OBG_CAUVN
ID OBG_CAUVN Reviewed; 354 AA.
AC B8GYI7; O30861; Q7DB40;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 90.
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=CgtAC;
DE AltName: Full=GTP-binding protein Obg {ECO:0000255|HAMAP-Rule:MF_01454};
GN Name=cgtA; Synonyms=obg; OrderedLocusNames=CCNA_00317;
OS Caulobacter vibrioides (strain NA1000 / CB15N) (Caulobacter crescentus).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=565050;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=9335292; DOI=10.1128/jb.179.20.6426-6431.1997;
RA Maddock J., Bhatt A., Koch M., Skidmore J.;
RT "Identification of an essential Caulobacter crescentus gene encoding a
RT member of the Obg family of GTP-binding proteins.";
RL J. Bacteriol. 179:6426-6431(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NA1000 / CB15N;
RX PubMed=20472802; DOI=10.1128/jb.00255-10;
RA Marks M.E., Castro-Rojas C.M., Teiling C., Du L., Kapatral V.,
RA Walunas T.L., Crosson S.;
RT "The genetic basis of laboratory adaptation in Caulobacter crescentus.";
RL J. Bacteriol. 192:3678-3688(2010).
RN [3]
RP PROTEIN SEQUENCE OF N-TERMINUS, GDP- AND GTP-BINDING, POSSIBLE COFACTOR,
RP GTPASE ACTIVITY, AND NUCLEOTIDE-EXCHANGE RATES.
RX PubMed=10482526; DOI=10.1128/jb.181.18.5825-5832.1999;
RA Lin B., Covalle K.L., Maddock J.R.;
RT "The Caulobacter crescentus CgtA protein displays unusual guanine
RT nucleotide binding and exchange properties.";
RL J. Bacteriol. 181:5825-5832(1999).
RN [4]
RP DELETION OF N-TERMINAL 159 AMINO ACIDS.
RX PubMed=11231024; DOI=10.1016/s0014-5793(00)02402-9;
RA Lin B., Maddock J.R.;
RT "The N-terminal domain of the Caulobacter crescentus CgtA protein does not
RT function as a guanine nucleotide exchange factor.";
RL FEBS Lett. 489:108-111(2001).
RN [5]
RP PROTEIN SEQUENCE OF 176-181, AND MUTAGENESIS OF THR-192 AND THR-193.
RX PubMed=11251813; DOI=10.1046/j.1365-2958.2001.02285.x;
RA Lin B., Skidmore J.M., Bhatt A., Pfeffer S.M., Pawloski L., Maddock J.R.;
RT "Alanine scan mutagenesis of the switch I domain of the Caulobacter
RT crescentus CgtA protein reveals critical amino acids required for in vivo
RT function.";
RL Mol. Microbiol. 39:924-934(2001).
RN [6]
RP SUBCELLULAR LOCATION, LARGE SUBUNIT RIBOSOME ASSOCIATION, AND MUTAGENESIS
RP OF C-TERMINUS.
RX PubMed=14702318; DOI=10.1128/jb.186.2.481-489.2004;
RA Lin B., Thayer D.A., Maddock J.R.;
RT "The Caulobacter crescentus CgtAC protein cosediments with the free 50S
RT ribosomal subunit.";
RL J. Bacteriol. 186:481-489(2004).
RN [7]
RP FUNCTION IN CELL CYCLE PROGRESSION, AND MUTAGENESIS OF GLY-80; PRO-168;
RP GLY-171; LYS-172; SER-173; 213-ASP--GLY-216 AND ASN-280.
RX PubMed=15554976; DOI=10.1111/j.1365-2958.2004.04354.x;
RA Datta K., Skidmore J.M., Pu K., Maddock J.R.;
RT "The Caulobacter crescentus GTPase CgtAC is required for progression
RT through the cell cycle and for maintaining 50S ribosomal subunit levels.";
RL Mol. Microbiol. 54:1379-1392(2004).
RN [8]
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 [9]
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: An essential GTPase which binds GTP, GDP and ppGpp with
CC moderate affinity (with a twofold preference for GDP over GTP), shows
CC high guanine nucleotide exchange rate constants for both nucleotides,
CC and has a relatively low GTP hydrolysis rate. Deletion of the 159 N-
CC terminal residues makes a protein that is non-functional in vivo but
CC which retains nucleotide binding and GTPase activity. Required for cell
CC cycle progression from G1 to S phase and for DNA replication.
CC {ECO:0000269|PubMed:15554976}.
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 ECO:0000269|PubMed:14702318}. Note=Cosediments in sucrose gradients
CC with the 50S ribosomal subunit.
CC -!- INDUCTION: Constitutively expressed (at protein level).
CC {ECO:0000269|PubMed:9335292}.
CC -!- DISRUPTION PHENOTYPE: Essential for growth, it cannot be disrupted. As
CC protein levels decrease translating ribosomes, but not individual
CC subunits, also decrease. {ECO:0000269|PubMed:9335292}.
CC -!- MISCELLANEOUS: Site-specific mutations that are activating (168-Val) or
CC dominant negative (173-Asn or 280-Tyr) in ras-like proteins do not have
CC the same phenotype in this protein family.
