OLA1_ORYSJ
ID OLA1_ORYSJ Reviewed; 394 AA.
AC Q6Z1J6; A0A0P0XCP6; Q0J7E5;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Obg-like ATPase 1 {ECO:0000255|HAMAP-Rule:MF_03167};
DE EC=3.6.5.- {ECO:0000269|PubMed:19086295};
DE AltName: Full=Ribosome-binding ATPase YchF {ECO:0000303|PubMed:23550829};
DE Short=OsYchF1 {ECO:0000303|PubMed:23550829};
GN Name=YCHF1 {ECO:0000303|PubMed:23550829};
GN OrderedLocusNames=LOC_Os08g09940 {ECO:0000305},
GN Os08g0199300 {ECO:0000312|EMBL:BAF23120.2};
GN ORFNames=OsJ_26368 {ECO:0000312|EMBL:EEE68206.1},
GN OSJNBb0094P23.28 {ECO:0000312|EMBL:BAD03576.1};
OS Oryza sativa subsp. japonica (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=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
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).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [6]
RP FUNCTION, INTERACTION WITH GAP1, AND ACTIVITY REGULATION.
RC STRAIN=cv. Aichi asahi;
RX PubMed=19086295; DOI=10.1111/j.1469-8137.2008.02473.x;
RA Cheung M.-Y., Zeng N.-Y., Tong S.-W., Li W.-Y., Xue Y., Zhao K.-J.,
RA Wang C., Zhang Q., Fu Y., Sun Z., Sun S.-S., Lam H.-M.;
RT "Constitutive expression of a rice GTPase-activating protein induces
RT defense responses.";
RL New Phytol. 179:530-545(2008).
RN [7]
RP FUNCTION, ACTIVITY REGULATION, INTERACTION WITH GAP1, SUBCELLULAR LOCATION,
RP AND DOMAIN.
RX PubMed=20876569; DOI=10.1074/jbc.m110.172080;
RA Cheung M.Y., Xue Y., Zhou L., Li M.W., Sun S.S., Lam H.M.;
RT "An ancient P-loop GTPase in rice is regulated by a higher plant-specific
RT regulatory protein.";
RL J. Biol. Chem. 285:37359-37369(2010).
RN [8]
RP FUNCTION, INTERACTION WITH GAP1, AND SUBCELLULAR LOCATION.
RX PubMed=23550829; DOI=10.1111/pce.12108;
RA Cheung M.-Y., Li M.-W., Yung Y.-L., Wen C.-Q., Lam H.-M.;
RT "The unconventional P-loop NTPase OsYchF1 and its regulator OsGAP1 play
RT opposite roles in salinity stress tolerance.";
RL Plant Cell Environ. 36:2008-2020(2013).
RN [9]
RP INTERACTION WITH GAP1.
RX PubMed=26286751; DOI=10.1074/jbc.m115.655639;
RA Yung Y.L., Cheung M.Y., Miao R., Fong Y.H., Li K.P., Yu M.H., Chye M.L.,
RA Wong K.B., Lam H.M.;
RT "Site-directed mutagenesis shows the significance of interactions with
RT phospholipids and the G-protein OsYchF1 for the physiological functions of
RT the rice GTPase-activating protein 1 (OsGAP1).";
RL J. Biol. Chem. 290:23984-23996(2015).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH ATP AND GTP ANALOGS,
RP FUNCTION, AND MUTAGENESIS OF 231-MET--GLU-233.
RX PubMed=26912459; DOI=10.1073/pnas.1522966113;
RA Cheung M.Y., Li X., Miao R., Fong Y.H., Li K.P., Yung Y.L., Yu M.H.,
RA Wong K.B., Chen Z., Lam H.M.;
RT "ATP binding by the P-loop NTPase OsYchF1 (an unconventional G protein)
RT contributes to biotic but not abiotic stress responses.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:2648-2653(2016).
