OBG_PARD8
ID OBG_PARD8 Reviewed; 386 AA.
AC A6LD68;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 92.
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=BDI_1897;
OS Parabacteroides distasonis (strain ATCC 8503 / DSM 20701 / CIP 104284 / JCM
OS 5825 / NCTC 11152).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Tannerellaceae;
OC Parabacteroides.
OX NCBI_TaxID=435591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8503 / DSM 20701 / CIP 104284 / JCM 5825 / NCTC 11152;
RX PubMed=17579514; DOI=10.1371/journal.pbio.0050156;
RA Xu J., Mahowald M.A., Ley R.E., Lozupone C.A., Hamady M., Martens E.C.,
RA Henrissat B., Coutinho P.M., Minx P., Latreille P., Cordum H.,
RA Van Brunt A., Kim K., Fulton R.S., Fulton L.A., Clifton S.W., Wilson R.K.,
RA Knight R.D., Gordon J.I.;
RT "Evolution of symbiotic bacteria in the distal human intestine.";
RL PLoS Biol. 5:1574-1586(2007).
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; CP000140; ABR43632.1; -; Genomic_DNA.
DR RefSeq; WP_005854807.1; NC_009615.1.
DR AlphaFoldDB; A6LD68; -.
DR SMR; A6LD68; -.
DR STRING; 435591.BDI_1897; -.
DR EnsemblBacteria; ABR43632; ABR43632; BDI_1897.
DR KEGG; pdi:BDI_1897; -.
DR eggNOG; COG0536; Bacteria.
DR HOGENOM; CLU_011747_2_0_10; -.
DR OMA; VVFDWEP; -.
DR OrthoDB; 603226at2; -.
DR BioCyc; PDIS435591:G1G5A-1950-MON; -.
DR Proteomes; UP000000566; 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; 2.70.210.12; -; 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; IPR006074; GTP1-OBG_CS.
DR InterPro; IPR006169; GTP1_OBG_dom.
DR InterPro; IPR036726; GTP1_OBG_dom_sf.
DR InterPro; IPR045086; OBG_GTPase.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11702; PTHR11702; 1.
DR Pfam; PF01018; GTP1_OBG; 1.
DR Pfam; PF01926; MMR_HSR1; 1.
DR PIRSF; PIRSF002401; GTP_bd_Obg/CgtA; 1.
DR PRINTS; PR00326; GTP1OBG.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF82051; SSF82051; 1.
DR TIGRFAMs; TIGR02729; Obg_CgtA; 1.
DR PROSITE; PS51710; G_OBG; 1.
DR PROSITE; PS00905; GTP1_OBG; 1.
DR PROSITE; PS51883; OBG; 1.
PE 3: Inferred from homology;
KW Cytoplasm; GTP-binding; Hydrolase; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..386
FT /note="GTPase Obg"
FT /id="PRO_0000386107"
FT DOMAIN 4..162
FT /note="Obg"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01231"
FT DOMAIN 163..329
FT /note="OBG-type G"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT REGION 18..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 357..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 169..176
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT BINDING 176
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT BINDING 194..198
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT BINDING 196
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT BINDING 216..219
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT BINDING 283..286
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT BINDING 310..312
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
SQ SEQUENCE 386 AA; 43307 MW; 887FFE85AA47501D CRC64;
MAESNFVDYV KIYCRSGKGG RGSSHFRREK YIPKGGPDGG DGGRGGHVYL RGNRNYWTLL
HLKYERHIMA TNGESGSAKR SSGKDGEDRV IEVPCGTVVY DAETGEFICD VTEDGQQVML
LKGGRGGLGN FNFKTATNQA PRYSQPGEPA LERTVILQLK LLADVGLVGF PNAGKSTLLS
VVSAAKPKIA NYPFTTLEPN LGIVSYRDNR SFVMADIPGI IEGASEGKGL GLRFLRHIER
NSLLLFMVPA EADDIKKEYE ILHNELVKYN PELLDKRRVL AITKSDMLDE ELIEALSQDL
PEGIPYVFIS SITGLGIVEL KDLLWKELNK ENFHEAERIV HKNIDVSTLE FEDDDEYIFP
VDEDEDDPDE EYEEYWDDDE DEDTRK
