ID   CPP1_NICBE              Reviewed;         252 AA.
AC   G5DBJ0;
DT   29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2011, sequence version 1.
DT   25-MAY-2022, entry version 15.
DE   RecName: Full=Protein CHAPERONE-LIKE PROTEIN OF POR1, chloroplastic {ECO:0000303|PubMed:24151298};
DE            Short=NbCPP1 {ECO:0000303|PubMed:24151298};
DE   Flags: Precursor;
GN   Name=CPP1 {ECO:0000303|PubMed:24151298};
OS   Nicotiana benthamiana.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=4100 {ECO:0000312|EMBL:AEP68099.1};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, SUBUNIT,
RP   DISRUPTION PHENOTYPE, INTERACTION WITH POR1 AND POR2, AND J-LIKE DOMAIN.
RX   PubMed=24151298; DOI=10.1105/tpc.113.111096;
RA   Lee J.-Y., Lee H.-S., Song J.-Y., Jung Y.J., Reinbothe S., Park Y.-I.,
RA   Lee S.Y., Pai H.-S.;
RT   "Cell growth defect factor1/chaperone-like protein of POR1 plays a role in
RT   stabilization of light-dependent protochlorophyllide oxidoreductase in
RT   Nicotiana benthamiana and Arabidopsis.";
RL   Plant Cell 25:3944-3960(2013).
CC   -!- FUNCTION: Exhibits holdase chaperone activity involved in the
CC       stabilization of POR proteins against photooxidative stress in
CC       chloroplasts. Required for chloroplast development.
CC       {ECO:0000269|PubMed:24151298}.
CC   -!- SUBUNIT: Interacts with POR1 and POR2 in chloroplast.
CC       {ECO:0000269|PubMed:24151298}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast envelope
CC       {ECO:0000269|PubMed:24151298}. Plastid, chloroplast thylakoid membrane
CC       {ECO:0000269|PubMed:24151298}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- DISRUPTION PHENOTYPE: Reduced chloroplast biogenesis and chlorophyll
CC       synthesis associated with less POR protein accumulation.
CC       {ECO:0000269|PubMed:24151298}.
CC   -!- SIMILARITY: Belongs to the chaperone-like protein of POR1 protein
CC       family. {ECO:0000305}.
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DR   EMBL; JN609462; AEP68099.1; -; mRNA.
DR   AlphaFoldDB; G5DBJ0; -.
DR   SMR; G5DBJ0; -.
DR   GO; GO:0009941; C:chloroplast envelope; IDA:UniProtKB.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0055035; C:plastid thylakoid membrane; 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:0009658; P:chloroplast organization; IMP:UniProtKB.
DR   GO; GO:0009704; P:de-etiolation; IMP:UniProtKB.
DR   GO; GO:0006457; P:protein folding; IDA:UniProtKB.
DR   InterPro; IPR021788; CPP1-like.
DR   PANTHER; PTHR33372; PTHR33372; 1.
DR   Pfam; PF11833; CPP1-like; 1.
PE   1: Evidence at protein level;
KW   Chaperone; Chloroplast; Membrane; Plastid; Thylakoid; Transit peptide;
KW   Transmembrane; Transmembrane helix.
FT   TRANSIT         1..40
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           41..252
FT                   /note="Protein CHAPERONE-LIKE PROTEIN OF POR1,
FT                   chloroplastic"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000432769"
FT   TRANSMEM        156..176
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        201..221
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        231..251
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   REGION          61..116
FT                   /note="J-like domain required for holdase chaperone
FT                   activity"
FT                   /evidence="ECO:0000269|PubMed:24151298"
SQ   SEQUENCE   252 AA;  28174 MW;  173B6A8587F5C69E CRC64;
     MATTLISKLT LSSAFLGQQF SSRGNSMRSA PAGLFLRGPR CAATDTPYGG NIPQFPRVNV
     WDPYKRLGIS RDASEEEVWS SRNFLLNQYY NHERSAESIE AAFEKILMAS FINRKKTKIN
     LKTRLKKKVE ESPPWVQNLL SFVELPPPVI ILRRLFLFGF MACWSVMNST EAGPAFQVAI
     SFGACVYFLN DKTKSLGRAA LIGFGALVAG WFCGSLLVPM IPPNLLHPTW SLELLTSLFI
     YVSLFLGCTF LK