CC -!- FUNCTION: Hydrolyzes ATP, and can also hydrolyze GTP with lower
CC efficiency. Has lower affinity for GTP (Potential). Exhibits GTPase
CC activity (PubMed:19086295). Exhibits similar binding affinities and
CC hydrolytic activities toward both GTP and ATP (PubMed:20876569,
CC PubMed:26912459). Binds to the 26 S ribosomal RNA in vitro, but not to
CC the 5.8 S or 18 S rRNA (PubMed:20876569). Confers sensitivity to
CC salinity stress by suppressing the anti-oxidation enzymatic activities
CC and increasing lipid peroxidation thus leading to the accumulation of
CC reactive oxygen species (ROS) (PubMed:23550829). {ECO:0000255|HAMAP-
CC Rule:MF_03167, ECO:0000269|PubMed:19086295,
CC ECO:0000269|PubMed:20876569, ECO:0000269|PubMed:23550829,
CC ECO:0000269|PubMed:26912459}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU01047};
CC -!- ACTIVITY REGULATION: Activated by GAP1. {ECO:0000269|PubMed:19086295,
CC ECO:0000269|PubMed:20876569}.
CC -!- SUBUNIT: Monomer (Potential). Interacts with GAP1. {ECO:0000255|HAMAP-
CC Rule:MF_03167, ECO:0000269|PubMed:19086295,
CC ECO:0000269|PubMed:20876569, ECO:0000269|PubMed:23550829,
CC ECO:0000269|PubMed:26286751}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20876569,
CC ECO:0000269|PubMed:23550829}. Cytoplasm {ECO:0000255|HAMAP-
CC Rule:MF_03167}. Cytoplasm, cytosol {ECO:0000269|PubMed:20876569,
CC ECO:0000269|PubMed:23550829}. Note=Localized mainly in the cytosol
CC under NaCl treatment, but translocates to the plasma membrane upon
CC wounding. {ECO:0000269|PubMed:20876569, ECO:0000269|PubMed:23550829}.
CC -!- DOMAIN: The C-terminal domain is involved in RNA binding.
CC {ECO:0000269|PubMed:20876569}.
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; AP005416; BAD03576.1; -; Genomic_DNA.
DR EMBL; AP008214; BAF23120.2; -; Genomic_DNA.
DR EMBL; AP014964; BAT04246.1; -; Genomic_DNA.
DR EMBL; CM000145; EEE68206.1; -; Genomic_DNA.
DR EMBL; AK062256; BAG88257.1; -; mRNA.
DR EMBL; AK098917; BAG93810.1; -; mRNA.
DR RefSeq; XP_015650773.1; XM_015795287.1.
DR PDB; 5EE0; X-ray; 2.20 A; A=1-394.
DR PDB; 5EE1; X-ray; 2.55 A; A=1-394.
DR PDB; 5EE3; X-ray; 2.90 A; A/B=1-394.
DR PDB; 5EE9; X-ray; 2.75 A; A/B=1-394.
DR PDBsum; 5EE0; -.
DR PDBsum; 5EE1; -.
DR PDBsum; 5EE3; -.
DR PDBsum; 5EE9; -.
DR AlphaFoldDB; Q6Z1J6; -.
DR SMR; Q6Z1J6; -.
DR STRING; 4530.OS08T0199300-01; -.
DR PaxDb; Q6Z1J6; -.
DR PRIDE; Q6Z1J6; -.
DR EnsemblPlants; Os08t0199300-01; Os08t0199300-01; Os08g0199300.
DR GeneID; 4344894; -.
DR Gramene; Os08t0199300-01; Os08t0199300-01; Os08g0199300.
DR KEGG; osa:4344894; -.
DR eggNOG; KOG1491; Eukaryota.
DR HOGENOM; CLU_018395_1_0_1; -.
DR InParanoid; Q6Z1J6; -.
DR OMA; DFHDLCE; -.
DR OrthoDB; 738371at2759; -.
DR Proteomes; UP000000763; Chromosome 8.
DR Proteomes; UP000007752; Chromosome 8.
DR Proteomes; UP000059680; Chromosome 8.
