BOLA1_ARATH
ID BOLA1_ARATH Reviewed; 160 AA.
AC Q682I1; Q681B9; Q681R0; Q94EW7;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Protein BOLA1, chloroplastic {ECO:0000303|PubMed:24203231};
DE Flags: Precursor;
GN Name=BOLA1 {ECO:0000303|PubMed:24203231};
GN OrderedLocusNames=At1g55805 {ECO:0000312|Araport:AT1G55805};
GN ORFNames=F14J16 {ECO:0000312|EMBL:AC002304};
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|EMBL:BAD43149.1};
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 Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-160.
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP SUBCELLULAR LOCATION, INTERACTION WITH GRXC5; GRXS14; GRXS15; GRXS16 AND
RP GRXS17, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=24203231; DOI=10.1093/mp/sst156;
RA Couturier J., Wu H.C., Dhalleine T., Pegeot H., Sudre D., Gualberto J.M.,
RA Jacquot J.P., Gaymard F., Vignols F., Rouhier N.;
RT "Monothiol glutaredoxin-BolA interactions: redox control of Arabidopsis
RT thaliana BolA2 and SufE1.";
RL Mol. Plant 7:187-205(2014).
RN [6]
RP FUNCTION, AND INTERACTION WITH GRXS14 AND GRXS16.
RX PubMed=24714563; DOI=10.4161/psb.28564;
RA Dhalleine T., Rouhier N., Couturier J.;
RT "Putative roles of glutaredoxin-BolA holo-heterodimers in plants.";
RL Plant Signal. Behav. 9:E28564-E28564(2014).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 64-160, AND INTERACTION WITH
RP GRXS14.
RX PubMed=25012657; DOI=10.1074/jbc.m114.572701;
RA Roret T., Tsan P., Couturier J., Zhang B., Johnson M.K., Rouhier N.,
RA Didierjean C.;
RT "Structural and spectroscopic insights into BolA-glutaredoxin complexes.";
RL J. Biol. Chem. 289:24588-24598(2014).
CC -!- FUNCTION: May act either alone or in interaction with glutaredoxin as a
CC redox-regulated transcriptional regulator, or as a factor regulating
CC Fe-S cluster biogenesis (Probable). The glutaredoxin-BOLA1 heterodimers
CC bind a labile, oxygen sensitive iron-sulfur cluster (PubMed:24714563).
CC {ECO:0000269|PubMed:24714563, ECO:0000305|PubMed:24203231}.
CC -!- SUBUNIT: Interacts in vitro with GRXS14, GRXS15, GRXS16 and GRXS17, but
CC not with GRXC5 (PubMed:24203231). Interacts in vivo only with GRXS14
CC and GRXS16 (PubMed:24203231, PubMed:24714563).
CC {ECO:0000269|PubMed:24203231, ECO:0000269|PubMed:24714563}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:24203231}.
CC -!- MISCELLANEOUS: The GRXS14-BOLA1 apo-heterodimer model derived from NMR
CC data shows a domain arrangement totally different from the holo-
CC heterodimer showing evidence for a Rieske-type ligation of a [2Fe-2S]
CC cluster. {ECO:0000269|PubMed:25012657}.
CC -!- SIMILARITY: Belongs to the bolA/yrbA family.
CC {ECO:0000255|RuleBase:RU003860}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK63866.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAD93986.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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; AC002304; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002684; AEE33299.1; -; Genomic_DNA.
DR EMBL; AK175386; BAD43149.1; -; mRNA.
DR EMBL; AK175698; BAD43461.1; -; mRNA.
DR EMBL; AK175557; BAD43320.1; -; mRNA.
DR EMBL; AK220773; BAD93986.1; ALT_INIT; mRNA.
DR EMBL; AY143802; AAN28741.1; -; mRNA.
DR EMBL; AF389294; AAK63866.1; ALT_INIT; mRNA.
DR RefSeq; NP_564702.2; NM_104457.5.
DR PDB; 4PUG; X-ray; 2.00 A; A/B=64-160.
DR PDBsum; 4PUG; -.
DR AlphaFoldDB; Q682I1; -.
DR SMR; Q682I1; -.
DR STRING; 3702.AT1G55805.1; -.
DR iPTMnet; Q682I1; -.
DR MetOSite; Q682I1; -.
DR PaxDb; Q682I1; -.
DR PRIDE; Q682I1; -.
DR ProteomicsDB; 222815; -.
DR EnsemblPlants; AT1G55805.1; AT1G55805.1; AT1G55805.
DR GeneID; 842030; -.
DR Gramene; AT1G55805.1; AT1G55805.1; AT1G55805.
DR KEGG; ath:AT1G55805; -.
DR Araport; AT1G55805; -.
DR TAIR; locus:505006189; AT1G55805.
DR eggNOG; KOG2313; Eukaryota.
DR HOGENOM; CLU_109462_2_0_1; -.
DR InParanoid; Q682I1; -.
DR OMA; NGFEGMN; -.
DR OrthoDB; 1603661at2759; -.
DR PhylomeDB; Q682I1; -.
DR PRO; PR:Q682I1; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q682I1; baseline and differential.
DR Genevisible; Q682I1; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.30.300.90; -; 1.
DR InterPro; IPR002634; BolA.
DR InterPro; IPR036065; BolA-like_sf.
DR Pfam; PF01722; BolA; 1.
DR SUPFAM; SSF82657; SSF82657; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; 3D-structure; Chloroplast; Iron; Iron-sulfur; Metal-binding;
KW Plastid; Reference proteome; Transit peptide.
FT TRANSIT 1..50
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 51..160
FT /note="Protein BOLA1, chloroplastic"
FT /evidence="ECO:0000255"
FT /id="PRO_0000432127"
FT REGION 39..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 11
FT /note="S -> T (in Ref. 4; AAK63866)"
FT /evidence="ECO:0000305"
FT HELIX 68..80
FT /evidence="ECO:0007829|PDB:4PUG"
FT STRAND 83..89
FT /evidence="ECO:0007829|PDB:4PUG"
FT HELIX 91..94
FT /evidence="ECO:0007829|PDB:4PUG"
FT TURN 98..103
FT /evidence="ECO:0007829|PDB:4PUG"
FT STRAND 109..115
FT /evidence="ECO:0007829|PDB:4PUG"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:4PUG"
FT HELIX 124..134
FT /evidence="ECO:0007829|PDB:4PUG"
FT HELIX 136..140
FT /evidence="ECO:0007829|PDB:4PUG"
FT STRAND 145..151
FT /evidence="ECO:0007829|PDB:4PUG"
FT TURN 153..155
FT /evidence="ECO:0007829|PDB:4PUG"
SQ SEQUENCE 160 AA; 17672 MW; BA509C5367B134F9 CRC64;
MFSSSIRLIV SGFHRTQPLK SPVNSPSVFI SVPKFFNSES KSTGTGSRSV AMSSVEKTGS
DSGAIENRAS RMREKLQKEL EPVELVIEDV SYQHAGHAGM KGRTDDETHF NVKIVSKGFE
GMNLVKRHRL VYHLLREELD TGLHALSIVS KTPSESPSKD
