OBG_ECOLI
ID OBG_ECOLI Reviewed; 390 AA.
AC P42641; Q2M929;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=GTPase ObgE/CgtA {ECO:0000255|HAMAP-Rule:MF_01454};
DE EC=3.6.5.- {ECO:0000255|HAMAP-Rule:MF_01454, ECO:0000269|PubMed:11555285};
DE AltName: Full=GTP-binding protein Obg {ECO:0000255|HAMAP-Rule:MF_01454};
GN Name=obgE {ECO:0000303|PubMed:11555285};
GN Synonyms=cgtA {ECO:0000303|PubMed:12402086},
GN obg {ECO:0000255|HAMAP-Rule:MF_01454}, yhbZ;
GN OrderedLocusNames=b3183, JW3150;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [3]
RP DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9743119; DOI=10.1038/nbt0998-851;
RA Arigoni F., Talabot F., Peitsch M.C., Edgerton M.D., Meldrum E., Allet E.,
RA Fish R., Jamotte T., Curchod M.-L., Loferer H.;
RT "A genome-based approach for the identification of essential bacterial
RT genes.";
RL Nat. Biotechnol. 16:851-856(1998).
RN [4]
RP FUNCTION IN CHROMOSOME PARTITIONING, GTPASE-ACTIVITY, DNA-BINDING, SUBUNIT,
RP POSSIBLE COFACTOR, AND MUTAGENESIS OF GLY-80 AND ASP-85.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=11555285; DOI=10.1046/j.1365-2958.2001.02574.x;
RA Kobayashi G., Moriya S., Wada C.;
RT "Deficiency of essential GTP-binding protein ObgE in Escherichia coli
RT inhibits chromosome partition.";
RL Mol. Microbiol. 41:1037-1051(2001).
RN [5]
RP FUNCTION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=12402086; DOI=10.1007/s00284-002-3713-x;
RA Dutkiewicz R., Slominska M., Wegrzyn G., Czyz A.;
RT "Overexpression of the cgtA (yhbZ, obgE) gene, coding for an essential GTP-
RT binding protein, impairs the regulation of chromosomal functions in
RT Escherichia coli.";
RL Curr. Microbiol. 45:440-445(2002).
RN [6]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=11976298; DOI=10.1128/jb.184.10.2692-2698.2002;
RA Tan J., Jakob U., Bardwell J.C.A.;
RT "Overexpression of two different GTPases rescues a null mutation in a heat-
RT induced rRNA methyltransferase.";
RL J. Bacteriol. 184:2692-2698(2002).
RN [7]
RP FUNCTION, AND INDUCTION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
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 [8]
RP FUNCTION IN PLASMID REPLICATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=12826057; DOI=10.1016/s0147-619x(03)00021-0;
RA Ulanowska K., Sikora A., Wegrzyn G., Czyz A.;
RT "Role of the cgtA gene function in DNA replication of extrachromosomal
RT elements in Escherichia coli.";
RL Plasmid 50:45-52(2003).
RN [9]
RP SUBCELLULAR LOCATION, RIBOSOMAL-ASSOCIATION, BIOPHYSICOCHEMICAL PROPERTIES,
RP AND INTERACTION WITH SPOT.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=15292126; DOI=10.1128/jb.186.16.5249-5257.2004;
RA Wout P., Pu K., Sullivan S.M., Reese V., Zhou S., Lin B., Maddock J.R.;
RT "The Escherichia coli GTPase CgtAE cofractionates with the 50S ribosomal
RT subunit and interacts with SpoT, a ppGpp synthetase/hydrolase.";
RL J. Bacteriol. 186:5249-5257(2004).
RN [10]
RP FUNCTION IN RIBOSOME BIOGENESIS, RRNA-BINDING, INDUCTION, ASSOCIATION WITH
RP 30S AND 50S RIBOSOMAL SUBUNITS, AND MUTAGENESIS OF SER-314.
