OBG_THEM4
ID OBG_THEM4 Reviewed; 434 AA.
AC A6LJZ0;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 102.
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=Tmel_0372;
OS Thermosipho melanesiensis (strain DSM 12029 / CIP 104789 / BI429).
OC Bacteria; Thermotogae; Thermotogales; Fervidobacteriaceae; Thermosipho.
OX NCBI_TaxID=391009;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12029 / CIP 104789 / BI429;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Detter J.C.,
RA Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Nelson K., Gogarten J.P., Noll K., Richardson P.;
RT "Complete sequence of Thermosipho melanesiensis BI429.";
RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000716; ABR30241.1; -; Genomic_DNA.
DR RefSeq; WP_012056602.1; NC_009616.1.
DR AlphaFoldDB; A6LJZ0; -.
DR SMR; A6LJZ0; -.
DR STRING; 391009.Tmel_0372; -.
DR PRIDE; A6LJZ0; -.
DR EnsemblBacteria; ABR30241; ABR30241; Tmel_0372.
DR KEGG; tme:Tmel_0372; -.
DR eggNOG; COG0536; Bacteria.
DR HOGENOM; CLU_011747_2_1_0; -.
DR OMA; VVFDWEP; -.
DR Proteomes; UP000001110; 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.
FT CHAIN 1..434
FT /note="GTPase Obg"
FT /id="PRO_0000386353"
FT DOMAIN 4..162
FT /note="Obg"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01231"
FT DOMAIN 163..333
FT /note="OBG-type G"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT DOMAIN 355..434
FT /note="OCT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01229"
FT BINDING 169..176
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT BINDING 176
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT BINDING 194..198
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT BINDING 196
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT BINDING 215..218
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT BINDING 285..288
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT BINDING 314..316
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
SQ SEQUENCE 434 AA; 48049 MW; 430D7329D9D5D890 CRC64;
MERSDFVDRV IIYVKGGKGG DGSASFRHEK YVPKGGPDGG DGGNGGYVFL RANSNLSTLL
TVAEKKKYIA ENGENGKGKK MHGRNGKDII IDVPLGTVVK DFETGEIIAD LDKNGMVVCV
ARGGKGGRGN VHFKSSTMRT PKISERGAEG EERKLILELK LLADVGLVGY PNVGKSSFIS
KISNAKPKIA NYPFTTLIPN LGVVQVDDLQ FVVADIPGLI KGASKGVGLG NVFLRHVERC
SVIVHIVDIS GFEGRDPVND YFDIRRELEY FSEDLAKKEE IIVANKIDLL SKEELEERIQ
KLKNATGKET FPTSVLTGKG IREVIYKMAE MVKESKKLNV EGEIVNERVK RPKPIWKELP
EKFVIEIKRD GDDFVVAGPY VEEWAKRLNL TQRDGYNKFM ELLEKNGLDN KLREAGAKDG
DTVWIAGRAF EFKE
