ID   FTSH_POPEU              Reviewed;          47 AA.
AC   P84578;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 50.
DE   RecName: Full=ATP-dependent zinc metalloprotease FTSH, chloroplastic;
DE            EC=3.4.24.-;
DE   Flags: Fragments;
OS   Populus euphratica (Euphrates poplar).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Salicaceae; Saliceae; Populus.
OX   NCBI_TaxID=75702;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Leaf;
RX   PubMed=16740589; DOI=10.1093/aob/mcl106;
RA   Ferreira S., Hjernoe K., Larsen M., Wingsle G., Larsen P., Fey S.,
RA   Roepstorff P., Pais M.S.;
RT   "Proteome profiling of Populus euphratica Oliv. upon heat stress.";
RL   Ann. Bot. 98:361-377(2006).
CC   -!- FUNCTION: Seems to act as an ATP-dependent zinc metallopeptidase.
CC       {ECO:0000250|UniProtKB:P28691}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000305};
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane {ECO:0000250};
CC       Multi-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the AAA ATPase
CC       family. {ECO:0000255}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the peptidase M41
CC       family. {ECO:0000255}.
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DR   AlphaFoldDB; P84578; -.
DR   SMR; P84578; -.
DR   GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR041569; AAA_lid_3.
DR   Pfam; PF17862; AAA_lid_3; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell cycle; Cell division; Chloroplast;
KW   Direct protein sequencing; Hydrolase; Membrane; Metal-binding;
KW   Metalloprotease; Nucleotide-binding; Plastid; Protease; Zinc.
FT   CHAIN           <1..>47
FT                   /note="ATP-dependent zinc metalloprotease FTSH,
FT                   chloroplastic"
FT                   /id="PRO_0000084663"
FT   NON_CONS        9..10
FT                   /evidence="ECO:0000305"
FT   NON_CONS        24..25
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
FT   NON_TER         47
SQ   SEQUENCE   47 AA;  5198 MW;  15D3259A9F2075D6 CRC64;
     FLEYLDKDRV RVQLPGLSQE LLQKTPGFSG ADLANLLNEA AILAGRR