ID A0A0M4MCW6_9ACTN Unreviewed; 491 AA.
AC A0A0M4MCW6;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=GTPase Obg {ECO:0000256|HAMAP-Rule:MF_01454};
DE EC=3.6.5.- {ECO:0000256|HAMAP-Rule:MF_01454};
DE AltName: Full=GTP-binding protein Obg {ECO:0000256|HAMAP-Rule:MF_01454};
GN Name=obgE {ECO:0000313|EMBL:ALE19349.1};
GN Synonyms=cgtA {ECO:0000313|EMBL:ALE19349.1}, obg
GN {ECO:0000256|HAMAP-Rule:MF_01454, ECO:0000313|EMBL:ALE19349.1}, yhbZ
GN {ECO:0000313|EMBL:ALE19349.1};
GN ORFNames=AL705_07140 {ECO:0000313|EMBL:ALE19349.1}, LC603019_01416
GN {ECO:0000313|EMBL:VHO01484.1};
OS Lawsonella clevelandensis.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Lawsonellaceae;
OC Lawsonella.
OX NCBI_TaxID=1528099 {ECO:0000313|EMBL:ALE19349.1, ECO:0000313|Proteomes:UP000068137};
RN [1] {ECO:0000313|EMBL:ALE19349.1, ECO:0000313|Proteomes:UP000068137}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=X1698 {ECO:0000313|EMBL:ALE19349.1,
RC ECO:0000313|Proteomes:UP000068137};
RX PubMed=26659691;
RA Nicholson A.C., Bell M., Humrighouse B.W., McQuiston J.R.;
RT "Complete Genome Sequences for Two Strains of a Novel Fastidious, Partially
RT Acid-Fast, Gram-Positive Corynebacterineae Bacterium, Derived from Human
RT Clinical Samples.";
RL Genome Announc. 3:e01462-15(2015).
RN [2] {ECO:0000313|EMBL:ALE19349.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=X1698 {ECO:0000313|EMBL:ALE19349.1};
RX PubMed=27130323; DOI=10.1099/ijsem.0.001122;
RA Bell M.E., Bernard K.A., Harrington S.M., Patel N.B., Tucker T.A.,
RA Metcalfe M.G., McQuiston J.R.;
RT "Lawsonella clevelandensis gen. nov., sp. nov., a new member of the
RT suborder Corynebacterineae isolated from human abscesses.";
RL Int. J. Syst. Evol. Microbiol. 66:2929-2935(2016).
RN [3] {ECO:0000313|EMBL:VHO01484.1, ECO:0000313|Proteomes:UP000324288}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=USB-603019 {ECO:0000313|EMBL:VHO01484.1};
RA Seth-Smith MB H., Seth-Smith H.;
RL Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-Rule:MF_01454}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|HAMAP-Rule:MF_01454};
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_01454}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01454}.
CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase
CC superfamily. OBG GTPase family. {ECO:0000256|ARBA:ARBA00007699,
CC ECO:0000256|HAMAP-Rule:MF_01454}.
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DR EMBL; CP012390; ALE19349.1; -; Genomic_DNA.
DR EMBL; LR584267; VHO01484.1; -; Genomic_DNA.
DR RefSeq; WP_053962418.1; NZ_LR584267.1.
DR AlphaFoldDB; A0A0M4MCW6; -.
DR STRING; 1528099.AL705_07140; -.
DR GeneID; 84895316; -.
DR KEGG; cbq:AL705_07140; -.
DR PATRIC; fig|1528099.3.peg.1405; -.
DR OrthoDB; 9807318at2; -.
DR Proteomes; UP000068137; Chromosome.
DR Proteomes; UP000324288; Chromosome 1.
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; 3.30.300.350; GTP-binding protein OBG, C-terminal domain; 1.
DR Gene3D; 2.70.210.12; GTP1/OBG domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 NCBIfam; TIGR02729; Obg_CgtA; 1.
DR NCBIfam; TIGR03595; Obg_CgtA_exten; 1.
DR PANTHER; PTHR11702; DEVELOPMENTALLY REGULATED GTP-BINDING PROTEIN-RELATED; 1.
DR PANTHER; PTHR11702:SF31; MITOCHONDRIAL RIBOSOME-ASSOCIATED GTPASE 2; 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; Obg GTP-binding protein C-terminal domain; 1.
DR SUPFAM; SSF82051; Obg GTP-binding protein N-terminal domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51710; G_OBG; 1.
DR PROSITE; PS00905; GTP1_OBG; 1.
DR PROSITE; PS51883; OBG; 1.
DR PROSITE; PS51881; OCT; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01454};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW Rule:MF_01454}; Hydrolase {ECO:0000256|HAMAP-Rule:MF_01454};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01454};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01454};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01454}; Reference proteome {ECO:0000313|Proteomes:UP000068137}.
FT DOMAIN 2..159
FT /note="Obg"
FT /evidence="ECO:0000259|PROSITE:PS51883"
FT DOMAIN 160..340
FT /note="OBG-type G"
FT /evidence="ECO:0000259|PROSITE:PS51710"
FT DOMAIN 358..438
FT /note="OCT"
FT /evidence="ECO:0000259|PROSITE:PS51881"
FT REGION 443..491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 166..173
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01454"
FT BINDING 173
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01454"
FT BINDING 191..195
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01454"
FT BINDING 193
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01454"
FT BINDING 212..215
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01454"
FT BINDING 292..295
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01454"
FT BINDING 321..323
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01454"
SQ SEQUENCE 491 AA; 51877 MW; D51A650A10276ABD CRC64;
MARFIDRVTL HVTAGHGGHG CASVHREKFK PLGGPDGGNG GRGGDVVLVV DPQVHTLLDF
HFSPHAKAGK GQPGMGSHRN GAQGADLVLK VPDGTVVTTP EGELLADLTG AGTEFIVAKG
GNGGLGNAAL ISKTRKAPGF ALLGEEGESC DVVLELKSVA DVGLVGFPSA GKSSLISVLS
AAKPKIADYP FTTLQPNLGV VTAGDITYTI ADVPGLIPGA AEGRGLGLDF LRHIERTAVL
AHVVDCATLD PGRDPVSDVD AVEAELAAYQ PALEGDMGLG DLADRPRIVV LNKVDVPEAK
ELAEFVKDEF SARGWPVFAI SAVSREGLKE LSFALAEMVH TYRDEHPVEQ EKRVYVRPQM
KEDDSFRILH DPEIPGGFIV DGVKPARWVA QTAFDNDEAV GFLADRLAKL GVEEALAEAG
AVPGSAVTIG DVCFDWEPST LAGVDMTPTG RGTDVRLDHN TRVSAKERRH AKRIRHGLAD
EDSDMNDEST W
//
