(data stored in ACNUC7421 zone)

SWISSPROT: C5BFA4_EDWI9

ID   C5BFA4_EDWI9            Unreviewed;       392 AA.
AC   C5BFA4;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   05-JUL-2017, entry version 54.
DE   RecName: Full=GTPase Obg {ECO:0000256|HAMAP-Rule:MF_01454};
DE            EC=3.6.5.- {ECO:0000256|HAMAP-Rule:MF_01454};
DE   AltName: Full=GTP-binding protein Obg {ECO:0000256|HAMAP-Rule:MF_01454};
GN   Name=obg {ECO:0000256|HAMAP-Rule:MF_01454};
GN   OrderedLocusNames=NT01EI_0452 {ECO:0000313|EMBL:ACR67690.1};
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503 {ECO:0000313|EMBL:ACR67690.1, ECO:0000313|Proteomes:UP000001485};
RN   [1] {ECO:0000313|Proteomes:UP000001485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146 {ECO:0000313|Proteomes:UP000001485};
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) 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
CC       rates and a fairly low GTP hydrolysis rate. Plays a role in
CC       control of the cell cycle, stress response, ribosome biogenesis
CC       and in those bacteria that undergo differentiation, in
CC       morphogenesis control. {ECO:0000256|HAMAP-Rule:MF_01454}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01454};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_01454}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01454}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase
CC       superfamily. OBG GTPase family. {ECO:0000256|HAMAP-Rule:MF_01454}.
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DR   EMBL; CP001600; ACR67690.1; -; Genomic_DNA.
DR   RefSeq; WP_015869892.1; NC_012779.2.
DR   ProteinModelPortal; C5BFA4; -.
DR   STRING; 634503.NT01EI_0452; -.
DR   EnsemblBacteria; ACR67690; ACR67690; NT01EI_0452.
DR   GeneID; 7961277; -.
DR   KEGG; eic:NT01EI_0452; -.
DR   PATRIC; fig|634503.3.peg.411; -.
DR   eggNOG; ENOG4105C9R; Bacteria.
DR   eggNOG; COG0536; LUCA.
DR   HOGENOM; HOG000019084; -.
DR   KO; K03979; -.
DR   OMA; PHVGIVH; -.
DR   OrthoDB; POG091H025M; -.
DR   Proteomes; UP000001485; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-HAMAP.
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; 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.
PE   3: Inferred from homology;
DR   PRODOM; C5BFA4.
DR   SWISS-2DPAGE; C5BFA4.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001485};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01454};
KW   GTP-binding {ECO:0000256|HAMAP-Rule:MF_01454};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01454};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01454};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01454};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01454};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001485}.
FT   DOMAIN      160    333       OBG-type G (guanine nucleotide-binding).
FT                                {ECO:0000259|PROSITE:PS51710}.
FT   NP_BIND     166    173       GTP. {ECO:0000256|HAMAP-Rule:MF_01454}.
FT   NP_BIND     191    195       GTP. {ECO:0000256|HAMAP-Rule:MF_01454}.
FT   NP_BIND     213    216       GTP. {ECO:0000256|HAMAP-Rule:MF_01454}.
FT   NP_BIND     283    286       GTP. {ECO:0000256|HAMAP-Rule:MF_01454}.
FT   NP_BIND     314    316       GTP. {ECO:0000256|HAMAP-Rule:MF_01454}.
FT   METAL       173    173       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01454}.
FT   METAL       193    193       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01454}.
SQ   SEQUENCE   392 AA;  43600 MW;  0D355BAC9AF6BCFB CRC64;
     MKFVDEAVIH IEAGDGGNGC VSFRREKYIP KGGPDGGDGG DGGDVYLLAD ENLNTLIDYR
     FEKSFRAERG QNGQSRDCTG KRGQDVTIKV PVGTRITDVD TGEVLGDMTR HQQKLMVGKG
     GWHGLGNTRF KSSVNRTPRQ KTNGTPGDKR DLSLELLLLA DVGMLGLPNA GKSTFIRAVS
     AAKPKVADYP FTTLVPSLGV VRMDSEKSFV VADIPGLIEG ASEGAGLGIR FLRHLERCRV
     LLHLIDLAPI DESDPVENAR VIIGELEKYS EKLFQKPRWL VFNKADLLAP EEAKARAQAI
     ADALGWEGEH YLISAANREG VNALCWDVMN FLEAHPREAE VEEEKEKAKK AEFMWDDYHR
     EQLEQAEAEW EEEDDDDWDE DDDEGVEIIY QR
//

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