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Peptidyl-prolyl cis-trans isomerase FKBP13, chloroplastic (PPIase FKBP13) (EC 5.2.1.8) (FK506-binding protein 1) (FK506-binding protein 13) (AtFKBP13) (Immunophilin FKBP13) (Rotamase)

 FKB13_ARATH             Reviewed;         208 AA.
Q9SCY2; Q8M8T4;
20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 2.
05-DEC-2018, entry version 133.
RecName: Full=Peptidyl-prolyl cis-trans isomerase FKBP13, chloroplastic {ECO:0000303|PubMed:12424338};
Short=PPIase FKBP13 {ECO:0000303|PubMed:12424338};
EC=5.2.1.8 {ECO:0000305};
AltName: Full=FK506-binding protein 1;
AltName: Full=FK506-binding protein 13 {ECO:0000303|PubMed:12424338};
Short=AtFKBP13 {ECO:0000303|PubMed:12424338};
AltName: Full=Immunophilin FKBP13 {ECO:0000303|PubMed:15047905};
AltName: Full=Rotamase;
Flags: Precursor;
Name=FKBP13 {ECO:0000303|PubMed:12424338};
Synonyms=FKBP22-1 {ECO:0000305|PubMed:15047905}, FKBPK;
OrderedLocusNames=At5g45680 {ECO:0000312|Araport:AT5G45680};
ORFNames=MRA19.7 {ECO:0000312|EMBL:BAB09210.1};
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Columbia;
PubMed=12424338; DOI=10.1073/pnas.222550399;
Gupta R., Mould R.M., He Z., Luan S.;
"A chloroplast FKBP interacts with and affects the accumulation of
Rieske subunit of cytochrome bf complex.";
Proc. Natl. Acad. Sci. U.S.A. 99:15806-15811(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=9734815; DOI=10.1093/dnares/5.3.203;
Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 5. VI.
Sequence features of the regions of 1,367,185 bp covered by 19
physically assigned P1 and TAC clones.";
DNA Res. 5:203-216(1998).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 101-176.
STRAIN=cv. Columbia;
Kolukisaoglu U., Billion K., Eckhoff A., Moeller A., Saal B.,
Wanke D., Schulz B.;
"Structure and evolution of FKBP-like genes in Arabidopsis.";
Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
[6]
PROTEIN SEQUENCE OF 80-99, AND SUBCELLULAR LOCATION.
STRAIN=cv. Columbia;
PubMed=11719511; DOI=10.1074/jbc.M108575200;
Schubert M., Petersson U.A., Haas B.J., Funk C., Schroeder W.P.,
Kieselbach T.;
"Proteome map of the chloroplast lumen of Arabidopsis thaliana.";
J. Biol. Chem. 277:8354-8365(2002).
[7]
GENE FAMILY, AND NOMENCLATURE.
PubMed=15047905; DOI=10.1104/pp.103.031005;
He Z., Li L., Luan S.;
"Immunophilins and parvulins. Superfamily of peptidyl prolyl
isomerases in Arabidopsis.";
Plant Physiol. 134:1248-1267(2004).
[8]
FUNCTION.
PubMed=16765949; DOI=10.1016/j.febslet.2006.05.054;
Shapiguzov A., Edvardsson A., Vener A.V.;
"Profound redox sensitivity of peptidyl-prolyl isomerase activity in
Arabidopsis thylakoid lumen.";
FEBS Lett. 580:3671-3676(2006).
[9]
FUNCTION.
PubMed=17655280; DOI=10.1021/bi700426q;
Edvardsson A., Shapiguzov A., Petersson U.A., Schroder W.P.,
Vener A.V.;
"Immunophilin AtFKBP13 sustains all peptidyl-prolyl isomerase activity
in the thylakoid lumen from Arabidopsis thaliana deficient in AtCYP20-
2.";
Biochemistry 46:9432-9442(2007).
[10]
FUNCTION.
