OBG_MYCTU
ID OBG_MYCTU Reviewed; 479 AA.
AC P9WMT1; L0TCC8; P71909; Q7D750;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 48.
DE RecName: Full=GTPase Obg {ECO:0000255|HAMAP-Rule:MF_01454};
DE EC=3.6.5.- {ECO:0000255|HAMAP-Rule:MF_01454, ECO:0000269|PubMed:22578863};
DE AltName: Full=GTP-binding protein Obg {ECO:0000255|HAMAP-Rule:MF_01454};
GN Name=obg {ECO:0000255|HAMAP-Rule:MF_01454}; OrderedLocusNames=Rv2440c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP FUNCTION AS A GTPASE, MUTAGENESIS OF ASP-212, AND GTP-BINDING.
RC STRAIN=H37Rv;
RX PubMed=22578863; DOI=10.1016/j.enzmictec.2007.08.008;
RA Meena L.S., Chopra P., Bedwal R.S., Singh Y.;
RT "Cloning and characterization of GTP-binding proteins of Mycobacterium
RT tuberculosis H37Rv.";
RL Enzyme Microb. Technol. 42:138-144(2008).
RN [3]
RP FUNCTION AS A GTPASE, COFACTOR, INTERACTION WITH RSBW, SUBCELLULAR
RP LOCATION, INDUCTION, AUTOPHOSPHORYLATION, AND GTP-BINDING.
RC STRAIN=H37Rv;
RX PubMed=21352546; DOI=10.1186/1471-2180-11-43;
RA Sasindran S.J., Saikolappan S., Scofield V.L., Dhandayuthapani S.;
RT "Biochemical and physiological characterization of the GTP-binding protein
RT Obg of Mycobacterium tuberculosis.";
RL BMC Microbiol. 11:43-43(2011).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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 (By similarity).
CC GTPase activity is not inhibited by ATP or GDP. Overexpression
CC decreases cell growth starting in late log phase and continuing into
CC stationary phase (PubMed:21352546). {ECO:0000255|HAMAP-Rule:MF_01454,
CC ECO:0000269|PubMed:21352546}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01454,
CC ECO:0000269|PubMed:21352546};
CC -!- SUBUNIT: Monomer (By similarity). Interacts with anti-sigma-F factor
CC RsbW, was not seen to interact with RelA (PubMed:21352546).
CC {ECO:0000255|HAMAP-Rule:MF_01454, ECO:0000269|PubMed:21352546}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01454,
CC ECO:0000269|PubMed:22578863}. Cell membrane
CC {ECO:0000269|PubMed:21352546}. Note=Found to be entirely in cytoplasm
CC (PubMed:22578863). Also found to be 90% associated with cell membrane,
CC 10% in soluble extract. Associated with 30S and 50S ribosome subunits
CC as well as 70S ribosomes (PubMed:21352546).
CC {ECO:0000269|PubMed:21352546, ECO:0000269|PubMed:22578863}.
CC -!- INDUCTION: Expression increases about 5-fold from early log phase to
CC stationary phase, dropping in late stationary phase (at protein level).
CC {ECO:0000269|PubMed:21352546}.
CC -!- PTM: Autophosphorylates using GTP but not ATP; autophosphorylation
CC requires Mg(2+), is inhibited by cold GTP and to a lesser extent GDP
CC but not by ATP. {ECO:0000269|PubMed:21352546}.
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; AL123456; CCP45233.1; -; Genomic_DNA.
DR PIR; F70680; F70680.
DR RefSeq; NP_216956.1; NC_000962.3.
DR RefSeq; WP_003901405.1; NZ_NVQJ01000024.1.
DR AlphaFoldDB; P9WMT1; -.
DR SMR; P9WMT1; -.
DR STRING; 83332.Rv2440c; -.
DR PaxDb; P9WMT1; -.
DR DNASU; 885900; -.
DR GeneID; 45426430; -.
DR GeneID; 885900; -.
DR KEGG; mtu:Rv2440c; -.
DR TubercuList; Rv2440c; -.
DR eggNOG; COG0536; Bacteria.
DR OMA; VVFDWEP; -.
DR PhylomeDB; P9WMT1; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:MTBBASE.
DR GO; GO:0005840; C:ribosome; IDA:MTBBASE.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IDA:MTBBASE.
DR GO; GO:0000287; F:magnesium ion binding; IDA:MTBBASE.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:MTBBASE.
DR GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-UniRule.
DR CDD; cd01898; Obg; 1.
DR Gene3D; 2.70.210.12; -; 1.
DR Gene3D; 3.30.300.350; -; 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; IPR036346; GTP-bd_prot_GTP1/OBG_C_sf.
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; IPR015349; OCT_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11702; PTHR11702; 1.
DR Pfam; PF09269; DUF1967; 1.
DR Pfam; PF01018; GTP1_OBG; 1.
DR Pfam; PF01926; MMR_HSR1; 1.
DR PRINTS; PR00326; GTP1OBG.
DR SUPFAM; SSF102741; SSF102741; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF82051; SSF82051; 1.
DR TIGRFAMs; TIGR02729; Obg_CgtA; 1.
DR TIGRFAMs; TIGR03595; Obg_CgtA_exten; 1.
DR PROSITE; PS51710; G_OBG; 1.
DR PROSITE; PS00905; GTP1_OBG; 1.
DR PROSITE; PS51883; OBG; 1.
DR PROSITE; PS51881; OCT; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cytoplasm; GTP-binding; Hydrolase; Magnesium; Membrane;
KW Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..479
FT /note="GTPase Obg"
FT /id="PRO_0000386062"
FT DOMAIN 2..159
FT /note="Obg"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01231"
FT DOMAIN 160..340
FT /note="OBG-type G"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT DOMAIN 358..436
FT /note="OCT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01229"
FT REGION 434..479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 453..479
FT /note="Basic and 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 212..215
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT BINDING 292..295
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT BINDING 321..323
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT MUTAGEN 212
FT /note="D->A: No GTPase activity."
FT /evidence="ECO:0000269|PubMed:22578863"
SQ SEQUENCE 479 AA; 50461 MW; CC8D8741D9D40053 CRC64;
MPRFVDRVVI HTRAGSGGNG CASVHREKFK PLGGPDGGNG GRGGSIVFVV DPQVHTLLDF
HFRPHLTAAS GKHGMGNNRD GAAGADLEVK VPEGTVVLDE NGRLLADLVG AGTRFEAAAG
GRGGLGNAAL ASRVRKAPGF ALLGEKGQSR DLTLELKTVA DVGLVGFPSA GKSSLVSAIS
AAKPKIADYP FTTLVPNLGV VSAGEHAFTV ADVPGLIPGA SRGRGLGLDF LRHIERCAVL
VHVVDCATAE PGRDPISDID ALETELACYT PTLQGDAALG DLAARPRAVV LNKIDVPEAR
ELAEFVRDDI AQRGWPVFCV STATRENLQP LIFGLSQMIS DYNAARPVAV PRRPVIRPIP
VDDSGFTVEP DGHGGFVVSG ARPERWIDQT NFDNDEAVGY LADRLARLGV EEELLRLGAR
SGCAVTIGEM TFDWEPQTPA GEPVAMSGRG TDPRLDSNKR VGAAERKAAR SRRREHGDG