RC STRAIN=K12;
RX PubMed=15836769; DOI=10.1111/j.1365-2443.2005.00851.x;
RA Sato A., Kobayashi G., Hayashi H., Yoshida H., Wada A., Maeda M.,
RA Hiraga S., Takeyasu K., Wada C.;
RT "The GTP binding protein Obg homolog ObgE is involved in ribosome
RT maturation.";
RL Genes Cells 10:393-408(2005).
RN [11]
RP MUTAGENESIS OF PRO-168, AND POSSIBLE FUNCTION IN REPLICATION FORK
RP STABILITY.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15721258; DOI=10.1016/j.molcel.2005.01.012;
RA Foti J.J., Schienda J., Sutera V.A. Jr., Lovett S.T.;
RT "A bacterial G protein-mediated response to replication arrest.";
RL Mol. Cell 17:549-560(2005).
RN [12]
RP FUNCTION IN DNAA REGULATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=16518617; DOI=10.1007/s00203-006-0099-3;
RA Sikora A.E., Zielke R., Wegrzyn A., Wegrzyn G.;
RT "DNA replication defect in the Escherichia coli cgtA(ts) mutant arising
RT from reduced DnaA levels.";
RL Arch. Microbiol. 185:340-347(2006).
RN [13]
RP FUNCTION IN LATE STAGES OF 50S RIBOSOMAL SUBUNIT ASSEMBLY.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=16980477; DOI=10.1128/jb.00444-06;
RA Jiang M., Datta K., Walker A., Strahler J., Bagamasbad P., Andrews P.C.,
RA Maddock J.R.;
RT "The Escherichia coli GTPase CgtAE is involved in late steps of large
RT ribosome assembly.";
RL J. Bacteriol. 188:6757-6770(2006).
RN [14]
RP FUNCTION UNDER AMINO ACID STARVATION, AND ASSOCIATION WITH SPOT.
RC STRAIN=K12;
RX PubMed=17616600; DOI=10.1128/jb.00315-07;
RA Jiang M., Sullivan S.M., Wout P.K., Maddock J.R.;
RT "G-protein control of the ribosome-associated stress response protein
RT SpoT.";
RL J. Bacteriol. 189:6140-6147(2007).
RN [15]
RP FUNCTION IN CHROMOSOME SEGREGATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=17578452; DOI=10.1111/j.1365-2958.2007.05811.x;
RA Foti J.J., Persky N.S., Ferullo D.J., Lovett S.T.;
RT "Chromosome segregation control by Escherichia coli ObgE GTPase.";
RL Mol. Microbiol. 65:569-581(2007).
RN [16]
RP FUNCTION IN STRINGENT RESPONSE, PPGPP-BINDING, AND POSSIBLE ROLE IN
RP INHIBITION OF DNA REPLICATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=19555460; DOI=10.1111/j.1365-2958.2009.06767.x;
RA Persky N.S., Ferullo D.J., Cooper D.L., Moore H.R., Lovett S.T.;
RT "The ObgE/CgtA GTPase influences the stringent response to amino acid
RT starvation in Escherichia coli.";
RL Mol. Microbiol. 73:253-266(2009).
RN [17]
RP FUNCTION, DOMAIN, AND MUTAGENESIS OF LEU-159; GLY-163; PRO-168; GLY-216 AND
RP ARG-237.
RX PubMed=22863262; DOI=10.1111/j.1742-4658.2012.08731.x;
RA Kint C.I., Verstraeten N., Wens I., Liebens V.R., Hofkens J., Versees W.,
RA Fauvart M., Michiels J.;
RT "The Escherichia coli GTPase ObgE modulates hydroxyl radical levels in
RT response to DNA replication fork arrest.";
RL FEBS J. 279:3692-3704(2012).
RN [18]
RP FUNCTION IN PERSISTENCE, AND MUTAGENESIS OF GLY-93; GLY-166; PRO-168;
RP SER-173; THR-193 AND GLY-216.
