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Database: UniProt
Entry: W1TLJ8_9ACTO
LinkDB: W1TLJ8_9ACTO
Original site: W1TLJ8_9ACTO 
ID   W1TLJ8_9ACTO            Unreviewed;       506 AA.
AC   W1TLJ8;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 49.
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=Q618_VCMC00001G0073 {ECO:0000313|EMBL:ETI82492.1};
OS   Varibaculum cambriense DORA_20.
OC   Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC   Varibaculum.
OX   NCBI_TaxID=1403948 {ECO:0000313|EMBL:ETI82492.1, ECO:0000313|Proteomes:UP000018843};
RN   [1] {ECO:0000313|EMBL:ETI82492.1, ECO:0000313|Proteomes:UP000018843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DORA_20 {ECO:0000313|Proteomes:UP000018843};
RA   Brown C.T., Sharon I., Thomas B.C., Castelle C.J., Morowitz M.J.,
RA   Banfield J.F.;
RT   "A Varibaculum cambriense genome reconstructed from a premature infant gut
RT   community with otherwise low bacterial novelty that shifts toward anaerobic
RT   metabolism during the third week of life.";
RL   Submitted (DEC-2013) 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:ETI82492.1}.
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DR   EMBL; AZMI01000001; ETI82492.1; -; Genomic_DNA.
DR   AlphaFoldDB; W1TLJ8; -.
DR   STRING; 184870.HMPREF1862_00025; -.
DR   PATRIC; fig|1403948.3.peg.1255; -.
DR   eggNOG; COG0536; Bacteria.
DR   Proteomes; UP000018843; 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:UP000018843}.
FT   DOMAIN          2..159
FT                   /note="Obg"
FT                   /evidence="ECO:0000259|PROSITE:PS51883"
FT   DOMAIN          160..340
FT                   /note="OBG-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51710"
FT   DOMAIN          359..444
FT                   /note="OCT"
FT                   /evidence="ECO:0000259|PROSITE:PS51881"
FT   REGION          481..506
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         212..215
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01454"
FT   BINDING         292..295
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01454"
FT   BINDING         321..323
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01454"
SQ   SEQUENCE   506 AA;  54164 MW;  412A4F9B8D7DFCE6 CRC64;
     MASFVDRVKI DVTAGNGGNG CVSIRREKYK PLGGPDGGDG GRGGSVFLEV DPQSHTLLDY
     HHLPHRKATN GTPGMGDNRE GANGEDLVLP VPPGTVVKSE DGQILADLQG AGSRLEVARG
     GTGGKGNAAL ATRKRKAPGF ALLGEEGESR VLILELKSVA DVGLVGFPSS GKSSLIGAIS
     EAKPKIADYP FTTLVPNLGV VQAGDERFTV ADVPGLIPGA SQGKGLGLDF LRHIERCAVI
     AHVVDCANME SERNPIDDIE ALEAELAAYE SDLDEVSGYV PLGERPRVIV LNKMDIPDAA
     EMAKLQAEQL AEFGWPMYAV SAVTGRGLEA LVFALADMVL RLRKTEPERE VQPVQVLRPQ
     AVGDSSFTVT KQKTGQGLVY QVRGEKPERW VKQTDFANDE AIGFLADRLY NLGVETELLQ
     SGAKSGDTVV IGEMEGGVIF DFEPMQSAGA ELLGARGQDL RLGGSSRRTN QERREQYHQM
     MDGKEAARQN LRREAEQGLW TDPSTD
//
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