ID K0P213_9BACT Unreviewed; 334 AA.
AC K0P213;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 53.
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 ECO:0000313|EMBL:CCM10059.1};
GN ORFNames=CAHE_0282 {ECO:0000313|EMBL:CCM10059.1};
OS Cardinium endosymbiont cEper1 of Encarsia pergandiella.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Amoebophilaceae;
OC Cardinium.
OX NCBI_TaxID=1231626 {ECO:0000313|EMBL:CCM10059.1, ECO:0000313|Proteomes:UP000003996};
RN [1] {ECO:0000313|EMBL:CCM10059.1, ECO:0000313|Proteomes:UP000003996}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Zchori-Fein et al. 2004 {ECO:0000313|Proteomes:UP000003996};
RX PubMed=23133394; DOI=10.1371/journal.pgen.1003012;
RA Penz T., Schmitz-Esser S., Kelly S.E., Cass B.N., Muller A., Woyke T.,
RA Malfatti S.A., Hunter M.S., Horn M.;
RT "Comparative Genomics Suggests an Independent Origin of Cytoplasmic
RT Incompatibility in Cardinium hertigii.";
RL PLoS Genet. 8:e1003012-e1003012(2012).
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|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}.
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DR EMBL; HE983995; CCM10059.1; -; Genomic_DNA.
DR RefSeq; WP_014934433.1; NC_018605.1.
DR AlphaFoldDB; K0P213; -.
DR STRING; 1231626.CAHE_0282; -.
DR KEGG; che:CAHE_0282; -.
DR PATRIC; fig|1231626.3.peg.279; -.
DR eggNOG; COG0536; Bacteria.
DR HOGENOM; CLU_011747_2_0_10; -.
DR OrthoDB; 9807318at2; -.
DR BioCyc; CEND1231626:AL022_RS01280-MONOMER; -.
DR Proteomes; UP000003996; 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; 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; IPR006074; GTP1-OBG_CS.
DR InterPro; IPR006169; GTP1_OBG_dom.
DR InterPro; IPR036726; GTP1_OBG_dom_sf.
DR InterPro; IPR045086; OBG_GTPase.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR02729; Obg_CgtA; 1.
DR PANTHER; PTHR11702; DEVELOPMENTALLY REGULATED GTP-BINDING PROTEIN-RELATED; 1.
DR PANTHER; PTHR11702:SF31; MITOCHONDRIAL RIBOSOME-ASSOCIATED GTPASE 2; 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; 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.
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}.
FT DOMAIN 4..162
FT /note="Obg"
FT /evidence="ECO:0000259|PROSITE:PS51883"
FT DOMAIN 163..329
FT /note="OBG-type G"
FT /evidence="ECO:0000259|PROSITE:PS51710"
FT BINDING 169..176
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01454"
FT BINDING 176
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01454"
FT BINDING 194..198
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01454"
FT BINDING 196
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01454"
FT BINDING 216..219
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01454"
FT BINDING 283..286
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01454"
FT BINDING 310..312
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01454"
SQ SEQUENCE 334 AA; 35778 MW; F89FC8A9F57B0FEA CRC64;
MSSPNFIDHV KLYLRAGKGG AGLIHFIRAK FVPKGGPDGG DGGRGGHIIL RGAKQYGTLL
HLKYRKHIIA ANGEVGGDSC KTGASGKDVI IDVPLGTVAK SADNEEVFLE VLEDKKKYIL
MQGGKGGWGN TRFKTPTHQT PRIAYPGTPG MESWMVLELK LLADVGLVGL PNAGKSTLLS
VVSAAKPRID SYPFTTLVPN LGVVAYRDQQ SFVMADIPGI IEGAAGGRGL GTRFLRHIER
NAVLLFMVSA ESNSINSGYN MLLSELEAHN PLLLDKPRLL VVSKVDLLSQ TARKVLLQNL
PKGITCCFIS AATGEGIIDL KDLIWEKLSI SAVQ
//
