OBG_STRCO
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 03-AUG-2022, entry version 140.
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; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC 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;
CC Evidence={ECO:0000255|HAMAP-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.SCO2595; -.
DR GeneID; 1098029; -.
DR KEGG; sco:SCO2595; -.
DR PATRIC; fig|100226.15.peg.2641; -.
DR eggNOG; COG0536; Bacteria.
DR HOGENOM; CLU_011747_1_3_11; -.
DR InParanoid; P95722; -.
DR OMA; VVFDWEP; -.
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; 2.70.210.12; -; 1.
DR Gene3D; 3.30.300.350; -; 1.
DR Gene3D; 3.40.50.300; -; 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 PANTHER; PTHR11702; PTHR11702; 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; SSF102741; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF82051; SSF82051; 1.
DR TIGRFAMs; TIGR02729; Obg_CgtA; 1.
DR TIGRFAMs; TIGR03595; Obg_CgtA_exten; 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
