(data stored in ACNUC7421 zone)

SWISSPROT: OBG_DESOH

ID   OBG_DESOH               Reviewed;         333 AA.
AC   A8ZRY1;
DT   13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   11-DEC-2019, entry version 68.
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=Dole_0088;
OS   Desulfococcus oleovorans (strain DSM 6200 / Hxd3).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales;
OC   Desulfobacteraceae; Desulfococcus.
OX   NCBI_TaxID=96561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6200 / Hxd3;
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., Kiss H., Brettin T., Bruce D., Detter J.C., Han C.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Wawrik B.,
RA   Richardson P.;
RT   "Complete sequence of Desulfococcus oleovorans Hxd3.";
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}.
DR   EMBL; CP000859; ABW65898.1; -; Genomic_DNA.
DR   RefSeq; WP_012173517.1; NC_009943.1.
DR   SMR; A8ZRY1; -.
DR   STRING; 96561.Dole_0088; -.
DR   EnsemblBacteria; ABW65898; ABW65898; Dole_0088.
DR   KEGG; dol:Dole_0088; -.
DR   eggNOG; ENOG4105C9R; Bacteria.
DR   eggNOG; COG0536; LUCA.
DR   HOGENOM; HOG000019084; -.
DR   KO; K03979; -.
DR   OMA; VVFDWEP; -.
DR   OrthoDB; 603226at2; -.
DR   BioCyc; DOLE96561:G1GAC-89-MONOMER; -.
DR   Proteomes; UP000008561; 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   HAMAP; MF_01454; GTPase_Obg; 1.
DR   InterPro; IPR031167; G_OBG.
DR   InterPro; IPR035101; GTP-bd_Obg.
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; IPR006073; GTP_binding_domain.
DR   InterPro; IPR027417; P-loop_NTPase.
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;
DR   PRODOM; A8ZRY1.
DR   SWISS-2DPAGE; A8ZRY1.
KW   Cytoplasm; GTP-binding; Hydrolase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN           1..333
FT                   /note="GTPase Obg"
FT                   /id="PRO_0000385885"
FT   DOMAIN          1..159
FT                   /note="Obg"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01231"
FT   DOMAIN          160..329
FT                   /note="OBG-type G"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT   NP_BIND         166..173
FT                   /note="GTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT   NP_BIND         191..195
FT                   /note="GTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT   NP_BIND         213..216
FT                   /note="GTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT   NP_BIND         283..286
FT                   /note="GTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT   NP_BIND         310..312
FT                   /note="GTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT   METAL           173
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT   METAL           193
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
SQ   SEQUENCE   333 AA;  35064 MW;  359FB6A1E3522817 CRC64;
     MKFIDEATIT VSSGKGGRGC VSFRRERFVP RGGPDGGDGG SGGSLLFRVN PSKRTLYAFR
     SKKQFAAPNG APGEGRQKTG KSGDDLVIEV PPGTLIFDAD TGAIIRDMVS PEEDFVFLTG
     GRGGKGNKHF ATSTHQTPRF AQPGEPAQTA TVRLELKLLA DVGLIGLPNA GKSTLLSVIS
     AARPAIGAYP FTTLSPNLGM VTLAGAEPFA VADIPGLIEG AHTGAGLGIR FLKHIERTRL
     LVHLIDASAI DPADPVAPFR IINAELAMFS PALAERPQVV VLNKMDLTGA EALAQQFINA
     AGIKKCFLIS AATRSGVEEL KKHLFELLCS HDT
//

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