OLA1_ORYSI
ID OLA1_ORYSI Reviewed; 394 AA.
AC B8BBN7;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Obg-like ATPase 1 {ECO:0000255|HAMAP-Rule:MF_03167};
DE AltName: Full=Ribosome-binding ATPase YchF;
DE Short=OsYchF1;
GN ORFNames=OsI_28170 {ECO:0000312|EMBL:EEC83063.1};
OS Oryza sativa subsp. indica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39946 {ECO:0000312|Proteomes:UP000007015};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 93-11;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
CC -!- FUNCTION: Hydrolyzes ATP, and can also hydrolyze GTP with lower
CC efficiency. Has lower affinity for GTP (Potential). Exhibits GTPase
CC activity (By similarity). Exhibits similar binding affinities and
CC hydrolytic activities toward both GTP and ATP (By similarity). Binds to
CC the 26 S ribosomal RNA in vitro, but not to the 5.8 S or 18 S rRNA (By
CC similarity). Confers sensitivity to salinity stress by suppressing the
CC anti-oxidation enzymatic activities and increasing lipid peroxidation
CC thus leading to the accumulation of reactive oxygen species (ROS) (By
CC similarity). {ECO:0000250|UniProtKB:Q6Z1J6, ECO:0000255|HAMAP-
CC Rule:MF_03167}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU01047};
CC -!- ACTIVITY REGULATION: Activated by GAP1. {ECO:0000250|UniProtKB:Q6Z1J6}.
CC -!- SUBUNIT: Monomer (Potential). Interacts with GAP1 (By similarity).
CC {ECO:0000250|UniProtKB:Q6Z1J6, ECO:0000255|HAMAP-Rule:MF_03167}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03167}. Cell
CC membrane {ECO:0000250|UniProtKB:Q6Z1J6}. Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q6Z1J6}. Note=Localized mainly in the cytosol
CC under NaCl treatment, but translocates to the plasma membrane upon
CC wounding. {ECO:0000250|UniProtKB:Q6Z1J6}.
CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase
CC superfamily. OBG GTPase family. YchF/OLA1 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03167}.
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DR EMBL; CM000133; EEC83063.1; -; Genomic_DNA.
DR AlphaFoldDB; B8BBN7; -.
DR SMR; B8BBN7; -.
DR STRING; 39946.B8BBN7; -.
DR EnsemblPlants; BGIOSGA028156-TA; BGIOSGA028156-PA; BGIOSGA028156.
DR Gramene; BGIOSGA028156-TA; BGIOSGA028156-PA; BGIOSGA028156.
DR HOGENOM; CLU_018395_1_0_1; -.
DR OMA; DFHDLCE; -.
DR Proteomes; UP000007015; Chromosome 8.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:EnsemblPlants.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043023; F:ribosomal large subunit binding; IEA:UniProtKB-UniRule.
DR GO; GO:0043022; F:ribosome binding; IEA:UniProtKB-UniRule.
DR GO; GO:1900425; P:negative regulation of defense response to bacterium; IEA:EnsemblPlants.
DR GO; GO:1901001; P:negative regulation of response to salt stress; ISS:UniProtKB.
DR GO; GO:0009651; P:response to salt stress; ISS:UniProtKB.
DR CDD; cd04867; TGS_YchF_OLA1; 1.
DR CDD; cd01900; YchF; 1.
DR Gene3D; 1.10.150.300; -; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00944; YchF_OLA1_ATPase; 1.
DR InterPro; IPR004396; ATPase_YchF/OLA1.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR031167; G_OBG.
DR InterPro; IPR006073; GTP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR004095; TGS.
DR InterPro; IPR012676; TGS-like.
DR InterPro; IPR023192; TGS-like_dom_sf.
DR InterPro; IPR013029; YchF_C.
DR InterPro; IPR041706; YchF_N.
DR Pfam; PF01926; MMR_HSR1; 1.
DR Pfam; PF06071; YchF-GTPase_C; 1.
DR PIRSF; PIRSF006641; CHP00092; 1.
DR PRINTS; PR00326; GTP1OBG.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF81271; SSF81271; 1.
DR TIGRFAMs; TIGR00092; TIGR00092; 1.
DR PROSITE; PS51710; G_OBG; 1.
DR PROSITE; PS51880; TGS; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell membrane; Cytoplasm; GTP-binding; Hydrolase; Magnesium;
KW Membrane; Metal-binding; Nucleotide-binding; Reference proteome.
FT CHAIN 1..394
FT /note="Obg-like ATPase 1"
FT /id="PRO_0000433308"
FT DOMAIN 25..282
FT /note="OBG-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01047"
FT DOMAIN 303..386
FT /note="TGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01228"
FT BINDING 34..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03167"
FT BINDING 38
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01047"
FT BINDING 56..60
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01047"
FT BINDING 58
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01047"
FT BINDING 94..97
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01047"
FT BINDING 129
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q6Z1J6"
FT BINDING 230..231
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q6Z1J6"
FT BINDING 231
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03167"
FT BINDING 263..265
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01047"
FT BINDING 263..265
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01047"
SQ SEQUENCE 394 AA; 44347 MW; 026B5882516FA851 CRC64;
MPPKASKKDA APAERPILGR FSSHLKIGIV GLPNVGKSTF FNIVTKLSIP AENFPFCTID
PNEARVYVPD ERFDWLCQLY KPKSEVSAYL EINDIAGLVR GAHAGEGLGN AFLSHIRAVD
GIFHVLRAFE DKEVTHIDDS VDPVRDLETI GEELRLKDIE FVQNKIDDLE KSMKRSNDKQ
LKLEHELCEK VKAHLEDGKD VRFGDWKSAD IEILNTFQLL TAKPVVYLVN MSEKDYQRKK
NKFLPKIHAW VQEHGGETII PFSCAFERLL ADMPPDEAAK YCAENQIASV IPKIIKTGFA
AIHLIYFFTA GPDEVKCWQI RRQTKAPQAA GTIHTDFERG FICAEVMKFD DLKELGSESA
VKAAGKYRQE GKTYVVQDAD IIFFKFNVSG GGKK
