ID A0A0J6W5L8_9MYCO Unreviewed; 480 AA.
AC A0A0J6W5L8;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 39.
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=obg {ECO:0000256|HAMAP-Rule:MF_01454,
GN ECO:0000313|EMBL:KMO77784.1};
GN Synonyms=obgE {ECO:0000313|EMBL:TDL08588.1};
GN ORFNames=EUA04_14275 {ECO:0000313|EMBL:TDL08588.1}, MOBUDSM44075_01692
GN {ECO:0000313|EMBL:KMO77784.1}, WN67_29550
GN {ECO:0000313|EMBL:KKE98386.1};
OS Mycolicibacterium obuense.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=1807 {ECO:0000313|EMBL:KMO77784.1, ECO:0000313|Proteomes:UP000036313};
RN [1] {ECO:0000313|EMBL:KMO77784.1, ECO:0000313|Proteomes:UP000036313}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44075 {ECO:0000313|EMBL:KMO77784.1,
RC ECO:0000313|Proteomes:UP000036313};
RX PubMed=26079817; DOI=10.1093/gbe/evv111;
RA Das S., Pettersson B.M., Behra P.R., Ramesh M., Dasgupta S.,
RA Bhattacharya A., Kirsebom L.A.;
RT "Characterization of Three Mycobacterium spp. with Potential Use in
RT Bioremediation by Genome Sequencing and Comparative Genomics.";
RL Genome Biol. Evol. 7:1871-1886(2015).
RN [2] {ECO:0000313|EMBL:KKE98386.1, ECO:0000313|Proteomes:UP000034150}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UC1 {ECO:0000313|EMBL:KKE98386.1,
RC ECO:0000313|Proteomes:UP000034150};
RA Greninger A.L., Cunningham G., Chiu C.Y., Miller S.;
RT "Genome sequence of Mycobacterium obuense UC1.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:TDL08588.1, ECO:0000313|Proteomes:UP000294952}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=22DIII {ECO:0000313|EMBL:TDL08588.1,
RC ECO:0000313|Proteomes:UP000294952};
RA Tiago I., Alarico S., Pereira S.G., Coelho C., Maranha A., Empadinhas N.;
RT "High-quality-draft genome sequences of five non-tuberculosis
RT mycobacteriaceae isolated from a nosocomial environment.";
RL Submitted (JAN-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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KMO77784.1}.
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DR EMBL; LAUZ02000173; KKE98386.1; -; Genomic_DNA.
DR EMBL; JYNU01000009; KMO77784.1; -; Genomic_DNA.
DR EMBL; SDLP01000003; TDL08588.1; -; Genomic_DNA.
DR RefSeq; WP_046366658.1; NZ_SDLP01000003.1.
DR STRING; 1807.MOBUDSM44075_01692; -.
DR PATRIC; fig|1807.13.peg.6240; -.
DR OrthoDB; 9807318at2; -.
DR Proteomes; UP000034150; Unassembled WGS sequence.
DR Proteomes; UP000036313; Unassembled WGS sequence.
DR Proteomes; UP000294952; Unassembled WGS sequence.
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}.
FT DOMAIN 2..159
FT /note="Obg"
FT /evidence="ECO:0000259|PROSITE:PS51883"
FT DOMAIN 160..341
FT /note="OBG-type G"
FT /evidence="ECO:0000259|PROSITE:PS51710"
FT DOMAIN 359..437
FT /note="OCT"
FT /evidence="ECO:0000259|PROSITE:PS51881"
FT REGION 450..480
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 322..324
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01454"
SQ SEQUENCE 480 AA; 50676 MW; AAED269FDDEBC1F1 CRC64;
MTRFIDRVVI HARAGNGGNG CASVHREKFK PLGGPDGGNG GRGGSIVFVV DPQVHTLLDF
HFHPHVVAPS GKQGAGSNRD GAAGADLEVK VPDGTVVLDE QGRLLADLVG PGTRFEAAAG
GRGGLGNAAL ASRARKAPGF ALLGEKGEIR DLTLELKTVA DVGLVGFPSA GKSSLVSAIS
AAKPKIADYP FTTLAPNLGV VSAGDHTFTV ADVPGLIPGA SEGRGLGLDF LRHIERCAVL
VHVVDCATLE PGRDPISDIE ALEAEIAAYT PTLQGDTTLG DLAERPRAVV LNKIDVPEAR
ELADFVSEEI ASTFGWPVFE VSTVAREGLR PLTFALWDMV AAYRAAQPEV VPRRPVIRPV
PVDETSFSVE PDGQGGFVVR GTRPQRWVAQ TNFENDEAVG YLGDRLARLG VEDELLKLGA
RPGCAVTIGD MTFDWEPQTP AGVDVHLSGR GTDIRLEQSD RVSADERKAA RKARRESAPE
//
