ID A0A023X396_9ACTN Unreviewed; 417 AA.
AC A0A023X396;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 24-JAN-2024, entry version 48.
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=RradSPS_1530 {ECO:0000313|EMBL:AHY46813.1};
OS Rubrobacter radiotolerans.
OC Bacteria; Actinomycetota; Rubrobacteria; Rubrobacterales; Rubrobacteraceae;
OC Rubrobacter.
OX NCBI_TaxID=42256 {ECO:0000313|EMBL:AHY46813.1, ECO:0000313|Proteomes:UP000025229};
RN [1] {ECO:0000313|EMBL:AHY46813.1, ECO:0000313|Proteomes:UP000025229}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RSPS-4 {ECO:0000313|EMBL:AHY46813.1,
RC ECO:0000313|Proteomes:UP000025229};
RA Egas C.C., Barroso C.C., Froufe H.J.C., Pacheco J.J., Albuquerque L.L.,
RA da Costa M.M.S.;
RT "Complete genome sequence of the Radio-Resistant Rubrobacter radiotolerans
RT RSPS-4.";
RL Submitted (MAR-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}.
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DR EMBL; CP007514; AHY46813.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A023X396; -.
DR STRING; 42256.RradSPS_1530; -.
DR KEGG; rrd:RradSPS_1530; -.
DR PATRIC; fig|42256.3.peg.1549; -.
DR eggNOG; COG0536; Bacteria.
DR HOGENOM; CLU_011747_2_1_11; -.
DR OrthoDB; 9807318at2; -.
DR Proteomes; UP000025229; 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; 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; 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; 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:UP000025229}.
FT DOMAIN 1..157
FT /note="Obg"
FT /evidence="ECO:0000259|PROSITE:PS51883"
FT DOMAIN 158..325
FT /note="OBG-type G"
FT /evidence="ECO:0000259|PROSITE:PS51710"
FT DOMAIN 334..417
FT /note="OCT"
FT /evidence="ECO:0000259|PROSITE:PS51881"
FT REGION 15..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 118..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 218..221
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01454"
FT BINDING 282..285
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01454"
FT BINDING 306..308
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01454"
SQ SEQUENCE 417 AA; 44533 MW; 9294B23806EF151A CRC64;
MQFIDEARLT VRAGRGGDGS VSFNREKYKP RGGPDGGRGG DGGSVVLRAT EDLATLEYLY
HKNLVSAGRG RHGSGNNRSG ESGEDAIVEV PVGTLVFDSE GLISDLAKPG DSIVVARGGE
GGRGNGSFAT STRQAPKFRE RGLPGEEREI RLELRVLSDV GLVGLPNAGK SSLLAALSAA
RPKVGGYPFT TLTPKLGVVD ERGASREAGL REPFVVADIP GLISGASEGR GLGNRFLRHV
ARARVLALIL DASEDPEGAE ATLRAELYAA KLSDKPTVVA LNKVDLLDAE LREYVREIFP
GAVLISAATG EGVPEFREVL ARKLARAAEV AAPAHEREHR VFRPTWKGLR VEREDGVYVV
SGEEVERLAL KTDWGSEEGV EHFGRELERK GVVAALRRAG AAEGDEVRVG ETVFDFR
//
