FKB13_ARATH
ID FKB13_ARATH Reviewed; 208 AA.
AC Q9SCY2; Q8M8T4;
DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase FKBP13, chloroplastic {ECO:0000303|PubMed:12424338};
DE Short=PPIase FKBP13 {ECO:0000303|PubMed:12424338};
DE EC=5.2.1.8 {ECO:0000305};
DE AltName: Full=FK506-binding protein 1;
DE AltName: Full=FK506-binding protein 13 {ECO:0000303|PubMed:12424338};
DE Short=AtFKBP13 {ECO:0000303|PubMed:12424338};
DE AltName: Full=Immunophilin FKBP13 {ECO:0000303|PubMed:15047905};
DE AltName: Full=Rotamase;
DE Flags: Precursor;
GN Name=FKBP13 {ECO:0000303|PubMed:12424338};
GN Synonyms=FKBP22-1 {ECO:0000305|PubMed:15047905}, FKBPK;
GN OrderedLocusNames=At5g45680 {ECO:0000312|Araport:AT5G45680};
GN ORFNames=MRA19.7 {ECO:0000312|EMBL:BAB09210.1};
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=12424338; DOI=10.1073/pnas.222550399;
RA Gupta R., Mould R.M., He Z., Luan S.;
RT "A chloroplast FKBP interacts with and affects the accumulation of Rieske
RT subunit of cytochrome bf complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:15806-15811(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9734815; DOI=10.1093/dnares/5.3.203;
RA Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT features of the regions of 1,367,185 bp covered by 19 physically assigned
RT P1 and TAC clones.";
RL DNA Res. 5:203-216(1998).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 NUCLEOTIDE SEQUENCE [MRNA] OF 101-176.
RC STRAIN=cv. Columbia;
RA Kolukisaoglu U., Billion K., Eckhoff A., Moeller A., Saal B., Wanke D.,
RA Schulz B.;
RT "Structure and evolution of FKBP-like genes in Arabidopsis.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PROTEIN SEQUENCE OF 80-99, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=11719511; DOI=10.1074/jbc.m108575200;
RA Schubert M., Petersson U.A., Haas B.J., Funk C., Schroeder W.P.,
RA Kieselbach T.;
RT "Proteome map of the chloroplast lumen of Arabidopsis thaliana.";
RL J. Biol. Chem. 277:8354-8365(2002).
RN [7]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=15047905; DOI=10.1104/pp.103.031005;
RA He Z., Li L., Luan S.;
RT "Immunophilins and parvulins. Superfamily of peptidyl prolyl isomerases in
RT Arabidopsis.";
RL Plant Physiol. 134:1248-1267(2004).
RN [8]
RP FUNCTION.
RX PubMed=16765949; DOI=10.1016/j.febslet.2006.05.054;
RA Shapiguzov A., Edvardsson A., Vener A.V.;
RT "Profound redox sensitivity of peptidyl-prolyl isomerase activity in
RT Arabidopsis thylakoid lumen.";
RL FEBS Lett. 580:3671-3676(2006).
RN [9]
RP FUNCTION.
RX PubMed=17655280; DOI=10.1021/bi700426q;
RA Edvardsson A., Shapiguzov A., Petersson U.A., Schroder W.P., Vener A.V.;
RT "Immunophilin AtFKBP13 sustains all peptidyl-prolyl isomerase activity in
RT the thylakoid lumen from Arabidopsis thaliana deficient in AtCYP20-2.";
RL Biochemistry 46:9432-9442(2007).
RN [10]
RP FUNCTION.
RX PubMed=19717822; DOI=10.1093/pcp/pcp122;
RA Ingelsson B., Shapiguzov A., Kieselbach T., Vener A.V.;
RT "Peptidyl-prolyl isomerase activity in chloroplast thylakoid lumen is a
RT dispensable function of immunophilins in Arabidopsis thaliana.";
RL Plant Cell Physiol. 50:1801-1814(2009).
RN [11]
RP INTERACTION WITH LTO1.
