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Database: UniProt
Entry: A0A1U7NEM8_9FIRM
LinkDB: A0A1U7NEM8_9FIRM
Original site: A0A1U7NEM8_9FIRM 
ID   A0A1U7NEM8_9FIRM        Unreviewed;       427 AA.
AC   A0A1U7NEM8;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   24-JAN-2024, entry version 28.
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=obgE {ECO:0000313|EMBL:OLU38112.1};
GN   Synonyms=obg {ECO:0000256|HAMAP-Rule:MF_01454};
GN   ORFNames=BO222_09000 {ECO:0000313|EMBL:OLU38112.1};
OS   Ileibacterium valens.
OC   Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC   Erysipelotrichaceae; Ileibacterium.
OX   NCBI_TaxID=1862668 {ECO:0000313|EMBL:OLU38112.1, ECO:0000313|Proteomes:UP000186341};
RN   [1] {ECO:0000313|EMBL:OLU38112.1, ECO:0000313|Proteomes:UP000186341}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NYU-BL-A3 {ECO:0000313|EMBL:OLU38112.1,
RC   ECO:0000313|Proteomes:UP000186341};
RA   Cox L.M., Sohn J., Tyrrell K.L., Citron D.M., Lawson P.A., Patel N.B.,
RA   Iizumi T., Perez-Perez G.I., Goldstein E.J., Blaser M.J.;
RT   "Description of two novel members of the family Erysipelotrichaceae:
RT   Ileibacterium lipovorans gen. nov., sp. nov. and Dubosiella newyorkensis,
RT   gen. nov., sp. nov.";
RL   Submitted (NOV-2016) 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:0000256|HAMAP-Rule:MF_01454}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946,
CC         ECO:0000256|HAMAP-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|ARBA:ARBA00007699,
CC       ECO:0000256|HAMAP-Rule:MF_01454}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OLU38112.1}.
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DR   EMBL; MPJW01000177; OLU38112.1; -; Genomic_DNA.
DR   RefSeq; WP_075820355.1; NZ_MPJW01000177.1.
DR   AlphaFoldDB; A0A1U7NEM8; -.
DR   GeneID; 82203299; -.
DR   OrthoDB; 9807318at2; -.
DR   Proteomes; UP000186341; Unassembled WGS sequence.
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; 3.30.300.350; GTP-binding protein OBG, C-terminal domain; 1.
DR   Gene3D; 2.70.210.12; GTP1/OBG domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   HAMAP; MF_01454; GTPase_Obg; 1.
DR   InterPro; IPR031167; G_OBG.
DR   InterPro; IPR006073; GTP-bd.
DR   InterPro; IPR014100; GTP-bd_Obg/CgtA.
DR   InterPro; IPR036346; GTP-bd_prot_GTP1/OBG_C_sf.
DR   InterPro; IPR006074; GTP1-OBG_CS.
DR   InterPro; IPR006169; GTP1_OBG_dom.
DR   InterPro; IPR036726; GTP1_OBG_dom_sf.
DR   InterPro; IPR045086; OBG_GTPase.
DR   InterPro; IPR015349; OCT_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   NCBIfam; TIGR02729; Obg_CgtA; 1.
DR   NCBIfam; TIGR03595; Obg_CgtA_exten; 1.
DR   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR11702; DEVELOPMENTALLY REGULATED GTP-BINDING PROTEIN-RELATED; 1.
DR   PANTHER; PTHR11702:SF31; MITOCHONDRIAL RIBOSOME-ASSOCIATED GTPASE 2; 1.
DR   Pfam; PF09269; DUF1967; 1.
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; SSF102741; Obg GTP-binding protein C-terminal domain; 1.
DR   SUPFAM; SSF82051; Obg GTP-binding protein N-terminal domain; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51710; G_OBG; 1.
DR   PROSITE; PS00905; GTP1_OBG; 1.
DR   PROSITE; PS51883; OBG; 1.
DR   PROSITE; PS51881; OCT; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01454};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW   Rule:MF_01454}; Hydrolase {ECO:0000256|HAMAP-Rule:MF_01454};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01454};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01454};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_01454}; Reference proteome {ECO:0000313|Proteomes:UP000186341}.
FT   DOMAIN          1..158
FT                   /note="Obg"
FT                   /evidence="ECO:0000259|PROSITE:PS51883"
FT   DOMAIN          159..328
FT                   /note="OBG-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51710"
FT   DOMAIN          348..426
FT                   /note="OCT"
FT                   /evidence="ECO:0000259|PROSITE:PS51881"
FT   REGION          116..142
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         165..172
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01454"
FT   BINDING         172
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01454"
FT   BINDING         190..194
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01454"
FT   BINDING         192
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01454"
FT   BINDING         212..215
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01454"
FT   BINDING         282..285
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01454"
FT   BINDING         309..311
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01454"
SQ   SEQUENCE   427 AA;  47396 MW;  6AE46D983129342A CRC64;
     MFVDQVKVHL KAGKGGDGLV SFKHEKYVAN GGPFGGDGGH GGNIIFEADP GMVTLLDLRY
     HRIIRAEPGE KGKNKRMHGA TAPDTVIKVP LGTMIKKADT GQIIADLTEP GQRQIVAQGG
     RGGRGNSRFK SSRNTVPRYA EPGREGEEFD AIVELRTLAD VGLVGFPSVG KSTLLEAVTK
     AKPEIGDYPF TTISPNVGVV QTKDGRSFVM ADLPGLIEGA SQGKGLGHQF LKHIERCRVI
     VHVIDMGGSE GRDPVEDYRI INQELENYHL RLLDRPQIVV ANKMDLEEAQ ENLKRFKEAY
     PDLEVFETTT IIHEGLDPVL RKAADLLAVT PLFPLTDEKE EDEGVTYTFE EKEKPYTIVR
     HEDGVYEVTG RIIDEQFHPE KLTTDEDYFR FANQMRYLGI DKNLRAAGAK DGDTIMLQGY
     EFEFVEQ
//
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