RC STRAIN=K12 / BW25113, and TOP10;
RX PubMed=26051177; DOI=10.1016/j.molcel.2015.05.011;
RA Verstraeten N., Knapen W.J., Kint C.I., Liebens V., Van den Bergh B.,
RA Dewachter L., Michiels J.E., Fu Q., David C.C., Fierro A.C., Marchal K.,
RA Beirlant J., Versees W., Hofkens J., Jansen M., Fauvart M., Michiels J.;
RT "Obg and membrane depolarization are part of a microbial bet-hedging
RT strategy that leads to antibiotic tolerance.";
RL Mol. Cell 59:9-21(2015).
RN [19]
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 [20]
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).
RN [21]
RP STRUCTURE BY ELECTRON MICROSCOPY (5.5 ANGSTROMS) IN COMPLEX WITH 50S
RP RIBOSOMAL SUBUNIT AND GMP-PNP, FUNCTION, DOMAIN, RRNA-BINDING, AND
RP MUTAGENESIS OF 27-LYS--LYS-31; 76-ARG--ARG-82 AND 136-ARG--ARG-139.
RC STRAIN=K12 / DH5-alpha;
RX PubMed=24844575; DOI=10.1371/journal.pbio.1001866;
RA Feng B., Mandava C.S., Guo Q., Wang J., Cao W., Li N., Zhang Y., Zhang Y.,
RA Wang Z., Wu J., Sanyal S., Lei J., Gao N.;
RT "Structural and functional insights into the mode of action of a
RT universally conserved Obg GTPase.";
RL PLoS Biol. 12:E1001866-E1001866(2014).
CC -!- FUNCTION: An abundant, essential GTPase which binds GTP, GDP and ppGpp
CC with moderate affinity. Has high guanosine nucleotide exchange rate
CC constants for GTP and GDP, and a relatively low GTP hydrolysis rate
CC stimulated by the 50S ribosomal subunit. It is estimated there are
CC 34000 molecules in log-phase cells and 5600 molecules in stationary-
CC phase cells. Required for chromosome segregation. Plays a role in the
CC stringent response, perhaps by sequestering 50S ribosomal subunits and
CC decreasing protein synthesis (PubMed:19555460), and a non-essential
CC role in the late steps of ribosome biogenesis, perhaps acting as a
CC checkpoint for correct 50S subunit synthesis (Probable)
CC (PubMed:24844575). Overexpression increases bacterial persistence (in
CC exponential and stationary phase) in response to antibiotics
CC (PubMed:26051177). Cells expressing high levels of Obg are more likely
CC to form persister cells upon antibiotic exposure; this requires
CC alarmone (p)ppGpp and acts via induced HokB, depolarizing cells, which
CC probably reduces metabolic activity and induces persistence
CC (PubMed:26051177). The persister phenotype can be separated from the
CC essential phenotype (PubMed:26051177). {ECO:0000269|PubMed:11555285,
CC ECO:0000269|PubMed:11976298, ECO:0000269|PubMed:12402086,
CC ECO:0000269|PubMed:15836769, ECO:0000269|PubMed:16980477,
CC ECO:0000269|PubMed:17578452, ECO:0000269|PubMed:17616600,
CC ECO:0000269|PubMed:19555460, ECO:0000269|PubMed:26051177,
CC ECO:0000305|PubMed:24844575}.
CC -!- FUNCTION: Required for correct chromosome partitioning; in temperature-
CC sensitive (ts) mutant nucleoids do not partition but remain in the
CC middle of cell, cells elongate but do not divide. Overexpression
CC protects cells against UV damage. Ts mutants have impaired plasmid and
CC lamdba phage replication, possibly via effects on DnaA
CC (PubMed:12826057). Regulates DnaA levels. Genetic interactions of Val-
CC 168 and a C-terminal insertion mutant with the double-strand break
CC repair factors recA and recBCD, and with seqA suggests that ObgE,
CC either directly or indirectly, promotes replication fork stability
CC (PubMed:15721258). May protect replication forks from stress induced by
CC toxic levels of hydroxyl radicals (PubMed:22863262). Initiation of DNA
CC replication continues in ObgE-depleted cells.