RX PubMed=25412899; DOI=10.2174/0929866521666141121153138;
RA Lu Y., Du J.J., Yu Z.B., Peng J.J., Xu J.N., Wang X.Y.;
RT "Identification of potential targets for thylakoid oxidoreductase
RT AtVKOR/LTO1 in chloroplasts.";
RL Protein Pept. Lett. 22:219-225(2014).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 80-208, ACTIVITY REGULATION,
RP DISULFIDE BONDS, AND MUTAGENESIS OF CYS-84; CYS-96; CYS-185 AND CYS-190.
RX PubMed=15356344; DOI=10.1073/pnas.0405240101;
RA Gopalan G., He Z., Balmer Y., Romano P., Gupta R., Heroux A.,
RA Buchanan B.B., Swaminathan K., Luan S.;
RT "Structural analysis uncovers a role for redox in regulating FKBP13, an
RT immunophilin of the chloroplast thylakoid lumen.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:13945-13950(2004).
CC -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC cis-trans isomerization of proline imidic peptide bonds in
CC oligopeptides. Responsive of the major PPIase activity in the
CC chloroplast thylakoid lumen. Regulates the accumulation of Rieske
CC protein, an essential component of the photosynthetic electron
CC transport chain. {ECO:0000269|PubMed:16765949,
CC ECO:0000269|PubMed:17655280, ECO:0000269|PubMed:19717822}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-peptidylproline (omega=180) = [protein]-
CC peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
CC COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
CC ChEBI:CHEBI:83834; EC=5.2.1.8; Evidence={ECO:0000305};
CC -!- ACTIVITY REGULATION: PPIase activity is optimal in oxidized form (S-S)
CC and minimal in reduced form (SH). Reduction of the oxidized form is
CC mediated by thioredoxin (TRX-M). {ECO:0000269|PubMed:15356344}.
CC -!- SUBUNIT: Interacts in vitro with LTO1 (PubMed:25412899). The precursor,
CC but not the mature form of the protein, interacts with the Rieske
CC protein. {ECO:0000269|PubMed:25412899}.
CC -!- INTERACTION:
CC Q9SCY2; O23160: MYB73; NbExp=3; IntAct=EBI-2895757, EBI-25506855;
CC Q9SCY2; P0AA25: trxA; Xeno; NbExp=2; IntAct=EBI-2895757, EBI-368542;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid lumen
CC {ECO:0000269|PubMed:11719511}.
CC -!- TISSUE SPECIFICITY: Expressed in stems, leaves and developing flower
CC buds, but not in roots.
CC -!- MISCELLANEOUS: The interaction between FKBP and the Rieske protein
CC probably occurs before they are imported into the thylakoid.
CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family. {ECO:0000305}.
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DR EMBL; AJ490171; CAD35362.1; -; mRNA.
DR EMBL; AB012245; BAB09210.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95283.1; -; Genomic_DNA.
DR EMBL; AY065047; AAL57682.1; -; mRNA.
DR EMBL; AY091680; AAM10279.1; -; mRNA.
DR EMBL; AJ242483; CAB64723.1; -; mRNA.
DR RefSeq; NP_199380.1; NM_123935.5.
DR PDB; 1U79; X-ray; 1.85 A; A/B/C/D/E=80-208.
DR PDB; 1Y0O; X-ray; 1.89 A; A/B/C/D/E=80-208.
DR PDBsum; 1U79; -.
DR PDBsum; 1Y0O; -.
DR AlphaFoldDB; Q9SCY2; -.
DR SMR; Q9SCY2; -.
DR BioGRID; 19856; 3.
DR IntAct; Q9SCY2; 2.
DR STRING; 3702.AT5G45680.1; -.
DR PaxDb; Q9SCY2; -.
DR PRIDE; Q9SCY2; -.
DR ProteomicsDB; 230582; -.
DR EnsemblPlants; AT5G45680.1; AT5G45680.1; AT5G45680.
DR GeneID; 834607; -.
DR Gramene; AT5G45680.1; AT5G45680.1; AT5G45680.
DR KEGG; ath:AT5G45680; -.
DR Araport; AT5G45680; -.
DR TAIR; locus:2171958; AT5G45680.
DR eggNOG; KOG0549; Eukaryota.
DR HOGENOM; CLU_013615_10_0_1; -.
DR InParanoid; Q9SCY2; -.
