OBG_SALAI
ID OBG_SALAI Reviewed; 481 AA.
AC A8M0Y9;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 1.
DT 03-AUG-2022, entry version 85.
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=Sare_3858;
OS Salinispora arenicola (strain CNS-205).
OC Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae;
OC Salinispora.
OX NCBI_TaxID=391037;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CNS-205;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Foster B., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Jensen P.R., Moore B.S., Penn K., Jenkins C.,
RA Udwary D., Xiang L., Gontang E., Richardson P.;
RT "Complete sequence of Salinispora arenicola CNS-205.";
RL Submitted (OCT-2007) 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: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 -!- 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; CP000850; ABV99650.1; -; Genomic_DNA.
DR RefSeq; WP_012183889.1; NC_009953.1.
DR AlphaFoldDB; A8M0Y9; -.
DR SMR; A8M0Y9; -.
DR STRING; 391037.Sare_3858; -.
DR PRIDE; A8M0Y9; -.
DR EnsemblBacteria; ABV99650; ABV99650; Sare_3858.
DR GeneID; 5705889; -.
DR KEGG; saq:Sare_3858; -.
DR PATRIC; fig|391037.6.peg.3887; -.
DR eggNOG; COG0536; Bacteria.
DR HOGENOM; CLU_011747_2_1_11; -.
DR OMA; VVFDWEP; -.
DR OrthoDB; 603226at2; -.
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; 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 InterPro; IPR005225; Small_GTP-bd_dom.
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 TIGRFAMs; TIGR00231; small_GTP; 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; GTP-binding; Hydrolase; Magnesium; Metal-binding;
KW Nucleotide-binding.
FT CHAIN 1..481
FT /note="GTPase Obg"
FT /id="PRO_0000386217"
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..426
FT /note="OCT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01229"
FT REGION 440..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..470
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"
SQ SEQUENCE 481 AA; 50675 MW; F26D329F69A0E1F4 CRC64;
MTTFVDRVVL HLQAGDGGHG CVSIHREKFK PFGGPDGGNG GHGGSVSLVV DPQVHTLLDF
HFRPHVKASN GKGGAGSNRD GANGADLVLR VPNGTVVQTT GGTVLADLVG AGTTFEVARG
GRGGRGNAAL ANARRKAPGF AELGEPGDKL DAVLELKSVA DIGLVGYPSA GKSSLISVIS
AAKPKIADYP FTTLVPNLGV VRVDNHTFTV ADVPGLIPGA ATGKGLGLEF LRHVERCAVL
VHVVDTATLE TARDPVADID AIEAELTAYG GLADRPRLVA LNKIDVPDGR DLAEIVRPDL
EARGFRVFEV SAATREGLKE LMFAMGELVA AARAAAPPVE PTRIVIRPKA VDDAGFTVEA
APDGAWVVRG TRPERWIRQT NFDNEEAVGY LADRLARLGV EEKLGKAGAQ AGDLVRIGER
EFDWHPTLYA EFVPGVRGGD QRLAEKTQRP SAAERLAARK ARRQRPGDEP ESDELDGDSG
E
