FTSH_HELAN
ID FTSH_HELAN Reviewed; 260 AA.
AC P85190;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 1.
DT 03-AUG-2022, entry version 27.
DE RecName: Full=ATP-dependent zinc metalloprotease FTSH, chloroplastic;
DE EC=3.4.24.-;
DE Flags: Fragment;
GN Name=FTSH {ECO:0000250|UniProtKB:Q9FIM2};
OS Helianthus annuus (Common sunflower).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Asteroideae;
OC Heliantheae alliance; Heliantheae; Helianthus.
OX NCBI_TaxID=4232;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. RHA801 {ECO:0000269|Ref.1};
RA Kozik A., Michelmore R.W., Knapp S., Matvienko M., Rieseberg L., Lin H.,
RA van Damme M., Lavelle D., Chevalier P., Ziegle J., Ellison P., Kolkman J.,
RA Slabaugh M.S., Livingston K., Zhou Y., Lai Z., Church S., Jackson L.,
RA Bradford K.;
RT "Lettuce and sunflower ESTs from the compositae genome project
RT http://compgenomics.ucdavis.edu/.";
RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305}
RP IDENTIFICATION BY MASS SPECTROMETRY, AND INDUCTION.
RA Garcia J.S., Souza G.H.M.F., Eberlin M.N., Arruda M.A.Z.;
RT "Evaluation of metal-ion stress in sunflower (Heliantus annus L.) leaves
RT through proteomic changes.";
RL Metallomics 1:107-113(2009).
CC -!- FUNCTION: Probable ATP-dependent zinc metallopeptidase.
CC {ECO:0000250|UniProtKB:Q9FIM2}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q9FIM2};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q9FIM2};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000250|UniProtKB:Q9FIM2}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:Q9FIM2}; Stromal side
CC {ECO:0000250|UniProtKB:Q9FIM2}.
CC -!- INDUCTION: Down-regulated in response to zinc ion contamination and in
CC response to mixed metal ion contamination (cadmium, copper, lead and
CC zinc). {ECO:0000269|Ref.2}.
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 EMBL; BQ969737; -; NOT_ANNOTATED_CDS; mRNA.
DR AlphaFoldDB; P85190; -.
DR SMR; P85190; -.
DR PRIDE; P85190; -.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
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:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.20.58.760; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
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 SUPFAM; SSF140990; SSF140990; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00674; AAA; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Chloroplast; Hydrolase; Membrane; Metal-binding;
KW Metalloprotease; Nucleotide-binding; Plastid; Protease; Thylakoid; Zinc.
FT CHAIN <1..>260
FT /note="ATP-dependent zinc metalloprotease FTSH,
FT chloroplastic"
FT /id="PRO_0000397225"
FT ACT_SITE 220
FT /evidence="ECO:0000250|UniProtKB:Q9FIM2"
FT BINDING 219
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9FIM2"
FT BINDING 223
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9FIM2"
FT NON_TER 1
FT /evidence="ECO:0000305"
FT NON_TER 260
FT /evidence="ECO:0000305"
SQ SEQUENCE 260 AA; 27989 MW; 7D77498D91622452 CRC64;
NSALWPVAGE AEVPFISCSA SEFVELYVGM GASRVRDLFA RAKKEAPSII FIDEIDAVAK
SRDGRFRIVS NDEREQTLNQ LLTEMDGFDS NSAVIVLGAT NRADVLDPAL RRPGRFDRVV
MVETPDRVGR QAILNVHVSK KELPLGDDVD LASIASMTTG FTGADLANLV NEAALLAGRQ
NKVVVEKIDF IHAVERSIAG IEKKTAKLQG SEKAVVARHE AGHAVVGTAV SKLLAGQPRV
EKLSILPRSG RALGFTYTPS