CC {ECO:0000269|PubMed:11555285, ECO:0000269|PubMed:12402086,
CC ECO:0000269|PubMed:12826057, ECO:0000269|PubMed:12855728,
CC ECO:0000269|PubMed:15721258, ECO:0000269|PubMed:16518617,
CC ECO:0000269|PubMed:17578452, ECO:0000269|PubMed:22863262}.
CC -!- FUNCTION: Binds to pre-50S ribosomal subunits in a salt-dependent
CC manner. Acts as a ribosome anti-association factor; guanosine
CC nucleotides stimulate ObgE 50S subunit binding and also ObgE-mediated
CC 70S ribosome dissociation (GDPEYIPE: Almost abolishes 50S subunit binding."
FT /evidence="ECO:0000269|PubMed:24844575"
FT MUTAGEN 76..82
FT /note="RDCTGKR->GDCTGKG: Slight reduction in 50S subunit
FT binding."
FT /evidence="ECO:0000269|PubMed:24844575"
FT MUTAGEN 80
FT /note="G->E: Temperature-sensitive for growth at 42 degrees
FT Celsius, defects in chromosome partitioning; when
FT associated with N-85."
FT /evidence="ECO:0000269|PubMed:11555285"
FT MUTAGEN 85
FT /note="D->N: Temperature-sensitive for growth at 42 degrees
FT Celsius, defects in chromosome partitioning; when
FT associated with E-80."
FT /evidence="ECO:0000269|PubMed:11555285"
FT MUTAGEN 93
FT /note="G->D: No effect on persister cell formation upon
FT overexpression."
FT /evidence="ECO:0000269|PubMed:26051177"
FT MUTAGEN 136..139
FT /note="RTPR->GTPG: Almost abolishes 50S subunit binding."
FT /evidence="ECO:0000269|PubMed:24844575"
FT MUTAGEN 159
FT /note="L->Q: Increased sensitivity to HU upon
FT overexpression, supports normal growth, no effect in
FT mazEF/relBE or tonB deletions."
FT /evidence="ECO:0000269|PubMed:22863262"
FT MUTAGEN 163
FT /note="G->V: Increased sensitivity to HU upon
FT overexpression, supports normal growth, no effect in
FT mazEF/relBE or tonB deletions."
FT /evidence="ECO:0000269|PubMed:22863262"
FT MUTAGEN 166
FT /note="G->V: No increase in persister cells upon
FT overexpression, does not induce hokB expression, supports
FT normal growth."
FT /evidence="ECO:0000269|PubMed:26051177"
FT MUTAGEN 168
FT /note="P->V: Increased sensitivity to HU upon
FT overexpression, supports normal growth, no effect in
FT mazEF/relBE or tonB deletions. No effect on persister cell
FT formation upon overexpression."
FT /evidence="ECO:0000269|PubMed:15721258,
FT ECO:0000269|PubMed:22863262, ECO:0000269|PubMed:26051177"
FT MUTAGEN 173
FT /note="S->N: No effect on persister cell formation upon
FT overexpression."
FT /evidence="ECO:0000269|PubMed:26051177"
FT MUTAGEN 193
FT /note="T->A: No effect on persister cell formation upon
FT overexpression."
FT /evidence="ECO:0000269|PubMed:26051177"
FT MUTAGEN 216
FT /note="G->A: Increased sensitivity to HU upon
FT overexpression, supports normal growth, no effect in
FT mazEF/relBE or tonB deletions. No effect on persister cell
FT formation upon overexpression."
FT /evidence="ECO:0000269|PubMed:22863262,
FT ECO:0000269|PubMed:26051177"
FT MUTAGEN 237
FT /note="R->C: Increased sensitivity to HU upon
FT overexpression, supports normal growth, no effect in
FT mazEF/relBE or tonB deletions."
FT /evidence="ECO:0000269|PubMed:22863262"
FT MUTAGEN 314
FT /note="S->P: Severe growth defect at 42 degrees Celsius.
