OBG_VIBCH
ID OBG_VIBCH Reviewed; 390 AA.
AC Q9KUS8;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 13-OCT-2009, sequence version 2.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=GTPase Obg/CgtA {ECO:0000255|HAMAP-Rule:MF_01454};
DE EC=3.6.5.- {ECO:0000255|HAMAP-Rule:MF_01454, ECO:0000269|PubMed:25912137};
DE AltName: Full=CgtA {ECO:0000303|PubMed:17360576};
DE AltName: Full=GTP-binding protein Obg {ECO:0000255|HAMAP-Rule:MF_01454};
GN Name=cgtA {ECO:0000303|PubMed:17360576}; Synonyms=obg;
GN OrderedLocusNames=VC_0437;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
RN [2]
RP SUBUNIT, INTERACTION WITH SPOT, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=17360576; DOI=10.1073/pnas.0611650104;
RA Raskin D.M., Judson N., Mekalanos J.J.;
RT "Regulation of the stringent response is the essential function of the
RT conserved bacterial G protein CgtA in Vibrio cholerae.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:4636-4641(2007).
RN [3]
RP C-TERMINAL DELETIONS, OVEREXPRESSION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=18456812; DOI=10.1128/jb.02021-07;
RA Shah S., Das B., Bhadra R.K.;
RT "Functional analysis of the essential GTP-binding-protein-coding gene cgtA
RT of Vibrio cholerae.";
RL J. Bacteriol. 190:4764-4771(2008).
RN [4]
RP FUNCTION AS A GTPASE, AND MUTAGENESIS OF GLY-93 AND TYR-189.
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=25912137; DOI=10.1016/j.bbrc.2015.04.079;
RA Chatterjee A., Datta P.P.;
RT "Two conserved amino acids of juxtaposed domains of a ribosomal maturation
RT protein CgtA sustain its optimal GTPase activity.";
RL Biochem. Biophys. Res. Commun. 461:636-641(2015).
CC -!- FUNCTION: Depletion experiments lead to gene down regulation and a
CC dramatic increase in ppGpp levels, like those seen in the stringent
CC response (PubMed:17360576). There is no change in cell morphology in
CC depletion experiments (PubMed:17360576, PubMed:18456812), but cells are
CC very sensitive to the DNA-damaging agent hydroxyurea and are very
CC elongated. Overexpression reduces growth and leads to elongated cells.
CC Overexpression of proteins with C-terminal deletions of 29 or 62 amino
CC acids showed fewer elongated cells (PubMed:18456812).
CC {ECO:0000269|PubMed:17360576, ECO:0000269|PubMed:18456812}.
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. It may play a role in control of
CC the cell cycle, stress response, ribosome biogenesis and in those
CC bacteria that undergo differentiation, in morphogenesis control (By
CC similarity). GTPase activity is stimulated by 50S ribosomal subunits
CC (PubMed:25912137). {ECO:0000255|HAMAP-Rule:MF_01454,
CC ECO:0000269|PubMed:25912137}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01454};
CC -!- SUBUNIT: Monomer (By similarity). Interacts with SpoT (AC Q9KNM2) in a
CC yeast 2-hybrid assay. {ECO:0000255|HAMAP-Rule:MF_01454,
CC ECO:0000269|PubMed:17360576}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01454}.
CC -!- DISRUPTION PHENOTYPE: Essential for growth, it cannot be disrupted. One
CC group found this gene can be disrupted in a relA deletion strain
CC (PubMed:17360576). Another group has found that it cannot be disrupted
CC in a relA deletion strain, in agreement with data from E.coli
CC (PubMed:18456812) (RelA phosphorylates GTP to ppGpp).
CC {ECO:0000269|PubMed:17360576, ECO:0000269|PubMed:18456812}.
CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase
CC superfamily. OBG GTPase family. {ECO:0000255|HAMAP-Rule:MF_01454}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF93610.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE003852; AAF93610.1; ALT_INIT; Genomic_DNA.
DR PIR; D82322; D82322.
DR RefSeq; NP_230091.2; NC_002505.1.
DR RefSeq; WP_000673586.1; NZ_LT906614.1.
DR AlphaFoldDB; Q9KUS8; -.
DR SMR; Q9KUS8; -.
DR DIP; DIP-60891N; -.
DR IntAct; Q9KUS8; 1.
DR STRING; 243277.VC_0437; -.
DR DNASU; 2615698; -.
DR EnsemblBacteria; AAF93610; AAF93610; VC_0437.
DR KEGG; vch:VC_0437; -.
DR PATRIC; fig|243277.26.peg.411; -.
DR eggNOG; COG0536; Bacteria.
DR HOGENOM; CLU_011747_2_0_6; -.
DR OMA; VVFDWEP; -.
DR Proteomes; UP000000584; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
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; Reference proteome.
FT CHAIN 1..390
FT /note="GTPase Obg/CgtA"
FT /id="PRO_0000386377"
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 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"
FT MUTAGEN 93
FT /note="G->A: Decreased intrinsic GTPase, not stimulated by
FT 50S ribosomal subunit. Wild-type GTPase is restored; when
FT associated with G-194."
FT /evidence="ECO:0000269|PubMed:25912137"
FT MUTAGEN 189
FT /note="Y->G: Increased intrinsic GTPase, still stimulated
FT by 50S ribosomal subunit. Wild-type GTPase is restored;
FT when associated with A-98."
FT /evidence="ECO:0000269|PubMed:25912137"
SQ SEQUENCE 390 AA; 43046 MW; 3BA4914B1C1B5611 CRC64;
MKFVDEAVIK VQAGDGGNGV VSFWREKFVT NGGPDGGDGG DGGDVYMVAD ENLNTLIDYR
FQRFYEAERG KNGGGGNCTG KSGKDKELRV PVGTRAVDIH TNEIIGEVAE HGKKVMIAKG
GWHGLGNARF KSSVNRSPRQ KTLGTKGELR DIRLELLLLA DVGMLGMPNA GKSTFIRAVS
AAKPKVADYP FTTLVPSLGV VSVLPEKSFV VADIPGLIEG AAEGAGLGIR FLKHLERCRV
LLHMIDIMPA DQSDPAHNAL TIIDELEQYS EKLAKKPRWL VFNKVDLMSE EEADEIIQNI
IDALAWEGDY FKISAANRQG TKELCMKLAE FMDTLPREAE EKTEAEKVDF TWDYNHKDGL
AGREVITEDD DDWDDWDDEE DDGHVIYVRD
