BSD2_ARATH
ID BSD2_ARATH Reviewed; 136 AA.
AC Q9SN73; A0A178VHR7;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Protein BUNDLE SHEATH DEFECTIVE 2, chloroplastic {ECO:0000303|PubMed:29217567};
DE Short=AtBSD2 {ECO:0000303|PubMed:29217567};
DE Flags: Precursor;
GN Name=BSD2 {ECO:0000303|PubMed:29217567};
GN OrderedLocusNames=At3g47650 {ECO:0000312|Araport:AT3G47650};
GN ORFNames=F1P2.200 {ECO:0000312|EMBL:CAB61991.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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;
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 [4]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 57-136 IN COMPLEX WITH ZINC IONS
RP AND RBCL, FUNCTION, MUTAGENESIS OF 95-ASP--PHE-97; 100-GLN--LYS-102;
RP 108-TRP-LEU-109; 111-ARG--LYS-113 AND 117-LEU--GLY-119, AND INTERACTION
RP WITH RBCL.
RX PubMed=29217567; DOI=10.1126/science.aap9221;
RA Aigner H., Wilson R.H., Bracher A., Calisse L., Bhat J.Y., Hartl F.U.,
RA Hayer-Hartl M.;
RT "Plant RuBisCo assembly in E. coli with five chloroplast chaperones
RT including BSD2.";
RL Science 358:1272-1278(2017).
CC -!- FUNCTION: Chloroplast chaperone required for RuBisCo biogenesis and
CC translational regulation of the RuBisCo large subunit (RbcL)
CC (PubMed:29217567). Stabilizes an end-state assembly intermediate of
CC eight RbcL subunits until the small subunits (RBCSs) become available
CC to produce a complete stable RuBisCo complex containing eight small and
CC eight large subunits (PubMed:29217567). {ECO:0000269|PubMed:29217567}.
CC -!- SUBUNIT: Interacts with the RuBisCo large subunit (RbcL) assembled as
CC an intermediate complex made of eight RbcL and eight BSD2 subunits.
CC {ECO:0000269|PubMed:29217567}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000250|UniProtKB:Q9XF14}. Note=Associates with chloroplastic
CC polysomes. {ECO:0000250|UniProtKB:A0A2K3DZC4}.
CC -!- SIMILARITY: Belongs to the BSD2 chaperone family. {ECO:0000305}.
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DR EMBL; AL132955; CAB61991.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78314.1; -; Genomic_DNA.
DR EMBL; AF370246; AAK44061.1; -; mRNA.
DR EMBL; AY062972; AAL33818.1; -; mRNA.
DR PIR; T45725; T45725.
DR RefSeq; NP_190349.1; NM_114633.4.
DR PDB; 6EKB; X-ray; 1.90 A; A=57-136.
DR PDB; 6EKC; X-ray; 2.63 A; B1/B2/B3/B4/B5/B6/B7/B8/D1/D2/D3/D4/D5/D6/D7/D8/F1/F2/F3/F4/F5/F6/F7/F8/H1/H2/H3/H4/H5/H6=57-136.
DR PDBsum; 6EKB; -.
DR PDBsum; 6EKC; -.
DR AlphaFoldDB; Q9SN73; -.
DR SMR; Q9SN73; -.
DR STRING; 3702.AT3G47650.1; -.
DR PaxDb; Q9SN73; -.
DR PRIDE; Q9SN73; -.
DR ProteomicsDB; 185827; -.
DR EnsemblPlants; AT3G47650.1; AT3G47650.1; AT3G47650.
DR GeneID; 823919; -.
DR Gramene; AT3G47650.1; AT3G47650.1; AT3G47650.
DR KEGG; ath:AT3G47650; -.
DR Araport; AT3G47650; -.
DR TAIR; locus:2079132; AT3G47650.
DR eggNOG; ENOG502S25V; Eukaryota.
DR HOGENOM; CLU_152807_0_0_1; -.
DR InParanoid; Q9SN73; -.
DR OMA; ANFQSWE; -.
DR OrthoDB; 1528729at2759; -.
DR PhylomeDB; Q9SN73; -.
DR PRO; PR:Q9SN73; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SN73; baseline and differential.
DR GO; GO:0101031; C:chaperone complex; IDA:UniProtKB.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:1905538; F:polysome binding; IDA:UniProtKB.
