(data stored in ACNUC7421 zone)

SWISSPROT: OBG_ALCBS

ID   OBG_ALCBS               Reviewed;         391 AA.
AC   Q0VSE6;
DT   13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   11-DEC-2019, entry version 89.
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=ABO_0454;
OS   Alcanivorax borkumensis (strain ATCC 700651 / DSM 11573 / NCIMB 13689 /
OS   SK2).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Alcanivoracaceae; Alcanivorax.
OX   NCBI_TaxID=393595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700651 / DSM 11573 / NCIMB 13689 / SK2;
RX   PubMed=16878126; DOI=10.1038/nbt1232;
RA   Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T., Brecht M.,
RA   Buhrmester J., Chernikova T.N., Denaro R., Ferrer M., Gertler C.,
RA   Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N., Lang S., Linke B.,
RA   McHardy A.C., Meyer F., Nechitaylo T., Puehler A., Regenhardt D., Rupp O.,
RA   Sabirova J.S., Selbitschka W., Yakimov M.M., Timmis K.N., Vorhoelter F.-J.,
RA   Weidner S., Kaiser O., Golyshin P.N.;
RT   "Genome sequence of the ubiquitous hydrocarbon-degrading marine bacterium
RT   Alcanivorax borkumensis.";
RL   Nat. Biotechnol. 24:997-1004(2006).
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; AM286690; CAL15902.1; -; Genomic_DNA.
DR   RefSeq; WP_011587740.1; NC_008260.1.
DR   SMR; Q0VSE6; -.
DR   STRING; 393595.ABO_0454; -.
DR   PRIDE; Q0VSE6; -.
DR   EnsemblBacteria; CAL15902; CAL15902; ABO_0454.
DR   KEGG; abo:ABO_0454; -.
DR   eggNOG; ENOG4105C9R; Bacteria.
DR   eggNOG; COG0536; LUCA.
DR   HOGENOM; HOG000019084; -.
DR   KO; K03979; -.
DR   OMA; VVFDWEP; -.
DR   OrthoDB; 603226at2; -.
DR   BioCyc; ABOR393595:ABO_RS02355-MONOMER; -.
DR   Proteomes; UP000008871; 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; Q0VSE6.
DR   SWISS-2DPAGE; Q0VSE6.
KW   Cytoplasm; GTP-binding; Hydrolase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN           1..391
FT                   /note="GTPase Obg"
FT                   /id="PRO_0000385682"
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   391 AA;  42485 MW;  84FB2B283D8F0C52 CRC64;
     MQFVDEATID VHAGKGGDGC LSFRREKYVE FGGPDGGDGG AGGHVFVQAD TNINTLVDYR
     YDRIFKARNG EPGKGRQMTG KSAEDIILYV PVGTTVVDLD TDEVLADLTD TDKPVMVAQA
     GRGGLGNIHF KSSVNQAPRK TTKGKPGESR RLRLELKVLA DVGLLGMPNA GKSTLIRAIS
     AAKPKVADYP FTTLIPNLGV VKADRYRSFV VADIPGLIEG AAEGAGLGIR FLKHLARTRL
     LLHVVDLAPM DGSSPANHID AIADELDRFS PALAEQERWL VFNKIDLLAD DEAQAQVDAI
     VDELGWQGPV FKVSAAAGVG CEDLVYALMN AIEDRRLLER EDPAYAAAQQ DLRARLEEEA
     RERVQELKAE ARQARQNDDD DDHDVEVVYE P
//

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