OBG_VIBHA
ID OBG_VIBHA Reviewed; 391 AA.
AC Q6E0U3; Q9L5X7;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=GTPase Obg/CgtA {ECO:0000255|HAMAP-Rule:MF_01454};
DE EC=3.6.5.- {ECO:0000255|HAMAP-Rule:MF_01454};
DE AltName: Full=CgtA {ECO:0000303|PubMed:11160812};
DE AltName: Full=GTP-binding protein Obg {ECO:0000255|HAMAP-Rule:MF_01454};
GN Name=cgtA {ECO:0000303|PubMed:11160812}; Synonyms=obg;
OS Vibrio harveyi (Beneckea harveyi).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=669;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BB7;
RA Sikora A.E.;
RT "Sequence of Vibrio harveyi cgtA gene.";
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-99, AND DISRUPTION PHENOTYPE.
RC STRAIN=BB7;
RX PubMed=11160812; DOI=10.1099/00221287-147-1-183;
RA Czyz A., Zielke R., Konopa G., Wegrzyn G.;
RT "A Vibrio harveyi insertional mutant in the cgtA (obg, yhbZ) gene, whose
RT homologues are present in diverse organisms ranging from bacteria to humans
RT and are essential genes in many bacterial species.";
RL Microbiology 147:183-191(2001).
RN [3]
RP INDUCTION.
RC STRAIN=BB7;
RX PubMed=12855728; DOI=10.1099/mic.0.26292-0;
RA Zielke R., Sikora A., Dutkiewicz R., Wegrzyn G., Czyz A.;
RT "Involvement of the cgtA gene function in stimulation of DNA repair in
RT Escherichia coli and Vibrio harveyi.";
RL Microbiology 149:1763-1770(2003).
RN [4]
RP REVIEW.
RX PubMed=15827604;
RA Czyz A., Wegrzyn G.;
RT "The Obg subfamily of bacterial GTP-binding proteins: essential proteins of
RT largely unknown functions that are evolutionarily conserved from bacteria
RT to humans.";
RL Acta Biochim. Pol. 52:35-43(2005).
RN [5]
RP REVIEW.
RX PubMed=15737924; DOI=10.1016/j.devcel.2005.02.002;
RA Michel B.;
RT "Obg/CtgA, a signaling protein that controls replication, translation, and
RT morphological development?";
RL Dev. Cell 8:300-301(2005).
CC -!- FUNCTION: Overexpression protects cells against UV damage.
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 -!- INDUCTION: Induced in a dose-dependent manner by UV irradiation (at
CC protein level). {ECO:0000269|PubMed:12855728}.
CC -!- DISRUPTION PHENOTYPE: Deletion of all but the first 99 amino acids
CC confers multiple defects in several cellular processes, including
CC increased sensitivity to UV irradiation. It is not clear if this is a
CC complete disruption or not, as in C.crescentus and E.coli this gene
CC cannot be disrupted. {ECO:0000269|PubMed:11160812}.
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; AY623050; AAT67594.1; -; Genomic_DNA.
DR EMBL; AF247677; AAF66421.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6E0U3; -.
DR SMR; Q6E0U3; -.
DR STRING; 669.AL538_11165; -.
DR PRIDE; Q6E0U3; -.
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; 3.40.50.300; -; 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; 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 PANTHER; PTHR11702; PTHR11702; 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; 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 1: Evidence at protein level;
KW Cytoplasm; GTP-binding; Hydrolase; Magnesium; Metal-binding;
KW Nucleotide-binding.
FT CHAIN 1..391
FT /note="GTPase Obg/CgtA"
FT /id="PRO_0000386380"
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 REGION 367..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..382
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 166..173
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT BINDING 173
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT BINDING 191..195
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT BINDING 193
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT BINDING 213..216
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT BINDING 283..286
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT BINDING 314..316
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
SQ SEQUENCE 391 AA; 43419 MW; 5434F5AD3ADE4B64 CRC64;
MKFVDEAVVK VQAGDGGSGV VSFWREKFIT KGGPDGGDGG DGGDVYIQAD ENLNTLIDYR
FQRFYEAERG ENGRGGNCTG KRGKDITLRV PVGTRAVDIH TNEIVAEVAE HGKKVMVAKG
GWHGLGNTRF KSSVNRAPRQ RTLGTKGEIR EIRLELLLLA DVGMLGLPNA GKSTFIRAVS
AAKPKVADYP FTTLIPSLGV VSVVPEKSFV VADIPGLIEG AADGAGLGIR FLKHLERCRV
LLHMIDIMPI DQSDPIQNAL TIIDELEQYS EKLAGKPRWL VFNKTDLMPE EEANEKIQEI
LDALGWEDEY FKISAINRNG TKELCYKLAD FMENLPREEE EVAEEDKVNF MWDDYHKDAI
AGKDVITEED DDDWDDCDDE DDDGHVVYVR D
