FTSH_TOBAC
ID FTSH_TOBAC Reviewed; 714 AA.
AC O82150;
DT 13-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=ATP-dependent zinc metalloprotease FTSH, chloroplastic;
DE EC=3.4.24.-;
DE AltName: Full=DS9;
DE Flags: Precursor;
GN Name=FTSH;
OS Nicotiana tabacum (Common tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4097;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10852937; DOI=10.2307/3871219;
RA Seo S., Okamoto M., Iwai T., Iwano M., Fukui K., Isogai A., Nakajima N.,
RA Ohashi Y.;
RT "Reduced levels of chloroplast FtsH protein in tobacco mosaic virus-
RT infected tobacco leaves accelerate the hypersensitive reaction.";
RL Plant Cell 12:917-932(2000).
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; AB017480; BAA33755.2; -; mRNA.
DR RefSeq; NP_001313011.1; NM_001326082.1.
DR AlphaFoldDB; O82150; -.
DR SMR; O82150; -.
DR STRING; 4097.O82150; -.
DR MEROPS; M41.020; -.
DR PRIDE; O82150; -.
DR GeneID; 107821735; -.
DR KEGG; nta:107821735; -.
DR Proteomes; UP000084051; Unplaced.
DR GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009534; C:chloroplast thylakoid; IBA:GO_Central.
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; IBA:GO_Central.
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; IBA:GO_Central.
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 Reference proteome; Transit peptide; Transmembrane; Transmembrane helix;
KW Zinc.
FT TRANSIT 1..?
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN ?..714
FT /note="ATP-dependent zinc metalloprotease FTSH,
FT chloroplastic"
FT /id="PRO_0000000247"
FT TRANSMEM 55..75
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 196..216
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 516
FT /evidence="ECO:0000250"
FT BINDING 293..300
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 515
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 519
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 596
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 714 AA; 77111 MW; E97F40602CEE9EA1 CRC64;
MANSLLSSNF MGSQIFVSPP TPKTTKYFHF HSKRKSLIPQ SILNKKPNSD NSKNIPSKAA
LAALLFSSIT PHAYALDNTT PTVPTPRVIQ AEAANPTTSN PFSQNIILNA PKPQAQTNPE
LPEVSQWRYS EFLNAVKKGK VERVRFSKDG SALQLTAVDG RRATVTVPND PDLIDILAMN
GVDISVSEGD SAGNGLFNLI GNLFPFIAFA GLFYLFQRSQ GGPGGPGGLG GPMDFGRSKS
KFQEVPETGV TFADVAGADQ AKLELQEVVD FLKNPDKYTA LGAKIPKGCL LVGPPGTGKT
LLARAVAGEA GVPFFSCAAS EFVELFVGVG ASRVRDLFEK AKSKAPCIVF IDEIDAVGRQ
RGAGMGGGND EREQTINQLL TEMDGFSGNS GVIVLAATNR PDVLDSALLR PGRFDRQVTV
DRPDVAGRIK ILQVHSRGKA LTKDVDFEKI ARRTPGYTGA DLQNLMNEAA ILAARRELKE
ISKDEISDAL ERIIAGPEKK NAVVSDEKKK LVAYHEAGHA LVGALMPEYD PVAKISIIPR
GQAGGLTFFA PSEERLESGL YSRSYLENQM AVALGERVAE EVIFGQDNVT TGASNDFMQV
SRVARQMVER LGFSKKIGQV AIGGGGGNPF LGQQMSTQKD YSMATADVVD AEVRELVERA
YERATEIITT HIDILHKLAQ LLIEKETVDG EEFMSLFIDG KAELYISWVS KEED
