ID FTSH9_ARATH Reviewed; 806 AA.
AC Q9FIM2;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 27-MAR-2024, entry version 144.
DE RecName: Full=ATP-dependent zinc metalloprotease FTSH 9, chloroplastic;
DE Short=AtFTSH9;
DE EC=3.4.24.-;
DE Flags: Precursor;
GN Name=FTSH9; OrderedLocusNames=At5g58870; ORFNames=K19M22.7;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10048488; DOI=10.1093/dnares/5.6.379;
RA Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence
RT features of the regions of 1,081,958 bp covered by seventeen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:379-391(1998).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11299370; DOI=10.1104/pp.125.4.1912;
RA Adam Z., Adamska I., Nakabayashi K., Ostersetzer O., Haussuhl K.,
RA Manuell A., Zheng B., Vallon O., Rodermel S.R., Shinozaki K., Clarke A.K.;
RT "Chloroplast and mitochondrial proteases in Arabidopsis. A proposed
RT nomenclature.";
RL Plant Physiol. 125:1912-1918(2001).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=14630971; DOI=10.1105/tpc.017319;
RA Sakamoto W., Zaltsman A., Adam Z., Takahashi Y.;
RT "Coordinated regulation and complex formation of yellow variegated1 and
RT yellow variegated2, chloroplastic FtsH metalloproteases involved in the
RT repair cycle of photosystem II in Arabidopsis thylakoid membranes.";
RL Plant Cell 15:2843-2855(2003).
RN [6]
RP INDUCTION BY HIGH LIGHT.
RX PubMed=15266057; DOI=10.1104/pp.104.043299;
RA Sinvany-Villalobo G., Davydov O., Ben-Ari G., Zaltsman A., Raskind A.,
RA Adam Z.;
RT "Expression in multigene families. Analysis of chloroplast and
RT mitochondrial proteases.";
RL Plant Physiol. 135:1336-1345(2004).
RN [7]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=14996218; DOI=10.1111/j.1365-313x.2003.02014.x;
RA Yu F., Park S., Rodermel S.R.;
RT "The Arabidopsis FtsH metalloprotease gene family: interchangeability of
RT subunits in chloroplast oligomeric complexes.";
RL Plant J. 37:864-876(2004).
CC -!- FUNCTION: Probable ATP-dependent zinc metallopeptidase.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000269|PubMed:14630971}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:14630971}; Stromal side
CC {ECO:0000269|PubMed:14630971}.
CC -!- INDUCTION: By high light. {ECO:0000269|PubMed:15266057}.
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; AB016885; BAB09632.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97112.1; -; Genomic_DNA.
DR EMBL; AY059856; AAL24338.1; -; mRNA.
DR RefSeq; NP_568892.1; NM_125277.4.
DR AlphaFoldDB; Q9FIM2; -.
DR SMR; Q9FIM2; -.
DR STRING; 3702.Q9FIM2; -.
DR MEROPS; M41.A03; -.
DR PaxDb; 3702-AT5G58870-1; -.
DR ProteomicsDB; 228888; -.
DR EnsemblPlants; AT5G58870.1; AT5G58870.1; AT5G58870.
DR GeneID; 836004; -.
DR Gramene; AT5G58870.1; AT5G58870.1; AT5G58870.
DR KEGG; ath:AT5G58870; -.
DR Araport; AT5G58870; -.
DR TAIR; AT5G58870; FTSH9.
DR eggNOG; KOG0731; Eukaryota.
DR HOGENOM; CLU_000688_23_3_1; -.
DR InParanoid; Q9FIM2; -.
DR OMA; NSSCEHD; -.
DR OrthoDB; 117at2759; -.
DR PhylomeDB; Q9FIM2; -.
DR BRENDA; 3.4.24.B20; 399.
DR PRO; PR:Q9FIM2; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FIM2; baseline and differential.
DR Genevisible; Q9FIM2; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
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; ISS:TAIR.
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 CDD; cd19501; RecA-like_FtsH; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 3.30.720.210; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.20.58.760; Peptidase M41; 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 NCBIfam; TIGR01241; FtsH_fam; 1.
DR PANTHER; PTHR23076:SF49; ATP-DEPENDENT ZINC METALLOPROTEASE FTSH 9, CHLOROPLASTIC; 1.
DR PANTHER; PTHR23076; METALLOPROTEASE M41 FTSH; 1.
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; FtsH protease domain-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00674; AAA; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Chloroplast; Hydrolase; Membrane; Metal-binding;
KW Metalloprotease; Nucleotide-binding; Plastid; Protease; Reference proteome;
KW Thylakoid; Transit peptide; Transmembrane; Transmembrane helix; Zinc.
FT TRANSIT 1..62
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT TRANSIT 63..?
FT /note="Thylakoid"
FT /evidence="ECO:0000255"
FT CHAIN ?..806
FT /note="ATP-dependent zinc metalloprotease FTSH 9,
FT chloroplastic"
FT /id="PRO_0000341334"
FT TRANSMEM 133..153
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 271..291
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 84..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..98
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..116
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 595
FT /evidence="ECO:0000250"
FT BINDING 369..376
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 594
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 598
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 677
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 806 AA; 87838 MW; 074470A8A1E6F4F9 CRC64;
MTSIELLSPL IHDKFRFSTC CSTSSLLYLH ASSFFRDRSF GFRQNPNRFV SNSSIQLPQS
VPGSINQERF NLWQGFSRKK STSSSRTIVN CQEGDQKASS SEGEGKTNKD KGRKQGKNEL
WWSKGKKWQW KPIIQAQEIG VMLLQLGIVM FVVRLLRPGI PLPGSEPRTQ TTFMSVPYSD
FLSKVNNDEV QKVEVDGFHV LFKLKDDGNL QESETSSSSI KLSESSETML RSVAPTKRVV
YSTTRPRDIK TPYEKMLENN VEFGSPDKRS GGFFNSGLIV LFYIAVLAGL LHRFPVNFSQ
STTGQLRTRK SGGPGGGKVS GDGETITFAD VAGVDEAKEE LEEIVEFLKN PDRYVRLGAR
PPRGVLLVGL PGTGKTLLAK AVAGESDVPF ISCSASEFVE LYVGMGASRV RDLFARAKKE
APSIIFIDEI DAVAKSRDGK FRMVSNDERE QTLNQLLTEM DGFDSSSAVI VLGATNRADV
LDPALRRPGR FDRVVTVESP DKVGRESILK VHVSKKELPL GDDVNLASIA SMTTGFTGAD
LANLVNEAAL LAGRKSKMTV DKIDFIHAVE RSIAGIEKKT ARLKGSEKAV VARHEAGHAV
VGTAVASLLS GQSRVEKLSI LPRSGGALGF TYIPPTHEDR YLLFIDELHG RLVTLLGGRA
AEEVVYSGRI STGALDDIRR ATDMAYKAVA EYGLNEKIGP VSVATLSAGG IDDSGGSPWG
RDQGHLVDLV QREVTNLLQS ALDVALTVVR ANPDVLEGLG AQLEDEEKVE GEELQKWLNR
VVPSEELAVF IKGKQTALLP AQASSS
//
