(data stored in ACNUC7421 zone)

SWISSPROT: OBG_HISS2

ID   OBG_HISS2               Reviewed;         392 AA.
AC   B0UVI2;
DT   13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   11-DEC-2019, entry version 74.
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=HSM_0121;
OS   Histophilus somni (strain 2336) (Haemophilus somnus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Histophilus.
OX   NCBI_TaxID=228400;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2336;
RG   US DOE Joint Genome Institute;
RA   Siddaramappa S., Duncan A.J., Challacombe J.F., Rainey D., Gillaspy A.F.,
RA   Carson M., Gipson J., Gipson M., Bruce D., Detter J.C., Han C.S., Land M.,
RA   Tapia R., Thompson L.S., Orvis J., Zaitshik J., Barnes G., Brettin T.S.,
RA   Dyer D.W., Inzana T.J.;
RT   "Complete sequence of Haemophilus somnus 2336.";
RL   Submitted (FEB-2008) 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; CP000947; ACA30934.1; -; Genomic_DNA.
DR   RefSeq; WP_012340385.1; NC_010519.1.
DR   SMR; B0UVI2; -.
DR   EnsemblBacteria; ACA30934; ACA30934; HSM_0121.
DR   GeneID; 31486396; -.
DR   KEGG; hsm:HSM_0121; -.
DR   HOGENOM; HOG000019084; -.
DR   KO; K03979; -.
DR   OMA; VVFDWEP; -.
DR   OrthoDB; 603226at2; -.
DR   BioCyc; HSOM228400:G1GB8-122-MONOMER; -.
DR   Proteomes; UP000008543; 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; B0UVI2.
DR   SWISS-2DPAGE; B0UVI2.
KW   Cytoplasm; GTP-binding; Hydrolase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN           1..392
FT                   /note="GTPase Obg"
FT                   /id="PRO_0000385967"
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   392 AA;  43444 MW;  673851DED0665225 CRC64;
     MKFIDEALIR IEAGDGGNGC VSFRREKFIP KGGPDGGDGG DGGDVYLIAD ENLNTLIDYR
     FEKSFAAERG ENGRSSDCTG RRGKDITLRV PVGTRAIDND TKEVLGDLTK HGTKMLVAKG
     GYHGLGNARF KSSVNRAPRQ KTNGTPGEKR DLQLELMLLA DVGMLGLPNA GKSTFIRAVS
     AAKPKVADYP FTTLVPSLGV TRVDTSRSFV IADIPGLIEG ASEGAGLGVR FLKHLERCHV
     LIHLVDIAPI DESDPADNIA IIEGELFQYS EKLANKPRWL VFNKIDILSD EEATARAKNI
     MQRLGGEDDY YLISAATGKN VDVLCRDIMD FIEENPRQEQ EKIDAQEVKF KWDDYHQEQL
     SEQVFTEDDQ EEDDWDDWSE DDEEGVEIIY KP
//

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