OBG_THET8
ID OBG_THET8 Reviewed; 416 AA.
AC Q5SHE9; Q7X493;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=GTPase Obg {ECO:0000255|HAMAP-Rule:MF_01454};
DE EC=3.6.5.- {ECO:0000255|HAMAP-Rule:MF_01454};
DE AltName: Full=GTP-binding protein Obg {ECO:0000255|HAMAP-Rule:MF_01454};
DE AltName: Full=TT1381;
GN Name=obg {ECO:0000255|HAMAP-Rule:MF_01454}; OrderedLocusNames=TTHA1781;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Kukimoto-Niino M., Murayama K., Terada T., Kuramitsu S., Shirouzu M.,
RA Yokoyama S.;
RT "Crystal structure of the conserved protein TT1381 from Thermus
RT thermophilus HB8.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.07 ANGSTROMS), AND SUBUNIT.
RX PubMed=15019792; DOI=10.1016/j.jmb.2004.01.047;
RA Kukimoto-Niino M., Murayama K., Inoue M., Terada T., Tame J.R.,
RA Kuramitsu S., Shirouzu M., Yokoyama S.;
RT "Crystal structure of the GTP-binding protein Obg from Thermus thermophilus
RT HB8.";
RL J. Mol. Biol. 337:761-770(2004).
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.
CC {ECO:0000255|HAMAP-Rule:MF_01454}.
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 ECO:0000269|PubMed:15019792}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01454}.
CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase
CC superfamily. OBG GTPase family. {ECO:0000255|HAMAP-Rule:MF_01454}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB110607; BAC76805.2; -; Genomic_DNA.
DR EMBL; AP008226; BAD71604.1; -; Genomic_DNA.
DR RefSeq; WP_011228913.1; NC_006461.1.
DR RefSeq; YP_145047.1; NC_006461.1.
DR PDB; 1UDX; X-ray; 2.07 A; A=1-416.
DR PDBsum; 1UDX; -.
DR AlphaFoldDB; Q5SHE9; -.
DR SMR; Q5SHE9; -.
DR STRING; 300852.55773163; -.
DR EnsemblBacteria; BAD71604; BAD71604; BAD71604.
DR GeneID; 3169474; -.
DR KEGG; ttj:TTHA1781; -.
DR PATRIC; fig|300852.9.peg.1751; -.
DR eggNOG; COG0536; Bacteria.
DR HOGENOM; CLU_011747_2_1_0; -.
DR OMA; VVFDWEP; -.
DR PhylomeDB; Q5SHE9; -.
DR EvolutionaryTrace; Q5SHE9; -.
DR Proteomes; UP000000532; 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; 3.30.300.350; -; 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 InterPro; IPR005225; Small_GTP-bd_dom.
