasm; GTP-binding; Hydrolase; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..458
FT /note="GTPase Obg"
FT /id="PRO_0000385903"
FT DOMAIN 1..157
FT /note="Obg"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01231"
FT DOMAIN 158..326
FT /note="OBG-type G"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT DOMAIN 341..419
FT /note="OCT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01229"
FT REGION 420..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 164..171
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT BINDING 171
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT BINDING 189..193
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT BINDING 191
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT BINDING 210..213
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT BINDING 280..283
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT BINDING 307..309
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
SQ SEQUENCE 458 AA; 50527 MW; AB851D10C1453D10 CRC64;
MSFLDRVKIY VKAGKGGDGC LSFRREKFIE FGGPNGGNGG KGGDVYIKTE RNLTTLLELA
YNPHIEAKNG EKGGTYNKTG VGADDLTIYV PCGTIVKKDG EIIADLTEEG QSVLVAKGGR
GGRGNQSFKT HSNTAPRISE IGQPGEEITL YLELKVLADL GLVGFPNAGK STFLSRVSAA
RPKIADYPFT TLNPNLGIAM HKKVSFVIAD IPGIIEGASE GKGLGHQFLK HIERTRVLLH
LVDPMGFKDI DAVESVKVIE KELKTFDREL AKKPRIIALN KADLPEAKEV YNKIVKKYKK
HKVFLISAAT GEGVDKVLNE IVKVISATPV PNVAISKSTV AVHGVEPLFK IVPLEDGRVQ
VFGRKIEDMV NMTHFNQLQG VERLRNIFKK IGLEKALIKK GVMPGDIIVV GQKEFEWSGT
ELDSERAEQP DFEGYKRRTT QAERLEKRRQ RRLKKEEK
