ID A0AAE8NJA0_BURCE Unreviewed; 370 AA. AC A0AAE8NJA0; DT 29-MAY-2024, integrated into UniProtKB/TrEMBL. DT 29-MAY-2024, sequence version 1. DT 02-OCT-2024, entry version 3. 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=obg {ECO:0000256|HAMAP-Rule:MF_01454, GN ECO:0000313|EMBL:SQA54370.1}; GN Synonyms=obgE {ECO:0000313|EMBL:MDN7914068.1}; GN ORFNames=E3D38_44935 {ECO:0000313|EMBL:TEU32962.1}, NCTC10661_05234 GN {ECO:0000313|EMBL:SQA54370.1}, QZM77_27860 GN {ECO:0000313|EMBL:MDN7914068.1}; OS Burkholderia cepacia (Pseudomonas cepacia). OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex. OX NCBI_TaxID=292 {ECO:0000313|EMBL:SQA54370.1, ECO:0000313|Proteomes:UP000250416}; RN [1] {ECO:0000313|EMBL:SQA54370.1, ECO:0000313|Proteomes:UP000250416} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NCTC10661 {ECO:0000313|EMBL:SQA54370.1, RC ECO:0000313|Proteomes:UP000250416}; RG Pathogen Informatics; RA Doyle S.; RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:TEU32962.1, ECO:0000313|Proteomes:UP000298185} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B19 {ECO:0000313|EMBL:TEU32962.1}, and b19 RC {ECO:0000313|Proteomes:UP000298185}; RA Farzana R., Walsh T.R.; RT "Burkholderia cepacia outbreak."; RL Submitted (MAR-2019) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:MDN7914068.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=AU42024 {ECO:0000313|EMBL:MDN7914068.1}; RA Lipuma J., Spilker T., Caverly L.; RT "A collection of bacterial strains from the Burkholderia cepacia Research RT Laboratory and Repository."; RL Submitted (JUL-2023) 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: 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:SQA54370.1}. 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; JAUJSP010000020; MDN7914068.1; -; Genomic_DNA. DR EMBL; UARD01000034; SQA54370.1; -; Genomic_DNA. DR EMBL; SNSP01000148; TEU32962.1; -; Genomic_DNA. DR RefSeq; WP_042975354.1; NZ_UARD01000034.1. DR Proteomes; UP000250416; Unassembled WGS sequence. DR Proteomes; UP000298185; Unassembled WGS sequence. DR Proteomes; UP001171618; Unassembled WGS sequence. 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; IPR006074; GTP1-OBG_CS. 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; PS00905; GTP1_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}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, 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}. 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 REGION 128..147 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 166..173 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01454" 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 370 AA; 39783 MW; F1B8E8A9775DFA69 CRC64; MKFIDEARIE VIAGDGGDGS ASMRREKFVP FGGPDGGDGG RGGSVYAIAD RNINTLIDYR YAKKHLARNG ENGRGSDCYG KGGDDVTLRM PVGTIISDMD TGELIADLTE HDQQVMLAQG GAGGLGNLHF KSSTNRAPRQ KTDGKPGERR MLKLELKVLA DVGLLGMPNA GKSTFISSVS NARPKIADYP FTTLAPNLGV VRVGPSKSFV IADIPGLIEG AAEGAGLGHQ FLRHLQRTGV LLHLVDLAPF DESVDPVAEA TAIVGELRKY DEALYEKPRW LVLNKLDMVP EDERKARVAD FLERFEWDGP VFEISALTGQ GCEALCYAIY DYLSEHSDAH RAAEAEDLAA DVRFRDAPPA KGEAAPGDDA //