DR GO; GO:0044183; F:protein folding chaperone; IDA:UniProtKB.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IDA:UniProtKB.
DR GO; GO:0110102; P:ribulose bisphosphate carboxylase complex assembly; IDA:UniProtKB.
DR InterPro; IPR036410; HSP_DnaJ_Cys-rich_dom_sf.
DR SUPFAM; SSF57938; SSF57938; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chaperone; Chloroplast; Metal-binding; Plastid;
KW Reference proteome; Repeat; Transit peptide; Zinc; Zinc-finger.
FT TRANSIT 1..56
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 57..136
FT /note="Protein BUNDLE SHEATH DEFECTIVE 2, chloroplastic"
FT /id="PRO_0000447230"
FT ZN_FING 62..133
FT /note="CR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00546"
FT BINDING 72
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:29217567,
FT ECO:0007744|PDB:6EKB, ECO:0007744|PDB:6EKC"
FT BINDING 75
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:29217567,
FT ECO:0007744|PDB:6EKB, ECO:0007744|PDB:6EKC"
FT BINDING 78
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:29217567,
FT ECO:0007744|PDB:6EKB"
FT BINDING 80
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:29217567,
FT ECO:0007744|PDB:6EKB"
FT BINDING 83
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:29217567,
FT ECO:0007744|PDB:6EKB, ECO:0007744|PDB:6EKC"
FT BINDING 86
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:29217567,
FT ECO:0007744|PDB:6EKB, ECO:0007744|PDB:6EKC"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:29217567,
FT ECO:0007744|PDB:6EKB, ECO:0007744|PDB:6EKC"
FT BINDING 110
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:29217567,
FT ECO:0007744|PDB:6EKB, ECO:0007744|PDB:6EKC"
FT BINDING 115
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:29217567,
FT ECO:0007744|PDB:6EKB"
FT BINDING 118
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:29217567,
FT ECO:0007744|PDB:6EKB, ECO:0007744|PDB:6EKC"
FT BINDING 121
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:29217567,
FT ECO:0007744|PDB:6EKB, ECO:0007744|PDB:6EKC"
FT MUTAGEN 95..97
FT /note="DHF->NHS: No visible impact on chaperone function."
FT /evidence="ECO:0000269|PubMed:29217567"
FT MUTAGEN 100..102
FT /note="QFK->EAA: No visible impact on chaperone function."
FT /evidence="ECO:0000269|PubMed:29217567"
FT MUTAGEN 108..109
FT /note="WL->AE: Impaired chaperone function leading to
FT altered stabilization of RbcL complexes and reduction of
FT assembled RuBisCo."
FT /evidence="ECO:0000269|PubMed:29217567"
FT MUTAGEN 111..113
FT /note="RGK->EGE: Impaired chaperone function leading to
FT altered stabilization of RbcL complexes and reduction of
FT assembled RuBisCo."
FT /evidence="ECO:0000269|PubMed:29217567"
FT MUTAGEN 117..119
FT /note="LCG->ECT: Impaired chaperone function leading to
FT altered stabilization of RbcL complexes and reduction of
FT assembled RuBisCo."
FT /evidence="ECO:0000269|PubMed:29217567"
FT TURN 73..77
FT /evidence="ECO:0007829|PDB:6EKB"
FT STRAND 79..82
FT /evidence="ECO:0007829|PDB:6EKB"
FT TURN 84..88
FT /evidence="ECO:0007829|PDB:6EKB"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:6EKB"
FT TURN 108..112
FT /evidence="ECO:0007829|PDB:6EKB"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:6EKB"
FT TURN 119..123
FT /evidence="ECO:0007829|PDB:6EKB"
FT STRAND 124..127
FT /evidence="ECO:0007829|PDB:6EKB"
SQ SEQUENCE 136 AA; 14546 MW; D491656FFB0354A0 CRC64;
MANSLCFFSS PPTFCFQSPS KNPKPSHFFS TNDNTSSLVQ KRELLQTSRS QSFEVKAANN
NPQGTKPNSL VCANCEGEGC VACSQCKGGG VNLIDHFNGQ FKAGALCWLC RGKKEVLCGD
CNGAGFIGGF LSTFDE
