ID   FTSH_CAPAN              Reviewed;         662 AA.
AC   Q39444;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=ATP-dependent zinc metalloprotease FTSH, chloroplastic;
DE            EC=3.4.24.-;
DE   Flags: Precursor; Fragment;
GN   Name=FTSH;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Houlne G., Schantz M.L., Schantz R.;
RL   Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Seems to act as an ATP-dependent zinc metallopeptidase.
CC       {ECO:0000250}.
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:0000305};
CC       Multi-pass membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the AAA ATPase
CC       family. {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the peptidase M41
CC       family. {ECO:0000305}.
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DR   EMBL; X90472; CAA62084.1; -; mRNA.
DR   PIR; S58298; S58298.
DR   AlphaFoldDB; Q39444; -.
DR   SMR; Q39444; -.
DR   MEROPS; M41.020; -.
DR   PRIDE; Q39444; -.
DR   Proteomes; UP000189700; Genome assembly.
DR   GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
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   Gene3D; 1.20.58.760; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_01458; FtsH; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR041569; AAA_lid_3.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR003960; ATPase_AAA_CS.
DR   InterPro; IPR005936; FtsH.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000642; Peptidase_M41.
DR   InterPro; IPR037219; Peptidase_M41-like.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF17862; AAA_lid_3; 1.
DR   Pfam; PF01434; Peptidase_M41; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF140990; SSF140990; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR01241; FtsH_fam; 1.
DR   PROSITE; PS00674; AAA; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Cell cycle; Cell division; Chloroplast; Hydrolase; Membrane;
KW   Metal-binding; Metalloprotease; Nucleotide-binding; Plastid; Protease;
KW   Transit peptide; Transmembrane; Transmembrane helix; Zinc.
FT   TRANSIT         <1..?
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..662
FT                   /note="ATP-dependent zinc metalloprotease FTSH,
FT                   chloroplastic"
FT                   /id="PRO_0000000245"
FT   TRANSMEM        35..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        173..193
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        493
FT                   /evidence="ECO:0000250"
FT   BINDING         270..277
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         492
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         496
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         573
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
FT   NON_TER         662
SQ   SEQUENCE   662 AA;  71061 MW;  AF3411BDC502C6A1 CRC64;
     KYFNFHSKRK CIITQSTLNK KPNSDNFKNA QSKAALAALL FSSITPHAIA LDDAAPIASP
     PQVMEVEAPN PNTSNPLPFS QNLVLNAPKT QASPVSDLPE STQWRYSEFL NAVKKGKVER
     VRFSKDGSAL QLTAVDGRRA NVIVPNDPDL IDILAMNGVD ISVSEGEGGN GLFSVIGNLL
     FPFIAFAGLF FLFRRSQGGP GGPGGLGGPM DFGRSKSKFQ EVPETGVTFA DVAGADQAKL
     ELQEVVDFLK NPDKYTALGA KIPKGCLLVG PPGTGKTLLA RAVAGEAGVP FFSCAASEFV
     ELFVGVGASR VRHLFENAKS KAPCIVFIDE IDAVGRQRGA GLGGGNDERE QTINQLLTEM
     DGFSGNSGVI VLAATNRPDV LDSALLRPGK FDRQVTVDRP DVAGRVRILQ VHSRGKALAK
     DVDFDKIARR TPGFTGADLQ NLMNEAAILA ARRDLKEISK DEISDALERI IAGPEKKNAV
     VSDEKKKLVA YHEAGHALVG ALMPEYDPVA KISIIPRGQA GGLTFFAPSE ERLESGLYSR
     SYLENQMAVA LGGRVAEEVI FGEDNVTTGA SNDFMQVSRV ARQMVERLGF SKKIGQVAIG
     GGGGNPFLGQ QMSTQKDYSM ATADVVDSEV RELVEKAYER AKQIITTHID ILHKLAQLLI
     EK