OBG_SALTY
ID OBG_SALTY Reviewed; 390 AA.
AC Q8ZLS5;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 121.
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};
GN Name=obg {ECO:0000255|HAMAP-Rule:MF_01454}; Synonyms=yhbZ;
GN OrderedLocusNames=STM3301;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [2]
RP SUBUNIT, INTERACTION WITH RLUD AND S9, AND GDP- AND GTP-BINDING.
RC STRAIN=FIRN / SL3261;
RX PubMed=17905831; DOI=10.1110/ps.072900907;
RA Lamb H.K., Thompson P., Elliott C., Charles I.G., Richards J., Lockyer M.,
RA Watkins N., Nichols C., Stammers D.K., Bagshaw C.R., Cooper A.,
RA Hawkins A.R.;
RT "Functional analysis of the GTPases EngA and YhbZ encoded by Salmonella
RT typhimurium.";
RL Protein Sci. 16:2391-2402(2007).
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 -!- FUNCTION: Binds GDP with a dissociation constant of 1.7 uM and GTP with
CC a dissociation constant of 6.5 uM.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01454};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=6.5 uM for GTP;
CC KM=1.7 uM for GDP;
CC -!- SUBUNIT: Monomer (By similarity). Binds RluD (AC P65836) as well as the
CC 30S ribosomal subunit protein S9 (PubMed:17905831). {ECO:0000255|HAMAP-
CC Rule:MF_01454, ECO:0000269|PubMed:17905831}.
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}.
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DR EMBL; AE006468; AAL22171.1; -; Genomic_DNA.
DR RefSeq; NP_462212.1; NC_003197.2.
DR RefSeq; WP_000673556.1; NC_003197.2.
DR AlphaFoldDB; Q8ZLS5; -.
DR SMR; Q8ZLS5; -.
DR STRING; 99287.STM3301; -.
DR PaxDb; Q8ZLS5; -.
DR EnsemblBacteria; AAL22171; AAL22171; STM3301.
DR GeneID; 1254824; -.
DR KEGG; stm:STM3301; -.
DR PATRIC; fig|99287.12.peg.3501; -.
DR HOGENOM; CLU_011747_2_0_6; -.
DR OMA; VVFDWEP; -.
DR PhylomeDB; Q8ZLS5; -.
DR BioCyc; SENT99287:STM3301-MON; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
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; GTP-binding; Hydrolase; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..390
FT /note="GTPase Obg"
FT /id="PRO_0000386233"
FT DOMAIN 1..159
FT /note="Obg"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01231"
FT DOMAIN 160..333
FT /note="OBG-type G"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT REGION 127..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..142
FT /note="Polar 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 213..216
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT BINDING 283..286
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT BINDING 314..316
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
SQ SEQUENCE 390 AA; 43104 MW; 002E051A72319920 CRC64;
MKFVDEASIL VVAGDGGNGC VSFRREKYIP KGGPDGGDGG DGGDVWMEAD ENLNTLIDYR
FEKSFRAERG QNGASRDCTG KRGKDVTIKV PVGTRVIDQG TGETMGDMTK HGQRLLVAKG
GWHGLGNTRF KSSVNRTPRQ KTNGTPGDKR DLLLELMLLA DVGMLGMPNA GKSTFIRAVS
AAKPKVADYP FTTLVPSLGV VRMDSEKSFV VADIPGLIEG AAEGAGLGIR FLKHLERCRV
LLHLIDIDPI DGSDPVENAR IIIGELEKYS QDLAAKPRWL VFNKIDLMDK TEAEEKAKAI
AEALGWEGKY YLISAASQLG VKDLCWDVMT FIIENPIAQA EEAKQPEKVE FMWDDYHRQQ
LAEVEEDADD DWDDDWDEDD EEGVEFIYKR
