ID A0A0B2AJI6_9MICC Unreviewed; 528 AA.
AC A0A0B2AJI6;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 24-JAN-2024, entry version 44.
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:KHL01927.1};
GN Synonyms=obg {ECO:0000256|HAMAP-Rule:MF_01454};
GN ORFNames=LK10_14330 {ECO:0000313|EMBL:KHL01927.1};
OS Sinomonas humi.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Sinomonas.
OX NCBI_TaxID=1338436 {ECO:0000313|EMBL:KHL01927.1, ECO:0000313|Proteomes:UP000030982};
RN [1] {ECO:0000313|EMBL:KHL01927.1, ECO:0000313|Proteomes:UP000030982}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUSC 117 {ECO:0000313|EMBL:KHL01927.1,
RC ECO:0000313|Proteomes:UP000030982};
RA Lee L.-H.;
RT "Genome sequence of Sinomonas sp. MUSC 117.";
RL Submitted (SEP-2014) 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|ARBA:ARBA00001946,
CC 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:KHL01927.1}.
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DR EMBL; JTDL01000136; KHL01927.1; -; Genomic_DNA.
DR RefSeq; WP_043124951.1; NZ_JTDL01000136.1.
DR AlphaFoldDB; A0A0B2AJI6; -.
DR STRING; 1338436.LK10_14330; -.
DR OrthoDB; 9807318at2; -.
DR Proteomes; UP000030982; 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; 3.30.300.350; GTP-binding protein OBG, C-terminal domain; 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; 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 NCBIfam; TIGR02729; Obg_CgtA; 1.
DR NCBIfam; TIGR03595; Obg_CgtA_exten; 1.
DR PANTHER; PTHR11702; DEVELOPMENTALLY REGULATED GTP-BINDING PROTEIN-RELATED; 1.
DR PANTHER; PTHR11702:SF31; MITOCHONDRIAL RIBOSOME-ASSOCIATED GTPASE 2; 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; Obg GTP-binding protein C-terminal domain; 1.
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.
DR PROSITE; PS51881; OCT; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, 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:UP000030982}.
FT DOMAIN 2..159
FT /note="Obg"
FT /evidence="ECO:0000259|PROSITE:PS51883"
FT DOMAIN 160..343
FT /note="OBG-type G"
FT /evidence="ECO:0000259|PROSITE:PS51710"
FT DOMAIN 363..447
FT /note="OCT"
FT /evidence="ECO:0000259|PROSITE:PS51881"
FT REGION 459..528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 470..518
FT /note="Basic and acidic residues"
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 212..215
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01454"
FT BINDING 295..298
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01454"
FT BINDING 324..326
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01454"
SQ SEQUENCE 528 AA; 56653 MW; 0FC7541450804692 CRC64;
MASFVDRVVL HVSGGHGGHG CVSVKREKFK PLGGPDGGNG GNGGDVVLRV SSQTTTLLDY
HHSPHRHAEN GGPGMGDWRV GHRGETLVLP VPDGTVVKSR DGAVLADLVG EGAEFIAAAG
GQGGLGNAAL ATAKRKAPGF ALLGIAGEER DIVLELKSIA DVALVGFPSA GKSSLIAAMS
AARPKIADYP FTTLVPNLGV VQAGDIRFTI ADVPGLIEGA SEGRGLGHDF LRHVERCAAI
VHVLDCGTLE SDRNPLDDLD VIEGELAKYD VDMSFAGPDG EVVPLNERPR LVALNKVDLP
DGKAMADMVR AELEGRGYRV FEVSATSHEG LRALGFAMAE IVQHARDEVK AAPPKVSPAV
LRPRAVNEKS FTIRKEERNL EPLFRIIGEK PERWVKQTDF TNDEAVGYLS DRLNRLGVED
ELFKVGAHAG DTVVIGEDDA VVFDWEPTMS AGAELLAGPR GSDVRLSDWS RPTRAQKRDE
FEDRKAARAA AREELEAERR AGIWTESSRR KEWAPDLKSE ESDDDGEF
//
