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OBG_ACIBT
ID   OBG_ACIBT               Reviewed;         406 AA.
AC   A3M7M2;
DT   13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 2.
DT   03-AUG-2022, entry version 90.
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}; OrderedLocusNames=A1S_2498;
OS   Acinetobacter baumannii (strain ATCC 17978 / CIP 53.77 / LMG 1025 / NCDC
OS   KC755 / 5377).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=400667;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17978 / CIP 53.77 / LMG 1025 / NCDC KC755 / 5377;
RX   PubMed=17344419; DOI=10.1101/gad.1510307;
RA   Smith M.G., Gianoulis T.A., Pukatzki S., Mekalanos J.J., Ornston L.N.,
RA   Gerstein M., Snyder M.;
RT   "New insights into Acinetobacter baumannii pathogenesis revealed by high-
RT   density pyrosequencing and transposon mutagenesis.";
RL   Genes Dev. 21:601-614(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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01454};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01454}.
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; CP000521; ABO12916.2; -; Genomic_DNA.
DR   RefSeq; WP_001212949.1; NZ_CP053098.1.
DR   AlphaFoldDB; A3M7M2; -.
DR   SMR; A3M7M2; -.
DR   KEGG; acb:A1S_2498; -.
DR   HOGENOM; CLU_011747_2_0_6; -.
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; 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   3: Inferred from homology;
KW   Cytoplasm; GTP-binding; Hydrolase; Magnesium; Metal-binding;
KW   Nucleotide-binding.
FT   CHAIN           1..406
FT                   /note="GTPase Obg"
FT                   /id="PRO_0000385668"
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          120..143
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          381..406
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        126..141
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        384..399
FT                   /note="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: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   406 AA;  44462 MW;  20D5F7F8A26657DB CRC64;
     MRFVDEAVIT VEAGDGGNGV ASFRREKFVP FGGPDGGDGG RGGSIYIQAD DDTSTLVDYR
     YTRKFRAERG KNGAGANCTG RGGEDVVLKV PVGTTIVDTD SGDIIGDLVE DGQRVMVASG
     GEGGLGNTHF KSSTNRAPRK CTTGTKGEFR EIRLELKVLA DVGLLGMPNA GKSTFIRAVS
     AAKPKVADYP FTTMVPNLGV VDADRHRSFV MADIPGLIEG AAEGAGLGIR FLKHLARTRI
     LLHIIDVQPI DGSDPAHNAK AIMNELAKFS PTLAKLPIVL VLNKLDQIAE ESREEWCQHI
     LDELQWTGPV FKTSGLLEEG TKEVVYYLMD QIEQQREREV EDPEYAAEVR AFREQLEAET
     REQTIAAKEA YRAMRKAQRL ESMMDDDDDF DDDEDDGDVE SIYVRD
 
 
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