OLA1_ARATH
ID OLA1_ARATH Reviewed; 394 AA.
AC Q9SA73; Q8LDR5;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Obg-like ATPase 1 {ECO:0000255|HAMAP-Rule:MF_03167};
DE AltName: Full=Ribosome-binding ATPase YchF {ECO:0000303|PubMed:23550829};
DE Short=AtYchF1 {ECO:0000303|PubMed:23550829};
GN Name=YchF1 {ECO:0000303|PubMed:23550829};
GN OrderedLocusNames=At1g30580 {ECO:0000312|Araport:AT1G30580};
GN ORFNames=T5I8.3 {ECO:0000312|EMBL:AAD25745.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702 {ECO:0000312|Proteomes:UP000006548};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Kim C.J., Quinitio C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH CAR4/GAP1, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=cv. Col-2, and cv. Columbia;
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 [6]
RP FUNCTION, AND MUTAGENESIS OF 231-LEU--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 (By similarity). Confers sensitivity to salinity stress by
CC suppressing the anti-oxidation enzymatic activities and increasing
CC lipid peroxidation thus leading to the accumulation of reactive oxygen
CC species (ROS) (PubMed:23550829). Acts as negative regulator of disease
CC resistance against bacterial pathogen (PubMed:26912459).
CC {ECO:0000250|UniProtKB:Q6Z1J6, ECO:0000255|HAMAP-Rule:MF_03167,
CC ECO:0000269|PubMed:23550829, 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:0000250|UniProtKB:Q6Z1J6}.
CC -!- SUBUNIT: Monomer (Potential). Interacts with CAR4/GAP1
CC (PubMed:23550829). {ECO:0000255|HAMAP-Rule:MF_03167,
CC ECO:0000269|PubMed:23550829}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03167}.
CC Cytoplasm, cytosol {ECO:0000269|PubMed:23550829}. Note=Localized mainly
CC in the cytosol under NaCl treatment, but translocates to the plasma
CC membrane upon wounding. {ECO:0000269|PubMed:23550829}.
CC -!- DISRUPTION PHENOTYPE: Increased tolerance to salinity stress.
CC {ECO:0000269|PubMed:23550829}.
CC -!- MISCELLANEOUS: Plants over-expressing OLA1 exhibit enhanced
CC susceptibility to the bacterial pathogen Pseudomonas syringae pv.
CC tomato strain DC3000. {ECO:0000269|PubMed:26912459}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC007060; AAD25745.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31246.1; -; Genomic_DNA.
DR EMBL; BT025965; ABG25054.1; -; mRNA.
DR EMBL; AY085845; AAM63059.1; -; mRNA.
DR PIR; A86431; A86431.
DR RefSeq; NP_174346.1; NM_102795.3.
DR AlphaFoldDB; Q9SA73; -.
DR SMR; Q9SA73; -.
DR STRING; 3702.AT1G30580.1; -.
DR iPTMnet; Q9SA73; -.
DR MetOSite; Q9SA73; -.
DR PaxDb; Q9SA73; -.
DR PRIDE; Q9SA73; -.
DR ProteomicsDB; 250903; -.
DR EnsemblPlants; AT1G30580.1; AT1G30580.1; AT1G30580.
DR GeneID; 839938; -.
DR Gramene; AT1G30580.1; AT1G30580.1; AT1G30580.
DR KEGG; ath:AT1G30580; -.
DR Araport; AT1G30580; -.
DR TAIR; locus:2204599; AT1G30580.
DR eggNOG; KOG1491; Eukaryota.
DR HOGENOM; CLU_018395_1_0_1; -.
DR InParanoid; Q9SA73; -.
DR OMA; DFHDLCE; -.
DR OrthoDB; 738371at2759; -.
DR PhylomeDB; Q9SA73; -.
DR PRO; PR:Q9SA73; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SA73; baseline and differential.
DR Genevisible; Q9SA73; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
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:0006952; P:defense response; IEA:UniProtKB-KW.
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; 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 ATP-binding; Cytoplasm; GTP-binding; Hydrolase; Magnesium; Metal-binding;
KW Nucleotide-binding; Plant defense; Reference proteome.
FT CHAIN 1..394
FT /note="Obg-like ATPase 1"
FT /id="PRO_0000433306"
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"
FT MUTAGEN 231..233
FT /note="LNE->KSD: Abolishes binding to ATP, but has no
FT effect on binding to GTP; abolishes its function as
FT negative regulator of disease resistance."
FT /evidence="ECO:0000269|PubMed:26912459"
FT CONFLICT 375
FT /note="V -> F (in Ref. 4; AAM63059)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 394 AA; 44471 MW; 4DD667F20AFEA603 CRC64;
MPPKAKAKDA GPVERPILGR FSSHLKIGIV GLPNVGKSTL FNTLTKLSIP AENFPFCTIE
PNEARVNIPD ERFDWLCQTY KPKSEIPAFL EIHDIAGLVR GAHEGQGLGN NFLSHIRAVD
GIFHVLRAFE DADIIHVDDI VDPVRDLETI TEELRLKDIE FVGKKIDDVE KSMKRSNDKQ
LKIELELLQK VKAWLEDGKD VRFGDWKTAD IEILNTFQLL SAKPVVYLIN LNERDYQRKK
NKFLPKIHAW VQEHGGDTMI PFSGVFERSL ADMAPDEAAK YCEENKLQSA LPRIIKTGFS
AINLIYFFTA GPDEVKCWQI RRQSKAPQAA GAIHTDFERG FICAEVMKFE DLKELGNEPA
VKAAGKYRQE GKTYVVQDGD IIFFKFNVSG GGKK
