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GTPase Obg/CgtA (EC 3.6.5.-) (CgtAC) (GTP-binding protein Obg)

 OBG_CAUVN               Reviewed;         354 AA.
B8GYI7; O30861; Q7DB40;
13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
03-MAR-2009, sequence version 1.
25-APR-2018, entry version 71.
RecName: Full=GTPase Obg/CgtA {ECO:0000255|HAMAP-Rule:MF_01454};
EC=3.6.5.- {ECO:0000255|HAMAP-Rule:MF_01454};
AltName: Full=CgtAC;
AltName: Full=GTP-binding protein Obg {ECO:0000255|HAMAP-Rule:MF_01454};
Name=cgtA; Synonyms=obg; OrderedLocusNames=CCNA_00317;
Caulobacter vibrioides (strain NA1000 / CB15N) (Caulobacter
crescentus).
Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
Caulobacteraceae; Caulobacter.
NCBI_TaxID=565050;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, AND DISRUPTION
PHENOTYPE.
PubMed=9335292; DOI=10.1128/jb.179.20.6426-6431.1997;
Maddock J., Bhatt A., Koch M., Skidmore J.;
"Identification of an essential Caulobacter crescentus gene encoding a
member of the Obg family of GTP-binding proteins.";
J. Bacteriol. 179:6426-6431(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=NA1000 / CB15N;
PubMed=20472802; DOI=10.1128/JB.00255-10;
Marks M.E., Castro-Rojas C.M., Teiling C., Du L., Kapatral V.,
Walunas T.L., Crosson S.;
"The genetic basis of laboratory adaptation in Caulobacter
crescentus.";
J. Bacteriol. 192:3678-3688(2010).
[3]
PROTEIN SEQUENCE OF N-TERMINUS, GDP- AND GTP-BINDING, POSSIBLE
COFACTOR, GTPASE ACTIVITY, AND NUCLEOTIDE-EXCHANGE RATES.
PubMed=10482526;
Lin B., Covalle K.L., Maddock J.R.;
"The Caulobacter crescentus CgtA protein displays unusual guanine
nucleotide binding and exchange properties.";
J. Bacteriol. 181:5825-5832(1999).
[4]
DELETION OF N-TERMINAL 159 AMINO ACIDS.
PubMed=11231024; DOI=10.1016/S0014-5793(00)02402-9;
Lin B., Maddock J.R.;
"The N-terminal domain of the Caulobacter crescentus CgtA protein does
not function as a guanine nucleotide exchange factor.";
FEBS Lett. 489:108-111(2001).
[5]
PROTEIN SEQUENCE OF 176-181, AND MUTAGENESIS OF THR-192 AND THR-193.
PubMed=11251813; DOI=10.1046/j.1365-2958.2001.02285.x;
Lin B., Skidmore J.M., Bhatt A., Pfeffer S.M., Pawloski L.,
Maddock J.R.;
"Alanine scan mutagenesis of the switch I domain of the Caulobacter
crescentus CgtA protein reveals critical amino acids required for in
vivo function.";
Mol. Microbiol. 39:924-934(2001).
[6]
SUBCELLULAR LOCATION, LARGE SUBUNIT RIBOSOME ASSOCIATION, AND
MUTAGENESIS OF C-TERMINUS.
PubMed=14702318; DOI=10.1128/JB.186.2.481-489.2004;
Lin B., Thayer D.A., Maddock J.R.;
"The Caulobacter crescentus CgtAC protein cosediments with the free
50S ribosomal subunit.";
J. Bacteriol. 186:481-489(2004).
[7]
FUNCTION IN CELL CYCLE PROGRESSION, AND MUTAGENESIS OF GLY-80;
PRO-168; GLY-171; LYS-172; SER-173; 213-ASP--GLY-216 AND ASN-280.
PubMed=15554976; DOI=10.1111/j.1365-2958.2004.04354.x;
Datta K., Skidmore J.M., Pu K., Maddock J.R.;
"The Caulobacter crescentus GTPase CgtAC is required for progression
through the cell cycle and for maintaining 50S ribosomal subunit
levels.";
Mol. Microbiol. 54:1379-1392(2004).
[8]
REVIEW.
PubMed=15827604;
Czyz A., Wegrzyn G.;
"The Obg subfamily of bacterial GTP-binding proteins: essential
proteins of largely unknown functions that are evolutionarily
conserved from bacteria to humans.";
Acta Biochim. Pol. 52:35-43(2005).
[9]
REVIEW.
PubMed=15737924; DOI=10.1016/j.devcel.2005.02.002;
Michel B.;
"Obg/CtgA, a signaling protein that controls replication, translation,
and morphological development?";
Dev. Cell 8:300-301(2005).
-!- FUNCTION: An essential GTPase which binds GTP, GDP and ppGpp with
moderate affinity (with a twofold preference for GDP over GTP),
shows high guanine nucleotide exchange rate constants for both
nucleotides, and has a relatively low GTP hydrolysis rate.
Deletion of the 159 N-terminal residues makes a protein that is
non-functional in vivo but which retains nucleotide binding and
GTPase activity. Required for cell cycle progression from G1 to S
phase and for DNA replication. {ECO:0000269|PubMed:15554976}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000255|HAMAP-Rule:MF_01454};
-!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01454}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01454,
ECO:0000269|PubMed:14702318}. Note=Cosediments in sucrose
gradients with the 50S ribosomal subunit.
-!- INDUCTION: Constitutively expressed (at protein level).
{ECO:0000269|PubMed:9335292}.
-!- DISRUPTION PHENOTYPE: Essential for growth, it cannot be
disrupted. As protein levels decrease translating ribosomes, but
not individual subunits, also decrease.
{ECO:0000269|PubMed:9335292}.
