OBG_LIMRD
ID OBG_LIMRD Reviewed; 438 AA.
AC A5VJ99;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 102.
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=Lreu_0658;
OS Limosilactobacillus reuteri (strain DSM 20016) (Lactobacillus reuteri).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Limosilactobacillus.
OX NCBI_TaxID=557436;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20016;
RX PubMed=21379339; DOI=10.1371/journal.pgen.1001314;
RA Frese S.A., Benson A.K., Tannock G.W., Loach D.M., Kim J., Zhang M.,
RA Oh P.L., Heng N.C., Patil P.B., Juge N., Mackenzie D.A., Pearson B.M.,
RA Lapidus A., Dalin E., Tice H., Goltsman E., Land M., Hauser L., Ivanova N.,
RA Kyrpides N.C., Walter J.;
RT "The evolution of host specialization in the vertebrate gut symbiont
RT Lactobacillus reuteri.";
RL PLoS Genet. 7:E1001314-E1001314(2011).
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}.
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DR EMBL; CP000705; ABQ82923.1; -; Genomic_DNA.
DR RefSeq; WP_003668233.1; NZ_AZDD01000002.1.
DR AlphaFoldDB; A5VJ99; -.
DR SMR; A5VJ99; -.
DR STRING; 557436.Lreu_0658; -.
DR PRIDE; A5VJ99; -.
DR EnsemblBacteria; ABQ82923; ABQ82923; Lreu_0658.
DR GeneID; 66470809; -.
DR KEGG; lre:Lreu_0658; -.
DR PATRIC; fig|557436.17.peg.730; -.
DR eggNOG; COG0536; Bacteria.
DR HOGENOM; CLU_011747_2_1_9; -.
DR OMA; VVFDWEP; -.
DR Proteomes; UP000001991; 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 Gene3D; 3.30.300.350; -; 1.
DR Gene3D; 3.40.50.300; -; 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 PANTHER; PTHR11702; PTHR11702; 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; SSF102741; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF82051; SSF82051; 1.
DR TIGRFAMs; TIGR02729; Obg_CgtA; 1.
DR TIGRFAMs; TIGR03595; Obg_CgtA_exten; 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; GTP-binding; Hydrolase; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..438
FT /note="GTPase Obg"
FT /id="PRO_0000386000"
FT DOMAIN 2..160
FT /note="Obg"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01231"
FT DOMAIN 161..337
FT /note="OBG-type G"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT DOMAIN 360..438
FT /note="OCT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01229"
FT BINDING 167..174
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT BINDING 174
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT BINDING 192..196
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT BINDING 194
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT BINDING 214..217
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT BINDING 284..287
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT BINDING 318..320
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
SQ SEQUENCE 438 AA; 47976 MW; 091193B1A22547E1 CRC64;
MNMFVDQIKI EVHAGKGGDG MVAFRREKYV PNGGPAGGDG GRGGSIILKV DEGLRTLMDF
RYHRIFKAKN GGNGMSKQMT GPSAEDTIIA VPQGTTVRDL DTGKIIGDLV EKDQELVVAK
GGRGGRGNIH FASAKNPAPE IAENGEPGED HYLELELKML ADVGLIGFPS VGKSTLLSVV
TGAKPKIAAY EFTTLTPNLG MVMLPDGRDF AMADMPGLIE GASKGIGLGL KFLRHIERTR
VLLHLVDMSS EDPHQAIERY RQINKELADY DPELLKRPQI VVATKMDLPN SADNLAAFKA
DLAADKTLEK QPEIFPISAV THQGVQQLMQ LTADLLDKTP AFDSESHDKE LVAEYRAAAP
DKKDEADFTI TKDEDGTWVL GGEKLIRLFK MTDLTHEESQ LRFARQLRHM GVDDALRAKG
VQDGDLVRIE KFVFEFIQ