PubMed=19717822; DOI=10.1093/pcp/pcp122;
Ingelsson B., Shapiguzov A., Kieselbach T., Vener A.V.;
"Peptidyl-prolyl isomerase activity in chloroplast thylakoid lumen is
a dispensable function of immunophilins in Arabidopsis thaliana.";
Plant Cell Physiol. 50:1801-1814(2009).
[11]
INTERACTION WITH LTO1.
PubMed=25412899;
Lu Y., Du J.J., Yu Z.B., Peng J.J., Xu J.N., Wang X.Y.;
"Identification of potential targets for thylakoid oxidoreductase
AtVKOR/LTO1 in chloroplasts.";
Protein Pept. Lett. 22:219-225(2014).
[12]
X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 80-208, ACTIVITY REGULATION,
DISULFIDE BONDS, AND MUTAGENESIS OF CYS-84; CYS-96; CYS-185 AND
CYS-190.
PubMed=15356344; DOI=10.1073/pnas.0405240101;
Gopalan G., He Z., Balmer Y., Romano P., Gupta R., Heroux A.,
Buchanan B.B., Swaminathan K., Luan S.;
"Structural analysis uncovers a role for redox in regulating FKBP13,
an immunophilin of the chloroplast thylakoid lumen.";
Proc. Natl. Acad. Sci. U.S.A. 101:13945-13950(2004).
-!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes
the cis-trans isomerization of proline imidic peptide bonds in
oligopeptides. Responsive of the major PPIase activity in the
chloroplast thylakoid lumen. Regulates the accumulation of Rieske
protein, an essential component of the photosynthetic electron
transport chain. {ECO:0000269|PubMed:16765949,
ECO:0000269|PubMed:17655280, ECO:0000269|PubMed:19717822}.
-!- CATALYTIC ACTIVITY:
Reaction=[protein]-peptidylproline (omega=180) = [protein]-
peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
ChEBI:CHEBI:83834; EC=5.2.1.8; Evidence={ECO:0000305};
-!- ACTIVITY REGULATION: PPIase activity is optimal in oxidized form
(S-S) and minimal in reduced form (SH). Reduction of the oxidized
form is mediated by thioredoxin (TRX-M).
{ECO:0000269|PubMed:15356344}.
-!- SUBUNIT: Interacts in vitro with LTO1 (PubMed:25412899). The
precursor, but not the mature form of the protein, interacts with
the Rieske protein. {ECO:0000269|PubMed:25412899}.
-!- INTERACTION:
P0AA25:trxA (xeno); NbExp=2; IntAct=EBI-2895757, EBI-368542;
-!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid lumen
{ECO:0000269|PubMed:11719511}.
-!- TISSUE SPECIFICITY: Expressed in stems, leaves and developing
flower buds, but not in roots.
-!- MISCELLANEOUS: The interaction between FKBP and the Rieske protein
probably occurs before they are imported into the thylakoid.
-!- SIMILARITY: Belongs to the FKBP-type PPIase family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AJ490171; CAD35362.1; -; mRNA.
EMBL; AB012245; BAB09210.1; -; Genomic_DNA.
EMBL; CP002688; AED95283.1; -; Genomic_DNA.
EMBL; AY065047; AAL57682.1; -; mRNA.
EMBL; AY091680; AAM10279.1; -; mRNA.
EMBL; AJ242483; CAB64723.1; -; mRNA.
RefSeq; NP_199380.1; NM_123935.5.
UniGene; At.28277; -.
PDB; 1U79; X-ray; 1.85 A; A/B/C/D/E=80-208.
PDB; 1Y0O; X-ray; 1.89 A; A/B/C/D/E=80-208.
PDBsum; 1U79; -.
PDBsum; 1Y0O; -.
ProteinModelPortal; Q9SCY2; -.
SMR; Q9SCY2; -.
BioGrid; 19856; 2.
IntAct; Q9SCY2; 1.
STRING; 3702.AT5G45680.1; -.
PaxDb; Q9SCY2; -.