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 TIGRFAMs; TIGR00231; small_GTP; 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 3D-structure; Cytoplasm; GTP-binding; Hydrolase; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..416
FT /note="GTPase Obg"
FT /id="PRO_0000386361"
FT DOMAIN 1..157
FT /note="Obg"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01231"
FT DOMAIN 158..324
FT /note="OBG-type G"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT DOMAIN 336..414
FT /note="OCT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01229"
FT REGION 25..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 62..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..77
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 164..171
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT BINDING 171
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT BINDING 189..193
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT BINDING 191
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT BINDING 211..214
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT BINDING 277..280
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT BINDING 305..307
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT STRAND 4..11
FT /evidence="ECO:0007829|PDB:1UDX"
FT STRAND 44..48
FT /evidence="ECO:0007829|PDB:1UDX"
FT TURN 73..75
FT /evidence="ECO:0007829|PDB:1UDX"
FT STRAND 84..88
FT /evidence="ECO:0007829|PDB:1UDX"
FT STRAND 90..96
FT /evidence="ECO:0007829|PDB:1UDX"
FT TURN 97..99
FT /evidence="ECO:0007829|PDB:1UDX"
FT STRAND 102..106
FT /evidence="ECO:0007829|PDB:1UDX"
FT STRAND 112..116
FT /evidence="ECO:0007829|PDB:1UDX"
FT HELIX 125..128
FT /evidence="ECO:0007829|PDB:1UDX"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:1UDX"
FT STRAND 147..154
FT /evidence="ECO:0007829|PDB:1UDX"
FT STRAND 159..163
FT /evidence="ECO:0007829|PDB:1UDX"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:1UDX"
FT HELIX 170..177
FT /evidence="ECO:0007829|PDB:1UDX"
FT STRAND 195..200
FT /evidence="ECO:0007829|PDB:1UDX"
FT STRAND 202..204
FT /evidence="ECO:0007829|PDB:1UDX"
FT STRAND 206..211
FT /evidence="ECO:0007829|PDB:1UDX"
FT HELIX 219..221
FT /evidence="ECO:0007829|PDB:1UDX"
FT HELIX 227..233
FT /evidence="ECO:0007829|PDB:1UDX"
FT STRAND 235..244
FT /evidence="ECO:0007829|PDB:1UDX"
FT HELIX 249..263
FT /evidence="ECO:0007829|PDB:1UDX"
FT HELIX 265..269
FT /evidence="ECO:0007829|PDB:1UDX"
FT STRAND 272..277
FT /evidence="ECO:0007829|PDB:1UDX"
FT HELIX 284..295
FT /evidence="ECO:0007829|PDB:1UDX"
FT TURN 296..298
FT /evidence="ECO:0007829|PDB:1UDX"
FT STRAND 301..303
FT /evidence="ECO:0007829|PDB:1UDX"
FT TURN 306..308
FT /evidence="ECO:0007829|PDB:1UDX"
FT HELIX 312..324
FT /evidence="ECO:0007829|PDB:1UDX"
FT STRAND 345..350
FT /evidence="ECO:0007829|PDB:1UDX"
FT STRAND 353..357
FT /evidence="ECO:0007829|PDB:1UDX"
FT HELIX 359..365
FT /evidence="ECO:0007829|PDB:1UDX"
FT STRAND 368..370
FT /evidence="ECO:0007829|PDB:1UDX"
FT HELIX 373..375
FT /evidence="ECO:0007829|PDB:1UDX"
FT HELIX 376..385
FT /evidence="ECO:0007829|PDB:1UDX"
FT HELIX 388..393
FT /evidence="ECO:0007829|PDB:1UDX"
FT TURN 394..396
FT /evidence="ECO:0007829|PDB:1UDX"
FT STRAND 402..405
FT /evidence="ECO:0007829|PDB:1UDX"
FT STRAND 408..411
FT /evidence="ECO:0007829|PDB:1UDX"
SQ SEQUENCE 416 AA; 44498 MW; 10969D7E66C4E21E CRC64;
MFQDVLVITV AAGRGGDGAV SFRREKFVPK GGPDGGDGGR GGSVYLRARG SVDSLSRLSK
RTYKAEDGEH GRGSQQHGRG GEDLVIEVPR GTRVFDADTG ELLADLTEEG QTVLVARGGA
GGRGNMHFVS PTRQAPRFAE AGEEGEKRRL RLELMLIADV GLVGYPNAGK SSLLAAMTRA
HPKIAPYPFT TLSPNLGVVE VSEEERFTLA DIPGIIEGAS EGKGLGLEFL RHIARTRVLL
YVLDAADEPL KTLETLRKEV GAYDPALLRR PSLVALNKVD LLEEEAVKAL ADALAREGLA
VLPVSALTGA GLPALKEALH ALVRSTPPPE MPKPVPRKEV QAGVEVVPVA EGVYEVRAPE
VERYLARIKG DLMEAAGYLQ EVFRRQGVEA ALRAKGVRAG DLVRIGGLEF EYIPEV
