ID A0A1B1YV32_9GAMM Unreviewed; 342 AA.
AC A0A1B1YV32;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=GTPase Obg {ECO:0000256|HAMAP-Rule:MF_01454};
DE EC=3.6.5.- {ECO:0000256|HAMAP-Rule:MF_01454};
DE AltName: Full=GTP-binding protein Obg {ECO:0000256|HAMAP-Rule:MF_01454};
GN Name=obgE {ECO:0000313|EMBL:ANX04622.1};
GN Synonyms=obg {ECO:0000256|HAMAP-Rule:MF_01454};
GN ORFNames=PG2T_10895 {ECO:0000313|EMBL:ANX04622.1};
OS Immundisolibacter cernigliae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Immundisolibacterales;
OC Immundisolibacteraceae; Immundisolibacter.
OX NCBI_TaxID=1810504 {ECO:0000313|EMBL:ANX04622.1, ECO:0000313|Proteomes:UP000092952};
RN [1] {ECO:0000313|Proteomes:UP000092952}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TR3.2 {ECO:0000313|Proteomes:UP000092952};
RA Singleton D.R., Dickey A.N., Scholl E.H., Wright F.A., Aitken M.D.;
RT "Complete genome sequence of Solimmundus cernigliae, representing a novel
RT lineage of polycyclic aromatic hydrocarbon degraders within the
RT Gammaproteobacteria.";
RL Submitted (MAR-2016) 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:0000256|HAMAP-Rule:MF_01454}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01454};
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_01454}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01454}.
CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase
CC superfamily. OBG GTPase family. {ECO:0000256|ARBA:ARBA00007699,
CC ECO:0000256|HAMAP-Rule:MF_01454}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01454}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP014671; ANX04622.1; -; Genomic_DNA.
DR RefSeq; WP_068805200.1; NZ_CP014671.1.
DR AlphaFoldDB; A0A1B1YV32; -.
DR STRING; 1810504.PG2T_10895; -.
DR KEGG; gbi:PG2T_10895; -.
DR InParanoid; A0A1B1YV32; -.
DR OrthoDB; 9807318at2; -.
DR Proteomes; UP000092952; 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; GTP1/OBG domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; IPR006169; GTP1_OBG_dom.
DR InterPro; IPR036726; GTP1_OBG_dom_sf.
DR InterPro; IPR045086; OBG_GTPase.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR02729; Obg_CgtA; 1.
DR PANTHER; PTHR11702; DEVELOPMENTALLY REGULATED GTP-BINDING PROTEIN-RELATED; 1.
DR PANTHER; PTHR11702:SF31; MITOCHONDRIAL RIBOSOME-ASSOCIATED GTPASE 2; 1.
DR Pfam; PF01018; GTP1_OBG; 1.
DR Pfam; PF01926; MMR_HSR1; 1.
DR PIRSF; PIRSF002401; GTP_bd_Obg/CgtA; 1.
DR PRINTS; PR00326; GTP1OBG.
DR SUPFAM; SSF82051; Obg GTP-binding protein N-terminal domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51710; G_OBG; 1.
DR PROSITE; PS51883; OBG; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01454};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW Rule:MF_01454}; Hydrolase {ECO:0000256|HAMAP-Rule:MF_01454};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01454};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01454};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01454}; Reference proteome {ECO:0000313|Proteomes:UP000092952}.
FT DOMAIN 1..159
FT /note="Obg"
FT /evidence="ECO:0000259|PROSITE:PS51883"
FT DOMAIN 160..334
FT /note="OBG-type G"
FT /evidence="ECO:0000259|PROSITE:PS51710"
FT BINDING 173
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01454"
FT BINDING 191..195
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01454"
FT BINDING 193
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01454"
FT BINDING 213..216
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01454"
FT BINDING 284..287
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01454"
FT BINDING 315..317
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01454"
SQ SEQUENCE 342 AA; 36122 MW; F70F6791EAB270B0 CRC64;
MRFVDEATIT VAGGKGGNGC MAFRREKYIP FGGPDGGDGG DGGSVYLVAD EGLSTLSDFR
YQREFRAESG HAGAGSCRTG RAGADREVTV PLGTEVRDAD TGEIIGDLTH HGQRLKVAAG
GFHGLGNTRY KSSINRAPRQ TSPGKPGELR RLALELRLLA DVGLLGAPNA GKSTLLAAVS
QARPKIADYP FTTLNPELGV VEVDRFRRFV MADIPGLIEG SAAGAGLGTQ FLRHLGRTRL
LLHVLDLAPA DPASIPAQEA RKIVAELEAF SPELAALPRW LVLNKADLLL PDEAAARGAQ
IADELGWSGP LFLISAATGS GCQALCEAIM RHLEQQALQA RE
//