PRIDE; Q9SCY2; -.
EnsemblPlants; AT5G45680.1; AT5G45680.1; AT5G45680.
GeneID; 834607; -.
Gramene; AT5G45680.1; AT5G45680.1; AT5G45680.
KEGG; ath:AT5G45680; -.
Araport; AT5G45680; -.
TAIR; locus:2171958; AT5G45680.
eggNOG; KOG0549; Eukaryota.
eggNOG; COG0545; LUCA.
HOGENOM; HOG000154887; -.
InParanoid; Q9SCY2; -.
KO; K01802; -.
OMA; ETTSCEF; -.
OrthoDB; EOG09360OGI; -.
PhylomeDB; Q9SCY2; -.
BRENDA; 5.2.1.8; 399.
EvolutionaryTrace; Q9SCY2; -.
PRO; PR:Q9SCY2; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; Q9SCY2; baseline and differential.
Genevisible; Q9SCY2; AT.
GO; GO:0009507; C:chloroplast; IDA:TAIR.
GO; GO:0009543; C:chloroplast thylakoid lumen; IEA:UniProtKB-SubCell.
GO; GO:0031977; C:thylakoid lumen; IDA:TAIR.
GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IDA:TAIR.
InterPro; IPR023566; PPIase_FKBP.
InterPro; IPR001179; PPIase_FKBP_dom.
PANTHER; PTHR10516; PTHR10516; 1.
Pfam; PF00254; FKBP_C; 1.
PROSITE; PS50059; FKBP_PPIASE; 1.
1: Evidence at protein level;
3D-structure; Chloroplast; Complete proteome;
Direct protein sequencing; Disulfide bond; Isomerase; Plastid;
Reference proteome; Rotamase; Thylakoid; Transit peptide.
TRANSIT 1 ? Chloroplast. {ECO:0000255}.
TRANSIT ? 79 Thylakoid. {ECO:0000269|PubMed:11719511}.
CHAIN 80 208 Peptidyl-prolyl cis-trans isomerase
FKBP13, chloroplastic.
/FTId=PRO_0000025526.
DOMAIN 109 208 PPIase FKBP-type. {ECO:0000255|PROSITE-
ProRule:PRU00277}.
DISULFID 84 96 {ECO:0000269|PubMed:15356344}.
DISULFID 185 190 {ECO:0000269|PubMed:15356344}.
MUTAGEN 84 84 C->S: Reduced PPIase activity; when
associated with S-96.
{ECO:0000269|PubMed:15356344}.
MUTAGEN 96 96 C->S: Reduced PPIase activity; when
associated with S-84.
{ECO:0000269|PubMed:15356344}.
MUTAGEN 185 185 C->S: Reduced PPIase activity; when
associated with S-190.
{ECO:0000269|PubMed:15356344}.
MUTAGEN 190 190 C->S: Reduced PPIase activity; when
associated with S-185.
{ECO:0000269|PubMed:15356344}.
CONFLICT 7 7 S -> T (in Ref. 1; CAD35362).
{ECO:0000305}.
STRAND 94 99 {ECO:0000244|PDB:1U79}.
STRAND 111 119 {ECO:0000244|PDB:1U79}.
STRAND 125 128 {ECO:0000244|PDB:1U79}.
HELIX 129 132 {ECO:0000244|PDB:1U79}.
STRAND 136 139 {ECO:0000244|PDB:1U79}.
STRAND 142 145 {ECO:0000244|PDB:1U79}.
HELIX 147 154 {ECO:0000244|PDB:1U79}.
STRAND 167 172 {ECO:0000244|PDB:1U79}.
HELIX 174 176 {ECO:0000244|PDB:1U79}.
TURN 177 181 {ECO:0000244|PDB:1U79}.
STRAND 183 186 {ECO:0000244|PDB:1U79}.
STRAND 189 192 {ECO:0000244|PDB:1U79}.
STRAND 198 207 {ECO:0000244|PDB:1U79}.
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


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