ID A0A1X1RRE0_MYCCE Unreviewed; 489 AA.
AC A0A1X1RRE0;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 30.
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 ORFNames=AWB95_10240 {ECO:0000313|EMBL:ORV13956.1}, CQY23_04200
GN {ECO:0000313|EMBL:PIB80229.1};
OS Mycobacterium celatum.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=28045 {ECO:0000313|EMBL:ORV13956.1, ECO:0000313|Proteomes:UP000193907};
RN [1] {ECO:0000313|EMBL:ORV13956.1, ECO:0000313|Proteomes:UP000193907}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44243 {ECO:0000313|EMBL:ORV13956.1,
RC ECO:0000313|Proteomes:UP000193907};
RA Tarcisio F., Conor M., Antonella G., Elisabetta G., Giulia F.S., Sara T.,
RA Anna F., Clotilde B., Roberto B., Veronica D.S., Fabio R., Monica P.,
RA Olivier J., Enrico T., Nicola S.;
RT "The new phylogeny of the genus Mycobacterium.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PIB80229.1, ECO:0000313|Proteomes:UP000230971}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 12882 {ECO:0000313|EMBL:PIB80229.1,
RC ECO:0000313|Proteomes:UP000230971};
RX PubMed=29030295; DOI=10.1016/j.meegid.2017.10.013;
RA Tortoli E., Fedrizzi T., Meehan C.J., Trovato A., Grottola A.,
RA Giacobazzi E., Serpini G.F., Tagliazucchi S., Fabio A., Bettua C.,
RA Bertorelli R., Frascaro F., De Sanctis V., Pecorari M., Jousson O.,
RA Segata N., Cirillo D.M.;
RT "The new phylogeny of the genus Mycobacterium: The old and the news.";
RL Infect. Genet. Evol. 56:19-25(2017).
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:ORV13956.1}.
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DR EMBL; LQOM01000025; ORV13956.1; -; Genomic_DNA.
DR EMBL; PDKV01000003; PIB80229.1; -; Genomic_DNA.
DR STRING; 28045.AWB95_10240; -.
DR OrthoDB; 9807318at2; -.
DR Proteomes; UP000193907; Unassembled WGS sequence.
DR Proteomes; UP000230971; 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..340
FT /note="OBG-type G"
FT /evidence="ECO:0000259|PROSITE:PS51710"
FT DOMAIN 358..436
FT /note="OCT"
FT /evidence="ECO:0000259|PROSITE:PS51881"
FT REGION 448..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..489
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: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 489 AA; 51550 MW; FD515D087D8B9FE5 CRC64;
MARFVDRVVI HARAGSGGNG CASVHREKFK PLGGPDGGNG GRGGSVILVV DPQVHTLLDF
HFHPHVVAPS GKQGMGGNRD GAAGADLEVK VPDGTVVLDE DGRLLADLVG AGTRFLAAAG
GRGGLGNAAL ASRARKAPGF ALLGEKGQAR DLTLELKTVA DVGLIGFPSA GKSSLVSAIS
AAKPKIADYP FTTLVPNLGV VSAGERTYTV ADVPGLIPGA SAGRGLGLDF LRHIERCAVL
VHVVDCATAD PGRDPVSDID ALEAELAAYQ PTLQGDSTLG DLTERPRAVV LNKVDVPEAR
ELAEFVRDDI AERGWPVFSV STATREGLQP LIFALADMVD EYHAAQPVVV PRRPVIRPVP
VDETGFTVQP DGQGGFVVCG ERPERWIAQT DFDNDEAVGY LGDRLARLGV EDELLRLGAQ
PGCAVTIGDM TFDWEPQTAA GVDVQLSSRG TDARLDRTER VGAAERKAAR RQRRAGDDAE
RSDEEERRI
//
