OBG_CHLAB
ID OBG_CHLAB Reviewed; 335 AA.
AC Q5L6R9;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
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:21195156};
DE AltName: Full=GTP-binding protein Obg {ECO:0000255|HAMAP-Rule:MF_01454};
GN Name=obg {ECO:0000255|HAMAP-Rule:MF_01454};
GN Synonyms=yhbZ {ECO:0000303|PubMed:21195156}; OrderedLocusNames=CAB194;
OS Chlamydia abortus (strain DSM 27085 / S26/3) (Chlamydophila abortus).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=218497;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 27085 / S26/3;
RX PubMed=15837807; DOI=10.1101/gr.3684805;
RA Thomson N.R., Yeats C., Bell K., Holden M.T.G., Bentley S.D.,
RA Livingstone M., Cerdeno-Tarraga A.-M., Harris B., Doggett J., Ormond D.,
RA Mungall K., Clarke K., Feltwell T., Hance Z., Sanders M., Quail M.A.,
RA Price C., Barrell B.G., Parkhill J., Longbottom D.;
RT "The Chlamydophila abortus genome sequence reveals an array of variable
RT proteins that contribute to interspecies variation.";
RL Genome Res. 15:629-640(2005).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, AND EXPRESSION IN E.COLI.
RC STRAIN=DSM 27085 / S26/3;
RX PubMed=21195156; DOI=10.1016/j.micpath.2010.12.005;
RA Polkinghorne A., Vaughan L.;
RT "Chlamydia abortus YhbZ, a truncated Obg family GTPase, associates with the
RT Escherichia coli large ribosomal subunit.";
RL Microb. Pathog. 50:200-206(2011).
CC -!- FUNCTION: An essential GTPase (4.1 pmol GTP/min) (PubMed:21195156).
CC Cannot substitute endogenous obg in E.coli, has a partially dominant-
CC negative phenotype upon overexpression in liquid culture leading to
CC decreased growth rate in a concentration-dependent fashion, with 50% of
CC cells being elongated (PubMed:21195156). Binds GTP, GDP and possibly
CC (p)ppGpp with moderate affinity, with high nucleotide exchange rates
CC and a fairly low GTP hydrolysis rate. It may play 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:21195156}.
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 ECO:0000305|PubMed:21195156}. Note=Associates with 50S ribosomal
CC subunit upon overexpression in E.coli. {ECO:0000269|PubMed:21195156}.
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; CR848038; CAH63652.1; -; Genomic_DNA.
DR RefSeq; WP_011096890.1; NC_004552.2.
DR AlphaFoldDB; Q5L6R9; -.
DR SMR; Q5L6R9; -.
DR EnsemblBacteria; CAH63652; CAH63652; CAB194.
DR KEGG; cab:CAB194; -.
DR eggNOG; COG0536; Bacteria.
DR HOGENOM; CLU_011747_2_3_0; -.
DR OMA; VVFDWEP; -.
DR OrthoDB; 603226at2; -.
DR Proteomes; UP000001012; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
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; 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; PS51883; OBG; 1.
PE 3: Inferred from homology;
KW Cytoplasm; GTP-binding; Hydrolase; Magnesium; Metal-binding;
KW Nucleotide-binding.
FT CHAIN 1..335
FT /note="GTPase Obg"
FT /id="PRO_0000385819"
FT DOMAIN 1..158
FT /note="Obg"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01231"
FT DOMAIN 159..334
FT /note="OBG-type G"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT BINDING 165..172
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT BINDING 172
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT BINDING 190..194
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT BINDING 192
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT BINDING 215..218
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT BINDING 285..288
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT BINDING 315..317
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
SQ SEQUENCE 335 AA; 36956 MW; 7AE1433C74212AFF CRC64;
MFLDQITIEL RAGKGGNGVV AWRKEKYLPK GGPYGGNGGV GGSIIIESAT HVYSFESYRN
IRFLKAEDGR PGATNNRSGK NGKDLVLIVP EGTLLRDVET KEILYDFAKS GERLVVCRGG
KGGKGNTFFK TSTNRAPTKA TPGKPGEIRQ VELELKLIAD IGLVGFPNAG KSTLFNTLAR
TEVKVGAYPF TTLQPVLGLV PCQEKLYQKP WIIADIPGII EGAHQNRGLG LDFLRHIERT
RLLLFVIDIC GCERSSPEED LRILMDELVH YREDLADKNR IIALNKIDDL LPDERQERLE
SFQKLFPSET FVLVSGLTGE GVDLLNSLFT NKLAV