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; AF019407; AAB81507.1; -; Genomic_DNA.
DR EMBL; CP001340; ACL93784.1; -; Genomic_DNA.
DR RefSeq; WP_010918204.1; NC_011916.1.
DR RefSeq; YP_002515692.1; NC_011916.1.
DR AlphaFoldDB; B8GYI7; -.
DR SMR; B8GYI7; -.
DR PRIDE; B8GYI7; -.
DR EnsemblBacteria; ACL93784; ACL93784; CCNA_00317.
DR GeneID; 7330770; -.
DR KEGG; ccs:CCNA_00317; -.
DR PATRIC; fig|565050.3.peg.315; -.
DR HOGENOM; CLU_011747_2_0_5; -.
DR OMA; VVFDWEP; -.
DR OrthoDB; 603226at2; -.
DR PhylomeDB; B8GYI7; -.
DR PRO; PR:B8GYI7; -.
DR Proteomes; UP000001364; 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; 3.40.50.300; -; 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; Direct protein sequencing; GTP-binding; Hydrolase; Magnesium;
KW Metal-binding; Nucleotide-binding; Reference proteome.
FT CHAIN 1..354
FT /note="GTPase Obg/CgtA"
FT /id="PRO_0000385810"
FT DOMAIN 1..159
FT /note="Obg"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01231"
FT DOMAIN 160..328
FT /note="OBG-type G"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT REGION 335..354
FT /note="Disordered"
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 280..283
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT BINDING 309..311
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT MUTAGEN 80
FT /note="G->E: Grow slowly at 23 degrees Celsius, die at 37
FT degrees Celsius; decrease in 50S ribosomal subunits at both
FT temperatures, partial cell division arrest at 37 degrees
FT Celsius."
FT /evidence="ECO:0000269|PubMed:15554976"
FT MUTAGEN 168
FT /note="P->G: Grows like wild-type at 30 degrees Celsius."
FT /evidence="ECO:0000269|PubMed:15554976"
FT MUTAGEN 168
FT /note="P->R: Grows poorly at 30 degrees Celsius, slightly
FT cold-sensitive."
FT /evidence="ECO:0000269|PubMed:15554976"
FT MUTAGEN 168
FT /note="P->V: Grows like wild-type at 30 degrees Celsius,
FT slightly cold-sensitive. Slight reduction in affinity for
FT GDP, slight increase in GDP exchange rates."
FT /evidence="ECO:0000269|PubMed:15554976"
FT MUTAGEN 171..173
FT /note="GKS->AAA: Unable to support growth."
FT /evidence="ECO:0000269|PubMed:14702318"
FT MUTAGEN 171
FT /note="G->A: Unable to support growth."
FT /evidence="ECO:0000269|PubMed:15554976"
FT MUTAGEN 172
FT /note="K->N: Unable to support growth."
FT /evidence="ECO:0000269|PubMed:15554976"
FT MUTAGEN 173
FT /note="S->N: Unable to support growth. Does not bind GTP,
FT decreased binding of GDP."
FT /evidence="ECO:0000269|PubMed:15554976"
FT MUTAGEN 192
FT /note="T->A: Supports growth. 2.5-fold and 7-fold reduced
FT binding to GDP and GTP respectively. No change in the GTP
FT hydrolysis rate."
FT /evidence="ECO:0000269|PubMed:11251813"
FT MUTAGEN 193
FT /note="T->A: Unable to support growth. 5-fold and 22-fold
FT reduced binding to GDP and GTP respectively. 10-fold
FT decreased GTP hydrolysis rate."
FT /evidence="ECO:0000269|PubMed:11251813"
FT MUTAGEN 213..216
FT /note="DIPG->AIPA: Unable to support growth."
FT /evidence="ECO:0000269|PubMed:15554976"
FT MUTAGEN 280
FT /note="N->K,Y: Grows poorly at 30 degrees Celsius."
FT /evidence="ECO:0000269|PubMed:15554976"
FT MUTAGEN 348..354
FT /note="Missing: No effect. Replacment of this region with
FT an epitope tag (3HA) decreases growth rate."
FT /evidence="ECO:0000269|PubMed:14702318"
SQ SEQUENCE 354 AA; 37871 MW; DF81EAC1012A5266 CRC64;
MKFLDQCKIY IRSGNGGGGS VSFRREKYIE YGGPDGGDGG RGGDVWIEAV EGLNTLIDYR
YQQHFKAGTG VHGMGRARHG AAGEDVVLKV PVGTEVLEED KETLIADLDH AGMRLLLAKG
GNGGWGNLHF KGPVNQAPKY ANPGQEGEER WIWLRLKLIA DVGLVGLPNA GKSTFLAAAS
AAKPKIADYP FTTLTPNLGV VDLSSSERFV LADIPGLIEG ASEGAGLGTR FLGHVERSAT
LIHLIDATQD DVAGAYETIR GELEAYGDEL ADKAEILALN KIDALDEETL AEKVAELEAV
SGIKPRLVSG VSGQGVTELL RAAYKQVRIR RGDLEEEIDD DEDHVDETPG GWTP
