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Database: UniProt
Entry: V7LL03_MYCAV
LinkDB: V7LL03_MYCAV
Original site: V7LL03_MYCAV 
ID   V7LL03_MYCAV            Unreviewed;       492 AA.
AC   V7LL03;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   24-JAN-2024, entry version 51.
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:ETB22143.1};
GN   Synonyms=obg {ECO:0000256|HAMAP-Rule:MF_01454};
GN   ORFNames=O973_08225 {ECO:0000313|EMBL:ETB22143.1};
OS   Mycobacterium avium subsp. avium 11-4751.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium avium complex (MAC).
OX   NCBI_TaxID=1391992 {ECO:0000313|EMBL:ETB22143.1, ECO:0000313|Proteomes:UP000035007};
RN   [1] {ECO:0000313|EMBL:ETB22143.1, ECO:0000313|Proteomes:UP000035007}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=11-4751 {ECO:0000313|EMBL:ETB22143.1,
RC   ECO:0000313|Proteomes:UP000035007};
RA   Bannantine J.P., Robbe-Austerman S., O'Connell C.;
RT   "Genome sequence of MAC strains.";
RL   Submitted (OCT-2013) 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:ETB22143.1}.
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DR   EMBL; AYOB01000161; ETB22143.1; -; Genomic_DNA.
DR   AlphaFoldDB; V7LL03; -.
DR   PATRIC; fig|1391992.3.peg.1705; -.
DR   Proteomes; UP000035007; 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..438
FT                   /note="OCT"
FT                   /evidence="ECO:0000259|PROSITE:PS51881"
FT   REGION          449..492
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        454..492
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   492 AA;  52239 MW;  98988C3BFAB2FCB0 CRC64;
     MPRFVDRVVI HARAGSGGNG CASVHREKFK PLGGPDGGNG GRGGSIVFVV DPQVHTLLDF
     HFHPHISAPS GKQGMGNNRD GAAGADLEVK VPDGTVVLDE NGRLLADLVG AGTRFEAAAG
     GRGGLGNAAL ASRARKAPGF ALLGEPGETR ELTLELKTVA DVGLIGFPSA GKSSLVSAIS
     AAKPKIADYP FTTLVPNLGV VSAGEHTFTV ADVPGLIPGA SAGRGLGLDF LRHIERCAVL
     VHVIDCATAD PGRDPISDID ALEAELAAYT PTLQGDVTLG DLTERPRAVV LNKIDVPEAR
     ELAEFVRDEI AERGWPVFLV STVAREGLQP LTFGLWQMIS EYQSAQPEIV PRRPVIRPVP
     VDDSGFRVEP DPRQPGAFVV SGARPERWVR QTNFDNDEAV GYLADRLARL GVEEELLRLG
     ARPGCAVTIG DMTFDWEPQT PAGQQVVLSG RGTDARLERT ERVGAAERKA ARRQRRTGDD
     AERGTTERGE NT
//
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