ID   OBG_STRCO               Reviewed;         478 AA.
AC   P95722;
DT   13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   27-MAR-2024, entry version 148.
DE   RecName: Full=GTPase Obg {ECO:0000255|HAMAP-Rule:MF_01454};
DE            EC=3.6.5.- {ECO:0000255|HAMAP-Rule:MF_01454};
DE   AltName: Full=GTP-binding protein Obg {ECO:0000255|HAMAP-Rule:MF_01454};
GN   Name=obg {ECO:0000255|HAMAP-Rule:MF_01454}; OrderedLocusNames=SCO2595;
GN   ORFNames=SCC88.06c;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=8981995; DOI=10.1128/jb.179.1.170-179.1997;
RA   Okamoto S., Itoh M., Ochi K.;
RT   "Molecular cloning and characterization of the obg gene of Streptomyces
RT   griseus in relation to the onset of morphological differentiation.";
RL   J. Bacteriol. 179:170-179(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(2002).
RN   [3]
RP   FUNCTION, INDUCTION, SUBCELLULAR LOCATION, OVEREXPRESSION, DISRUPTION
RP   PHENOTYPE, AND MUTAGENESIS OF PRO-168; GLY-171; LYS-172; SER-173; LEU-281
RP   AND ASP-285.
RX   PubMed=9786189; DOI=10.1046/j.1365-2958.1998.01042.x;
RA   Okamoto S., Ochi K.;
RT   "An essential GTP-binding protein functions as a regulator for
RT   differentiation in Streptomyces coelicolor.";
RL   Mol. Microbiol. 30:107-119(1998).
RN   [4]
RP   REVIEW.
RX   PubMed=15737924; DOI=10.1016/j.devcel.2005.02.002;
RA   Michel B.;
RT   "Obg/CtgA, a signaling protein that controls replication, translation, and
RT   morphological development?";
RL   Dev. Cell 8:300-301(2005).
CC   -!- FUNCTION: Plays an unknown essential role and a regulatory role in
CC       sporulation. Overexpression suppresses sporulation although cell growth
CC       rate was not reduced. Impaired differentiation was eliminated by
CC       addition of decoyinine, an inhibitor of GMP synthesis. Overexpression
CC       has no effect on undecylprodigiosin production, but decreases
CC       actinorhodin production. {ECO:0000269|PubMed:9786189}.
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:0000255|HAMAP-Rule:MF_01454}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01454};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01454}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01454,
CC       ECO:0000269|PubMed:9786189}. Cell membrane
CC       {ECO:0000269|PubMed:9786189}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:9786189}. Note=No longer associated with the cell
CC       membrane after salt-washing.
CC   -!- INDUCTION: Expressed during vegetative growth it disappears during
CC       stationary phase and sporulation (at protein level).
CC       {ECO:0000269|PubMed:9786189}.
CC   -!- DISRUPTION PHENOTYPE: Essential for growth, it cannot be disrupted.
CC       {ECO:0000269|PubMed:9786189}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase
CC       superfamily. OBG GTPase family. {ECO:0000255|HAMAP-Rule:MF_01454}.
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DR   EMBL; D87915; BAA13498.1; -; Genomic_DNA.
DR   EMBL; AL939113; CAB75376.1; -; Genomic_DNA.
DR   PIR; T42036; T42036.
DR   RefSeq; NP_626832.1; NC_003888.3.
DR   RefSeq; WP_003976206.1; NZ_VNID01000001.1.
DR   AlphaFoldDB; P95722; -.
DR   SMR; P95722; -.
DR   STRING; 100226.gene:17760199; -.
DR   PaxDb; 100226-SCO2595; -.
DR   PATRIC; fig|100226.15.peg.2641; -.
DR   eggNOG; COG0536; Bacteria.
DR   HOGENOM; CLU_011747_1_3_11; -.
DR   InParanoid; P95722; -.
DR   OrthoDB; 9807318at2; -.
DR   PhylomeDB; P95722; -.
DR   Proteomes; UP000001973; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR   GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
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   1: Evidence at protein level;
KW   Cell membrane; Cytoplasm; GTP-binding; Hydrolase; Magnesium; Membrane;
KW   Metal-binding; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..478
FT                   /note="GTPase Obg"
FT                   /id="PRO_0000386323"
FT   DOMAIN          2..159
FT                   /note="Obg"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01231"
FT   DOMAIN          160..330
FT                   /note="OBG-type G"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT   DOMAIN          348..430
FT                   /note="OCT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01229"
FT   REGION          60..88
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          438..478
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        439..472
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:0000255|HAMAP-Rule:MF_01454"
FT   BINDING         173
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT   BINDING         191..195
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT   BINDING         193
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT   BINDING         212..215
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT   BINDING         282..285
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT   BINDING         311..313
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT   MUTAGEN         168
FT                   /note="P->V: Overexpression suppresses sporulation more
FT                   than the wild-type gene."
FT                   /evidence="ECO:0000269|PubMed:9786189"
FT   MUTAGEN         171
FT                   /note="G->A: Overexpression enhances aerial mycelium
FT                   formation, also enhances actinorhodin production."
FT                   /evidence="ECO:0000269|PubMed:9786189"
FT   MUTAGEN         172
FT                   /note="K->N: No phenotype upon overexpression."
FT                   /evidence="ECO:0000269|PubMed:9786189"
FT   MUTAGEN         173
FT                   /note="S->N: No phenotype upon overexpression."
FT                   /evidence="ECO:0000269|PubMed:9786189"
FT   MUTAGEN         281
FT                   /note="L->I: No phenotype upon overexpression."
FT                   /evidence="ECO:0000269|PubMed:9786189"
FT   MUTAGEN         285
FT                   /note="D->A: No phenotype upon overexpression."
FT                   /evidence="ECO:0000269|PubMed:9786189"
SQ   SEQUENCE   478 AA;  51073 MW;  ACAFBCDCF4C9E53B CRC64;
     MTTFVDRVEL HVAAGNGGHG CASVHREKFK PLGGPDGGNG GRGGDVILTV DQSVTTLLDY
     HHSPHRKATN GKPGEGGNRS GKDGQDLVLP VPDGTVVLDG AGNVLADLVG HGTSYVAAQG
     GRGGLGNAAL ASARRKAPGF ALLGEPGDLQ DIHLELKTVA DVALVGYPSA GKSSLISVLS
     AAKPKIADYP FTTLVPNLGV VTAGETVYTV ADVPGLIPGA SQGKGLGLEF LRHVERCSVL
     VHVLDTATLE SERDPLSDLD VIETELREYG GLDNRPRIVV LNKIDVPDGK DLAEMVRPDL
     EARGYRVFEV SAVAHMGLRE LSFALAELVA TARAARPKEE ATRIVIRPKA VDDAGFTVTR
     EEDGLFRVRG EKPERWVRQT DFNNDEAVGY LSDRLNRLGV EDKLMKAGAR NGDGVAIGPE
     DNAVVFDWEP SVTAGAEMLG RRGEDHRFEA PRPAAQRRRD RDAERDEAQQ EFDGFEPF
//