DR Genevisible; Q6Z1J6; OS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
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; IMP:UniProtKB.
DR GO; GO:1901001; P:negative regulation of response to salt stress; IMP:UniProtKB.
DR GO; GO:0009651; P:response to salt stress; IDA: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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell membrane; Cytoplasm; GTP-binding;
KW Hydrolase; Magnesium; Membrane; Metal-binding; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..394
FT /note="Obg-like ATPase 1"
FT /id="PRO_0000433307"
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:0000269|PubMed:26912459,
FT ECO:0007744|PDB:5EE3"
FT BINDING 34..39
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:26912459,
FT ECO:0007744|PDB:5EE9"
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:0000269|PubMed:26912459,
FT ECO:0007744|PDB:5EE9"
FT BINDING 230..231
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:26912459,
FT ECO:0007744|PDB:5EE3"
FT BINDING 230
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:26912459,
FT ECO:0007744|PDB:5EE9"
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"
FT MUTAGEN 231..233
FT /note="MSE->KSD: Abolishes binding to ATP, but has no
FT effect on binding to GTP."
FT /evidence="ECO:0000269|PubMed:26912459"
FT STRAND 27..30
FT /evidence="ECO:0007829|PDB:5EE0"
FT STRAND 32..36
FT /evidence="ECO:0007829|PDB:5EE9"
FT HELIX 37..46
FT /evidence="ECO:0007829|PDB:5EE0"
FT HELIX 51..53
FT /evidence="ECO:0007829|PDB:5EE0"
FT STRAND 63..67
FT /evidence="ECO:0007829|PDB:5EE0"
FT HELIX 71..80
FT /evidence="ECO:0007829|PDB:5EE0"
FT STRAND 83..86
FT /evidence="ECO:0007829|PDB:5EE0"
FT STRAND 89..94
FT /evidence="ECO:0007829|PDB:5EE0"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:5EE1"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:5EE1"
FT HELIX 110..116
FT /evidence="ECO:0007829|PDB:5EE0"
FT STRAND 122..127
FT /evidence="ECO:0007829|PDB:5EE0"
FT HELIX 143..175
FT /evidence="ECO:0007829|PDB:5EE0"
FT HELIX 179..196
FT /evidence="ECO:0007829|PDB:5EE0"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:5EE0"
FT HELIX 208..217
FT /evidence="ECO:0007829|PDB:5EE0"
FT HELIX 220..222
FT /evidence="ECO:0007829|PDB:5EE0"
FT STRAND 225..230
FT /evidence="ECO:0007829|PDB:5EE0"
FT HELIX 233..238
FT /evidence="ECO:0007829|PDB:5EE0"
FT HELIX 244..253
FT /evidence="ECO:0007829|PDB:5EE0"
FT STRAND 259..262
FT /evidence="ECO:0007829|PDB:5EE0"
FT HELIX 264..271
FT /evidence="ECO:0007829|PDB:5EE0"
FT HELIX 275..285
FT /evidence="ECO:0007829|PDB:5EE0"
FT HELIX 291..301
FT /evidence="ECO:0007829|PDB:5EE0"
FT STRAND 304..321
FT /evidence="ECO:0007829|PDB:5EE0"
FT HELIX 326..331
FT /evidence="ECO:0007829|PDB:5EE0"
FT HELIX 335..339
FT /evidence="ECO:0007829|PDB:5EE0"
FT STRAND 341..348
FT /evidence="ECO:0007829|PDB:5EE0"
FT HELIX 349..355
FT /evidence="ECO:0007829|PDB:5EE0"
FT HELIX 358..363
FT /evidence="ECO:0007829|PDB:5EE0"
FT STRAND 368..370
FT /evidence="ECO:0007829|PDB:5EE0"
FT STRAND 380..386
FT /evidence="ECO:0007829|PDB:5EE0"
SQ SEQUENCE 394 AA; 44333 MW; C94B5882516FA856 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 GKTYVVQDGD IIFFKFNVSG GGKK
