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Database: UniProt
Entry: A0A2S3QJA7_9FIRM
LinkDB: A0A2S3QJA7_9FIRM
Original site: A0A2S3QJA7_9FIRM 
ID   A0A2S3QJA7_9FIRM        Unreviewed;       422 AA.
AC   A0A2S3QJA7;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 23.
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   ORFNames=CO251_03045 {ECO:0000313|EMBL:POB11794.1};
OS   Sulfobacillus sp. hq2.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales;
OC   Clostridiales Family XVII. Incertae Sedis; Sulfobacillus.
OX   NCBI_TaxID=2039167 {ECO:0000313|EMBL:POB11794.1, ECO:0000313|Proteomes:UP000237334};
RN   [1] {ECO:0000313|EMBL:POB11794.1, ECO:0000313|Proteomes:UP000237334}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=hq2 {ECO:0000313|Proteomes:UP000237334};
RA   He Q., Li Y., Han Y., Zhao W., Huang Z.;
RT   "Draft genome sequence of Sulfobacillus sp. hq2.";
RL   Submitted (SEP-2017) 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:POB11794.1}.
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DR   EMBL; NWUL01000018; POB11794.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S3QJA7; -.
DR   OrthoDB; 9807318at2; -.
DR   Proteomes; UP000237334; 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   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:UP000237334}.
FT   DOMAIN          1..157
FT                   /note="Obg"
FT                   /evidence="ECO:0000259|PROSITE:PS51883"
FT   DOMAIN          158..326
FT                   /note="OBG-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51710"
FT   DOMAIN          335..416
FT                   /note="OCT"
FT                   /evidence="ECO:0000259|PROSITE:PS51881"
FT   BINDING         164..171
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01454"
FT   BINDING         171
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01454"
FT   BINDING         189..193
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01454"
FT   BINDING         191
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01454"
FT   BINDING         210..213
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01454"
FT   BINDING         280..283
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01454"
FT   BINDING         307..309
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01454"
SQ   SEQUENCE   422 AA;  46007 MW;  F18A1422B8FEEB55 CRC64;
     MFVDEVRIYV EAGSGGNGAV AFRREKFVPT GGPEGGDGGR GGDIIFEVDP GLNTLMDFRH
     QKHYRAQNGQ NGAAKNMYGR DAEDVIVRVP PGTLVKKETG ELIADLTEPG SRTVIARGGR
     GGKGNSHFAS SRHRVPRIAE KGQPGEAFWV TLELNLLADV GLVGFPNAGK STLISKISAS
     RPKIADYPFT TLVPNLGVVS DYGDPFVVAD VPGLIEGAHT GLGLGDTFLR HLNRTRVLVH
     LVDVSPQMDR NAANDYRIIA HELQAFSPEL AARPVIIAAN KMDMEGSEEG LRALQEAVSP
     HVVWPISALS GAGIDALMWE VRRVLDITPK PEVQTVEPAL KPVVHGFSLE FDDKEGVRVV
     GDIEERASMT LWGNPHAEEY FLEYLRRRGL EGMLRRAHVA DNTPVRIGEG TFYWREGELV
     LE
//
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