FT Decreased levels of some ribosomal proteins, altered PTMs
FT of others."
FT /evidence="ECO:0000269|PubMed:15836769"
FT STRAND 2..12
FT /evidence="ECO:0007829|PDB:5M04"
FT STRAND 27..29
FT /evidence="ECO:0007829|PDB:5M04"
FT STRAND 45..49
FT /evidence="ECO:0007829|PDB:5M04"
FT HELIX 57..60
FT /evidence="ECO:0007829|PDB:5M04"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:5M04"
FT TURN 75..77
FT /evidence="ECO:0007829|PDB:5M04"
FT STRAND 86..90
FT /evidence="ECO:0007829|PDB:5M04"
FT STRAND 94..98
FT /evidence="ECO:0007829|PDB:5M04"
FT TURN 99..101
FT /evidence="ECO:0007829|PDB:5M04"
FT STRAND 104..108
FT /evidence="ECO:0007829|PDB:5M04"
FT STRAND 114..118
FT /evidence="ECO:0007829|PDB:5M04"
FT HELIX 127..130
FT /evidence="ECO:0007829|PDB:5M04"
FT TURN 133..135
FT /evidence="ECO:0007829|PDB:7BL5"
FT STRAND 149..157
FT /evidence="ECO:0007829|PDB:5M04"
FT STRAND 161..165
FT /evidence="ECO:0007829|PDB:5M04"
FT HELIX 172..179
FT /evidence="ECO:0007829|PDB:5M04"
FT STRAND 185..188
FT /evidence="ECO:0007829|PDB:5M04"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:5M04"
FT STRAND 198..204
FT /evidence="ECO:0007829|PDB:5M04"
FT STRAND 207..213
FT /evidence="ECO:0007829|PDB:5M04"
FT HELIX 214..218
FT /evidence="ECO:0007829|PDB:5M04"
FT STRAND 221..223
FT /evidence="ECO:0007829|PDB:5M04"
FT HELIX 226..233
FT /evidence="ECO:0007829|PDB:5M04"
FT HELIX 234..237
FT /evidence="ECO:0007829|PDB:5M04"
FT STRAND 240..248
FT /evidence="ECO:0007829|PDB:5M04"
FT TURN 250..252
FT /evidence="ECO:0007829|PDB:7BL4"
FT HELIX 255..269
FT /evidence="ECO:0007829|PDB:5M04"
FT HELIX 271..274
FT /evidence="ECO:0007829|PDB:5M04"
FT STRAND 278..283
FT /evidence="ECO:0007829|PDB:5M04"
FT HELIX 285..287
FT /evidence="ECO:0007829|PDB:5M04"
FT HELIX 290..303
FT /evidence="ECO:0007829|PDB:5M04"
FT TURN 315..317
FT /evidence="ECO:0007829|PDB:5M04"
FT HELIX 321..334
FT /evidence="ECO:0007829|PDB:5M04"
SQ SEQUENCE 390 AA; 43286 MW; 3A6EBF56F24B7C47 CRC64;
MKFVDEASIL VVAGDGGNGC VSFRREKYIP KGGPDGGDGG DGGDVWMEAD ENLNTLIDYR
FEKSFRAERG QNGASRDCTG KRGKDVTIKV PVGTRVIDQG TGETMGDMTK HGQRLLVAKG
GWHGLGNTRF KSSVNRTPRQ KTNGTPGDKR ELLLELMLLA DVGMLGMPNA GKSTFIRAVS
AAKPKVADYP FTTLVPSLGV VRMDNEKSFV VADIPGLIEG AAEGAGLGIR FLKHLERCRV
LLHLIDIDPI DGTDPVENAR IIISELEKYS QDLATKPRWL VFNKIDLLDK VEAEEKAKAI
AEALGWEDKY YLISAASGLG VKDLCWDVMT FIIENPVVQA EEAKQPEKVE FMWDDYHRQQ
LEEIAEEDDE DWDDDWDEDD EEGVEFIYKR