DR OMA; ETTSCEF; -.
DR OrthoDB; 1328688at2759; -.
DR PhylomeDB; Q9SCY2; -.
DR BRENDA; 5.2.1.8; 399.
DR EvolutionaryTrace; Q9SCY2; -.
DR PRO; PR:Q9SCY2; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9SCY2; baseline and differential.
DR Genevisible; Q9SCY2; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009543; C:chloroplast thylakoid lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0031977; C:thylakoid lumen; HDA:TAIR.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IDA:TAIR.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IEA:InterPro.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IEA:InterPro.
DR Gene3D; 3.10.50.40; -; 1.
DR InterPro; IPR044609; FKBP2/11.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR001179; PPIase_FKBP_dom.
DR PANTHER; PTHR45779; PTHR45779; 1.
DR Pfam; PF00254; FKBP_C; 1.
DR PROSITE; PS50059; FKBP_PPIASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chloroplast; Direct protein sequencing; Disulfide bond;
KW Isomerase; Plastid; Reference proteome; Rotamase; Thylakoid;
KW Transit peptide.
FT TRANSIT 1..?
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT TRANSIT ?..79
FT /note="Thylakoid"
FT /evidence="ECO:0000269|PubMed:11719511"
FT CHAIN 80..208
FT /note="Peptidyl-prolyl cis-trans isomerase FKBP13,
FT chloroplastic"
FT /id="PRO_0000025526"
FT DOMAIN 109..208
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT DISULFID 84..96
FT /evidence="ECO:0000269|PubMed:15356344"
FT DISULFID 185..190
FT /evidence="ECO:0000269|PubMed:15356344"
FT MUTAGEN 84
FT /note="C->S: Reduced PPIase activity; when associated with
FT S-96."
FT /evidence="ECO:0000269|PubMed:15356344"
FT MUTAGEN 96
FT /note="C->S: Reduced PPIase activity; when associated with
FT S-84."
FT /evidence="ECO:0000269|PubMed:15356344"
FT MUTAGEN 185
FT /note="C->S: Reduced PPIase activity; when associated with
FT S-190."
FT /evidence="ECO:0000269|PubMed:15356344"
FT MUTAGEN 190
FT /note="C->S: Reduced PPIase activity; when associated with
FT S-185."
FT /evidence="ECO:0000269|PubMed:15356344"
FT CONFLICT 7
FT /note="S -> T (in Ref. 1; CAD35362)"
FT /evidence="ECO:0000305"
FT STRAND 94..99
FT /evidence="ECO:0007829|PDB:1U79"
FT STRAND 111..119
FT /evidence="ECO:0007829|PDB:1U79"
FT STRAND 125..128
FT /evidence="ECO:0007829|PDB:1U79"
FT HELIX 129..132
FT /evidence="ECO:0007829|PDB:1U79"
FT STRAND 136..139
FT /evidence="ECO:0007829|PDB:1U79"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:1U79"
FT HELIX 147..154
FT /evidence="ECO:0007829|PDB:1U79"
FT STRAND 167..172
FT /evidence="ECO:0007829|PDB:1U79"
FT HELIX 174..176
FT /evidence="ECO:0007829|PDB:1U79"
FT TURN 177..181
FT /evidence="ECO:0007829|PDB:1U79"
FT STRAND 183..186
FT /evidence="ECO:0007829|PDB:1U79"
FT STRAND 189..192
FT /evidence="ECO:0007829|PDB:1U79"
FT STRAND 198..207
FT /evidence="ECO:0007829|PDB:1U79"
SQ SEQUENCE 208 AA; 22039 MW; 4E6640FE7955A48F CRC64;
MSSLGFSVGT CSPPSEKRKC RFLVNNSLNK AEAINLRNKQ KVSSDPELSF AQLSSCGRRE
AIIGFGFSIG LLDNVSALAE TTSCEFSVSP SGLAFCDKVV GYGPEAVKGQ LIKAHYVGKL
ENGKVFDSSY NRGKPLTFRI GVGEVIKGWD QGILGSDGIP PMLTGGKRTL RIPPELAYGD
RGAGCKGGSC LIPPASVLLF DIEYIGKA
