ID A0A101NCM2_9ACTN Unreviewed; 478 AA.
AC A0A101NCM2;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
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:KUM90661.1};
GN Synonyms=obg {ECO:0000256|HAMAP-Rule:MF_01454};
GN ORFNames=AQI94_02355 {ECO:0000313|EMBL:KUM90661.1};
OS Streptomyces pseudovenezuelae.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces; Streptomyces aurantiacus group.
OX NCBI_TaxID=67350 {ECO:0000313|EMBL:KUM90661.1, ECO:0000313|Proteomes:UP000053039};
RN [1] {ECO:0000313|EMBL:KUM90661.1, ECO:0000313|Proteomes:UP000053039}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40212 {ECO:0000313|EMBL:KUM90661.1,
RC ECO:0000313|Proteomes:UP000053039};
RA Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT "Draft genome sequence of Streptomyces pseudovenezuelae DSM 40212, type
RT strain for the species Streptomyces pseudovenezuelae.";
RL Submitted (OCT-2015) 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:KUM90661.1}.
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; LMWM01000003; KUM90661.1; -; Genomic_DNA.
DR RefSeq; WP_031043335.1; NZ_KQ948144.1.
DR AlphaFoldDB; A0A101NCM2; -.
DR OrthoDB; 9807318at2; -.
DR Proteomes; UP000053039; 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}.
FT DOMAIN 2..159
FT /note="Obg"
FT /evidence="ECO:0000259|PROSITE:PS51883"
FT DOMAIN 160..330
FT /note="OBG-type G"
FT /evidence="ECO:0000259|PROSITE:PS51710"
FT DOMAIN 348..430
FT /note="OCT"
FT /evidence="ECO:0000259|PROSITE:PS51881"
FT REGION 60..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 439..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..468
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 282..285
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01454"
FT BINDING 311..313
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01454"
SQ SEQUENCE 478 AA; 50852 MW; A37779FBEBAF2A0A CRC64;
MTTFVDRVEL HVAAGNGGHG CASVHREKFK PLGGPDGGNG GRGGDVILTV DQSVTTLLDY
HHSPHRKATN GKPGEGGNRS GKDGQDLVLP VPDGTVVLDK AGNVLADLVG HGTSYVAAQG
GRGGLGNAAL ASARRKAPGF ALLGVPGDLQ DIVLELKTVA DVALVGYPSA GKSSLISVLS
AAKPKIADYP FTTLVPNLGV VTAGDTVYTI ADVPGLIPGA SQGKGLGLEF LRHVERCSVL
VHVLDTATLE SDRDPVSDLD IIEAELTEYG GLGNRPRIVV LNKIDVPDGK DLAEMVRPDL
EARGYRVFEV SAVAHMGLKE LSFALADLVG TARAARPQEE ATRIVIRPKA VDDAGFTVVR
EEDGLYRVRG EKPERWVRQT DFSNDEAVGY LADRLNRLGV EEALMKAGAR SGDGVAIGPE
DNAVVFDWEP TVMAGAEMLG RRGEDHRFEE PRPAAQRRRD KQAERDEAAQ EFDDFEPF
//
