OBG_LISMH
ID OBG_LISMH Reviewed; 429 AA.
AC B8DHL1;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 80.
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=LMHCC_1032;
OS Listeria monocytogenes serotype 4a (strain HCC23).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=552536;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HCC23;
RX PubMed=21602330; DOI=10.1128/jb.05236-11;
RA Steele C.L., Donaldson J.R., Paul D., Banes M.M., Arick T., Bridges S.M.,
RA Lawrence M.L.;
RT "Genome sequence of lineage III Listeria monocytogenes strain HCC23.";
RL J. Bacteriol. 193:3679-3680(2011).
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; CP001175; ACK39380.1; -; Genomic_DNA.
DR RefSeq; WP_012581276.1; NC_011660.1.
DR AlphaFoldDB; B8DHL1; -.
DR SMR; B8DHL1; -.
DR KEGG; lmh:LMHCC_1032; -.
DR HOGENOM; CLU_011747_2_1_9; -.
DR OMA; VVFDWEP; -.
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; 3.30.300.350; -; 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; 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 InterPro; IPR005225; Small_GTP-bd_dom.
DR PANTHER; PTHR11702; PTHR11702; 1.
DR Pfam; PF09269; DUF1967; 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; SSF102741; SSF102741; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF82051; SSF82051; 1.
DR TIGRFAMs; TIGR02729; Obg_CgtA; 1.
DR TIGRFAMs; TIGR03595; Obg_CgtA_exten; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 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; GTP-binding; Hydrolase; Magnesium; Metal-binding;
KW Nucleotide-binding.
FT CHAIN 1..429
FT /note="GTPase Obg"
FT /id="PRO_0000386024"
FT DOMAIN 1..158
FT /note="Obg"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01231"
FT DOMAIN 159..329
FT /note="OBG-type G"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT DOMAIN 351..429
FT /note="OCT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01229"
FT REGION 124..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 212..215
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT BINDING 282..285
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
FT BINDING 310..312
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01454"
SQ SEQUENCE 429 AA; 47105 MW; 73383B996F96CA45 CRC64;
MFVDQVKIYV KAGNGGDGMV AFRREKFVPN GGPAGGDGGK GADVVFVVDE GLRTLVDFRF
KRIFKAEHGE HGMSKSMHGR GAEDLVVKVP QGTIVKDIDT GEIIADLVAH GQRAVIAKAG
RGGRGNKRFA TPANPAPELS ENGEPGQERN VQLELKVLAD VGLVGFPSVG KSTLLSVVSA
ARPKIAAYHF TTIVPNLGMV DAGDGRSFVM ADLPGLIEGA SQGVGLGHQF LRHIERTRVI
VHVIDMSGSE GRVPYEDYMA INNELEQYNL RLMERPQIIV ANKMDMPDAE ENLNEFKTKI
AEDIPVFPIS AVTKTGLREL LLAIADKLET TPEFPLNEIL EQEDEDTVLY KYVADEPDFE
ISREPDGTFV LSGAKIERLF TMTNFERDAS ISRFARQLRA MGVDEALRKR GAKDGDIVRL
LDYEFEFMD
