OBG_NEIG1
ID OBG_NEIG1 Reviewed; 384 AA.
AC Q5F5D9;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=GTPase Obg {ECO:0000255|HAMAP-Rule:MF_01454};
DE EC=3.6.5.- {ECO:0000255|HAMAP-Rule:MF_01454, ECO:0000269|PubMed:26122105};
DE AltName: Full=GTP-binding protein Obg {ECO:0000255|HAMAP-Rule:MF_01454};
GN Name=obg {ECO:0000255|HAMAP-Rule:MF_01454}; OrderedLocusNames=NGO1990;
OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=242231;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700825 / FA 1090;
RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F.,
RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C.,
RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S.,
RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.;
RT "The complete genome sequence of Neisseria gonorrhoeae.";
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, COFACTOR, SUBCELLULAR LOCATION, INDUCTION, DISRUPTION PHENOTYPE,
RP GTP-BINDING, AND MUTAGENESIS OF 192-THR-THR-193.
RC STRAIN=ATCC 700825 / FA 1090;
RX PubMed=26122105; DOI=10.1186/s12866-015-0453-1;
RA Zielke R.A., Wierzbicki I.H., Baarda B.I., Sikora A.E.;
RT "The Neisseria gonorrhoeae Obg protein is an essential ribosome-associated
RT GTPase and a potential drug target.";
RL BMC Microbiol. 15:129-129(2015).
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; the half-life of the GTP-bound
CC state is about 50 minutes (PubMed:26122105). Plays a role in control of
CC the cell cycle, stress response, ribosome biogenesis and in those
CC bacteria that undergo differentiation, in morphogenesis control (By
CC similarity). {ECO:0000255|HAMAP-Rule:MF_01454,
CC ECO:0000269|PubMed:26122105}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01454,
CC ECO:0000269|PubMed:26122105};
CC Note=Optimal binding to GTP occurs between 5-10 mM Mg(2+), binding to
CC GDP is inhibited at > 1 mM Mg(2+). {ECO:0000269|PubMed:26122105};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01454}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01454,
CC ECO:0000269|PubMed:26122105}. Note=Associates with 50S ribosomal
CC subunits. A small amount may associate with the cell inner membrane.
CC {ECO:0000269|PubMed:26122105}.
CC -!- INDUCTION: Expressed constitutively, reaches maximum expression in
CC early log phase and remains constant until stationary phase. Similar
CC levels are seen when cells are grown under iron-limiting conditions,
CC anoxically or in the presence of human serum, which mimic clinical
CC infections (at protein level). {ECO:0000269|PubMed:26122105}.
CC -!- DISRUPTION PHENOTYPE: Essential, it cannot be deleted.
CC {ECO:0000269|PubMed:26122105}.
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; AE004969; AAW90598.1; -; Genomic_DNA.
DR RefSeq; WP_003686881.1; NC_002946.2.
DR RefSeq; YP_209010.1; NC_002946.2.
DR AlphaFoldDB; Q5F5D9; -.
DR SMR; Q5F5D9; -.
DR STRING; 242231.NGO_1990; -.
DR EnsemblBacteria; AAW90598; AAW90598; NGO_1990.
DR GeneID; 66754124; -.
DR KEGG; ngo:NGO_1990; -.
DR PATRIC; fig|242231.10.peg.2401; -.
DR HOGENOM; CLU_011747_2_0_4; -.
DR OMA; VVFDWEP; -.
DR Proteomes; UP000000535; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0019003; F:GDP binding; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0043022; F:ribosome binding; IDA:UniProtKB.
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 1: Evidence at protein level;
KW Cytoplasm; GTP-binding; Hydrolase; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..384
FT /note="GTPase Obg"
FT /id="PRO_0000386081"
FT DOMAIN 1..159
FT /note="Obg"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01231"
FT DOMAIN 160..348
FT /note="OBG-type G"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT REGION 20..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 129..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..148
FT /note="Polar 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 284..287
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT BINDING 329..331
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT MUTAGEN 192..193
FT /note="TT->AA: Loss of GTP-binding, binds GDP normally."
FT /evidence="ECO:0000269|PubMed:26122105"
SQ SEQUENCE 384 AA; 41998 MW; 2779AC222A662EEA CRC64;
MKFIDEAKIE VAAGKGGNGA TSFRREKFVP RGGPDGGDGG KGGSVWAEAD ENTNTLVEYR
FVKRYQAKNG EKGHGSDRYG AGADDIVLKM PVGTLIRDLD TDEIVADLTY HGQRVCLAKG
GKGGLGNIHF KSSVNRAPKQ STPGEEGETR SLQLELKVLA DVGLLGMPNA GKSTLITAVS
AARPKIANYP FTTLHPNLGV VRIDENHSFV MADIPGLIEG AAEGAGLGHR FLKHLSRTGL
LLHVVDLAPF DETVNPAEEA LAIINELRKY DEELYGKPRW LVLNKLDMLD EEEARARTAA
FLEAVGWDYP EPDDRFQFDM ETPRLFQISA LTHQGTQELV HQINQYLAEK KRIEAEKAEA
EKAAANVEII EQQPKTDTGV FKPE