-!- MISCELLANEOUS: Site-specific mutations that are activating (168-
Val) or dominant negative (173-Asn or 280-Tyr) in ras-like
proteins do not have the same phenotype in this protein family.
-!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase
superfamily. OBG GTPase family. {ECO:0000255|HAMAP-Rule:MF_01454}.
-----------------------------------------------------------------------
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EMBL; AF019407; AAB81507.1; -; Genomic_DNA.
EMBL; CP001340; ACL93784.1; -; Genomic_DNA.
RefSeq; WP_010918204.1; NC_011916.1.
RefSeq; YP_002515692.1; NC_011916.1.
ProteinModelPortal; B8GYI7; -.
SMR; B8GYI7; -.
EnsemblBacteria; ACL93784; ACL93784; CCNA_00317.
GeneID; 7330770; -.
KEGG; ccs:CCNA_00317; -.
PATRIC; fig|565050.3.peg.315; -.
HOGENOM; HOG000019084; -.
KO; K03979; -.
OMA; PHVGIVH; -.
OrthoDB; POG091H025M; -.
PRO; PR:B8GYI7; -.
Proteomes; UP000001364; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO; GO:0003924; F:GTPase activity; IEA:InterPro.
GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
CDD; cd01898; Obg; 1.
Gene3D; 2.70.210.12; -; 1.
HAMAP; MF_01454; GTPase_Obg; 1.
InterPro; IPR031167; G_OBG.
InterPro; IPR035101; GTP-bd_Obg.
InterPro; IPR014100; GTP-bd_Obg/CgtA.
InterPro; IPR006074; GTP1-OBG_CS.
InterPro; IPR006169; GTP1_OBG_dom.
InterPro; IPR036726; GTP1_OBG_dom_sf.
InterPro; IPR006073; GTP_binding_domain.
InterPro; IPR027417; P-loop_NTPase.
Pfam; PF01018; GTP1_OBG; 1.
Pfam; PF01926; MMR_HSR1; 1.
PIRSF; PIRSF002401; GTP_bd_Obg/CgtA; 1.
PRINTS; PR00326; GTP1OBG.
SUPFAM; SSF52540; SSF52540; 1.
SUPFAM; SSF82051; SSF82051; 1.
TIGRFAMs; TIGR02729; Obg_CgtA; 1.
PROSITE; PS51710; G_OBG; 1.
PROSITE; PS00905; GTP1_OBG; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Direct protein sequencing; GTP-binding;
Hydrolase; Magnesium; Metal-binding; Nucleotide-binding;
Reference proteome.
CHAIN 1 354 GTPase Obg/CgtA.
/FTId=PRO_0000385810.
DOMAIN 160 328 OBG-type G. {ECO:0000255|HAMAP-
Rule:MF_01454}.
NP_BIND 166 173 GTP. {ECO:0000255|HAMAP-Rule:MF_01454}.
NP_BIND 191 195 GTP. {ECO:0000255|HAMAP-Rule:MF_01454}.
NP_BIND 213 216 GTP. {ECO:0000255|HAMAP-Rule:MF_01454}.
NP_BIND 280 283 GTP. {ECO:0000255|HAMAP-Rule:MF_01454}.
NP_BIND 309 311 GTP. {ECO:0000255|HAMAP-Rule:MF_01454}.
METAL 173 173 Magnesium. {ECO:0000255|HAMAP-
Rule:MF_01454}.
METAL 193 193 Magnesium. {ECO:0000255|HAMAP-
Rule:MF_01454}.
MUTAGEN 80 80 G->E: Grow slowly at 23 degrees Celsius,
die at 37 degrees Celsius; decrease in
50S ribosomal subunits at both
temperatures, partial cell division
arrest at 37 degrees Celsius.
{ECO:0000269|PubMed:15554976}.
MUTAGEN 168 168 P->G: Grows like wild-type at 30 degrees
Celsius. {ECO:0000269|PubMed:15554976}.
MUTAGEN 168 168 P->R: Grows poorly at 30 degrees Celsius,
slightly cold-sensitive.
{ECO:0000269|PubMed:15554976}.
MUTAGEN 168 168 P->V: Grows like wild-type at 30 degrees
Celsius, slightly cold-sensitive. Slight
reduction in affinity for GDP, slight
increase in GDP exchange rates.
{ECO:0000269|PubMed:15554976}.
MUTAGEN 171 173 GKS->AAA: Unable to support growth.
{ECO:0000269|PubMed:14702318}.
MUTAGEN 171 171 G->A: Unable to support growth.
{ECO:0000269|PubMed:15554976}.
MUTAGEN 172 172 K->N: Unable to support growth.
{ECO:0000269|PubMed:15554976}.
MUTAGEN 173 173 S->N: Unable to support growth. Does not
bind GTP, decreased binding of GDP.
{ECO:0000269|PubMed:15554976}.
MUTAGEN 192 192 T->A: Supports growth. 2.5-fold and 7-
fold reduced binding to GDP and GTP
respectively. No change in the GTP
hydrolysis rate.
{ECO:0000269|PubMed:11251813}.
MUTAGEN 193 193 T->A: Unable to support growth. 5-fold
and 22-fold reduced binding to GDP and
GTP respectively. 10-fold decreased GTP
hydrolysis rate.
{ECO:0000269|PubMed:11251813}.
MUTAGEN 213 216 DIPG->AIPA: Unable to support growth.
{ECO:0000269|PubMed:15554976}.
MUTAGEN 280 280 N->K,Y: Grows poorly at 30 degrees
Celsius. {ECO:0000269|PubMed:15554976}.
MUTAGEN 348 354 Missing: No effect. Replacment of this
region with an epitope tag (3HA)
decreases growth rate.
{ECO:0000269|PubMed:14702318}.
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


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