ID   FER_CAPAN               Reviewed;         144 AA.
AC   Q9ZTS2;
DT   19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Ferredoxin, chloroplastic;
DE   AltName: Full=PFLP;
DE   Flags: Precursor;
GN   Name=AP1;
OS   Capsicum annuum (Capsicum pepper).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Capsiceae; Capsicum.
OX   NCBI_TaxID=4072 {ECO:0000312|EMBL:AAD02175.1};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP   PHOSPHORYLATION AT THR-136.
RC   STRAIN=cv. ECW; TISSUE=Leaf;
RX   PubMed=12777051; DOI=10.1023/a:1023061303755;
RA   Dayakar B.V., Lin H.-J., Chen C.-H., Ger M.-J., Lee B.-H., Pai C.-H.,
RA   Chow D., Huang H.-E., Hwang S.-Y., Chung M.-C., Feng T.-Y.;
RT   "Ferredoxin from sweet pepper (Capsicum annuum L.) intensifying
RT   harpin(pss)-mediated hypersensitive response shows an enhanced production
RT   of active oxygen species (AOS).";
RL   Plant Mol. Biol. 51:913-924(2003).
CC   -!- FUNCTION: Ferredoxins are iron-sulfur proteins that transfer electrons
CC       in a wide variety of metabolic reactions.
CC       {ECO:0000250|UniProtKB:Q43517}.
CC   -!- FUNCTION: Delays the harpin-mediated hypersensitive response.
CC       {ECO:0000269|PubMed:12777051, ECO:0000305}.
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000255|RuleBase:RU000392, ECO:0000305};
CC       Note=Binds 1 [2Fe-2S] cluster. {ECO:0000255|RuleBase:RU000392,
CC       ECO:0000305};
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC       {ECO:0000269|PubMed:12777051}.
CC   -!- SIMILARITY: Belongs to the 2Fe2S plant-type ferredoxin family.
CC       {ECO:0000305}.
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DR   EMBL; AF039662; AAD02175.1; -; mRNA.
DR   AlphaFoldDB; Q9ZTS2; -.
DR   SMR; Q9ZTS2; -.
DR   iPTMnet; Q9ZTS2; -.
DR   Proteomes; UP000189700; Genome assembly.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006124; P:ferredoxin metabolic process; IEA:UniProt.
DR   CDD; cd00207; fer2; 1.
DR   Gene3D; 3.10.20.30; -; 1.
DR   InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR   InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR   InterPro; IPR006058; 2Fe2S_fd_BS.
DR   InterPro; IPR012675; Beta-grasp_dom_sf.
DR   InterPro; IPR010241; Fd_pln.
DR   Pfam; PF00111; Fer2; 1.
DR   SUPFAM; SSF54292; SSF54292; 1.
DR   TIGRFAMs; TIGR02008; fdx_plant; 1.
DR   PROSITE; PS00197; 2FE2S_FER_1; 1.
DR   PROSITE; PS51085; 2FE2S_FER_2; 1.
PE   1: Evidence at protein level;
KW   2Fe-2S; Chloroplast; Electron transport; Iron; Iron-sulfur; Metal-binding;
KW   Phosphoprotein; Plastid; Transit peptide; Transport.
FT   TRANSIT         1..47
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000250"
FT   CHAIN           48..144
FT                   /note="Ferredoxin, chloroplastic"
FT                   /id="PRO_0000008827"
FT   DOMAIN          50..140
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         86
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         91
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         94
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         124
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   MOD_RES         136
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:12777051"
SQ   SEQUENCE   144 AA;  15178 MW;  E9763663281D58EB CRC64;
     MASVSATMIS TSFMPRKPAV TSLKPIPNVG EALFGLKSAN GGKVTCMASY KVKLITPDGP
     IEFDCPDNVY ILDQAEEAGH DLPYSCRAGS CSSCAGKIAG GAVDQTDGNF LDDDQLEEGW
     VLTCVAYPQS DVTIETHKEA ELVG