(data stored in SCRATCH9089 zone)

SWISSPROT: OBG_PASMU

ID   OBG_PASMU               Reviewed;         390 AA.
AC   Q9CNS4;
DT   13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   11-DEC-2019, entry version 106.
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=PM0351;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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; AE004439; AAK02435.1; -; Genomic_DNA.
DR   RefSeq; WP_005721510.1; NC_002663.1.
DR   SMR; Q9CNS4; -.
DR   PRIDE; Q9CNS4; -.
DR   EnsemblBacteria; AAK02435; AAK02435; PM0351.
DR   GeneID; 29389036; -.
DR   KEGG; pmu:PM0351; -.
DR   eggNOG; ENOG4105C9R; Bacteria.
DR   eggNOG; COG0536; LUCA.
DR   HOGENOM; HOG000019084; -.
DR   KO; K03979; -.
DR   OMA; VVFDWEP; -.
DR   Proteomes; UP000000809; 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; Q9CNS4.
DR   SWISS-2DPAGE; Q9CNS4.
KW   Cytoplasm; GTP-binding; Hydrolase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN           1..390
FT                   /note="GTPase Obg"
FT                   /id="PRO_0000386110"
FT   DOMAIN          1..159
FT                   /note="Obg"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01231"
FT   DOMAIN          160..333
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         314..316
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   390 AA;  43120 MW;  A6E21D3C547A3C64 CRC64;
     MKFIDEALIR VEAGDGGNGC VSFRREKYIP KGGPDGGDGG DGGDVYLVAD ENLNTLIDYR
     FEKRFAAGRG ENGRSAGCTG HRGNDITLRV PVGTRAIDND TKEVLGDLTK HGAKMLVAKG
     GYHGLGNTRF KSSVNRAPRQ KTNGTPGEKR DLQLELMLLA DVGMLGLPNA GKSTFIRAVS
     AAKPKVADYP FTTLVPSLGV VRVDENHSFV VADIPGLIEG AAEGAGLGVR FLKHLERCRV
     LIHLVDIAPI DESDPAENIS IIESELFQYS EALADKPRWL VFNKIDTMSD EEAHERAQAI
     TERLGWDDDY YLISAVTGKN VQPLCRDIMD FIEANPRHEV EQTADEAEVK FKWDDYHQAQ
     LADHQFEDED EDWDDWSEED EEGVETIYKP
//

If you have problems or comments...

PBIL Back to PBIL home page