FTSH8_ARATH
ID FTSH8_ARATH Reviewed; 685 AA.
AC Q8W585; Q94AL5; Q9SHI8;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=ATP-dependent zinc metalloprotease FTSH 8, chloroplastic;
DE Short=AtFTSH8;
DE EC=3.4.24.-;
DE Flags: Precursor;
GN Name=FTSH8; OrderedLocusNames=At1g06430; ORFNames=F12K11.22, F12K11_24;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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 CONSERVED LUMENAL DOMAIN.
RX PubMed=11717304; DOI=10.1074/jbc.m105878200;
RA Bailey S., Thompson E., Nixon P.J., Horton P., Mullineaux C.W.,
RA Robinson C., Mann N.H.;
RT "A critical role for the Var2 FtsH homologue of Arabidopsis thaliana in the
RT photosystem II repair cycle in vivo.";
RL J. Biol. Chem. 277:2006-2011(2002).
RN [6]
RP SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
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 [7]
RP INDUCTION BY HEAT AND 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 [8]
RP SUBUNIT, TISSUE SPECIFICITY, 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).
RN [9]
RP SUBUNIT.
RX PubMed=16126834; DOI=10.1105/tpc.105.035071;
RA Zaltsman A., Ori N., Adam Z.;
RT "Two types of FtsH protease subunits are required for chloroplast
RT biogenesis and Photosystem II repair in Arabidopsis.";
RL Plant Cell 17:2782-2790(2005).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=18431481; DOI=10.1371/journal.pone.0001994;
RA Zybailov B., Rutschow H., Friso G., Rudella A., Emanuelsson O., Sun Q.,
RA van Wijk K.J.;
RT "Sorting signals, N-terminal modifications and abundance of the chloroplast
RT proteome.";
RL PLoS ONE 3:E1994-E1994(2008).
CC -!- FUNCTION: Part of a complex that function as an ATP-dependent zinc
CC metallopeptidase. Involved in the thylakoid formation and in the
CC removal of damaged D1 in the photosystem II, preventing cell death
CC under high-intensity light conditions.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Heterohexamers with FTSH1, FTSH2 and FTSH5. May also form
CC homooligomers. {ECO:0000269|PubMed:14996218,
CC ECO:0000269|PubMed:16126834}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000269|PubMed:14630971, ECO:0000269|PubMed:18431481}; Single-pass
CC membrane protein {ECO:0000269|PubMed:14630971}; Stromal side
CC {ECO:0000269|PubMed:14630971}.
CC -!- TISSUE SPECIFICITY: Expressed in cotyledons, cauline and rosette
CC leaves, stems, sepals, flovers and siliques. Very low in roots.
CC {ECO:0000269|PubMed:14996218}.
CC -!- INDUCTION: By heat and high light. {ECO:0000269|PubMed:15266057}.
CC -!- DOMAIN: The conserved lumenal (CL) domain (74-154) is present only in
CC some FtsH homologs from organisms performing oxygenic photosynthesis.
CC -!- DISRUPTION PHENOTYPE: No visible changes in phenotype, probably due to
CC a complementation by FTSH2. The presence of both FTSH1 or FTSH5
CC (subunit type A) and FTSH2 or FTSH8 (subunit type B) is essential for
CC an active complex formation. {ECO:0000269|PubMed:14630971}.
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; AC007592; AAF24819.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27986.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM59212.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM59213.1; -; Genomic_DNA.
DR EMBL; AF419565; AAL31897.1; -; mRNA.
DR EMBL; BT002649; AAO11565.1; -; mRNA.
DR EMBL; BT003813; AAO41866.1; -; mRNA.
DR EMBL; AY045951; AAK76625.2; -; mRNA.
DR RefSeq; NP_001321589.1; NM_001331629.1.
DR RefSeq; NP_001321590.1; NM_001331628.1.
DR RefSeq; NP_563766.3; NM_100523.6.
DR AlphaFoldDB; Q8W585; -.
DR SMR; Q8W585; -.
DR BioGRID; 22395; 2.
DR STRING; 3702.AT1G06430.1; -.
DR MEROPS; M41.025; -.
DR iPTMnet; Q8W585; -.
DR PaxDb; Q8W585; -.
DR PRIDE; Q8W585; -.
DR ProteomicsDB; 228887; -.
DR EnsemblPlants; AT1G06430.1; AT1G06430.1; AT1G06430.
DR EnsemblPlants; AT1G06430.2; AT1G06430.2; AT1G06430.
DR EnsemblPlants; AT1G06430.3; AT1G06430.3; AT1G06430.
DR GeneID; 837154; -.
DR Gramene; AT1G06430.1; AT1G06430.1; AT1G06430.
DR Gramene; AT1G06430.2; AT1G06430.2; AT1G06430.
DR Gramene; AT1G06430.3; AT1G06430.3; AT1G06430.
DR KEGG; ath:AT1G06430; -.
DR Araport; AT1G06430; -.
DR TAIR; locus:2009235; AT1G06430.
DR eggNOG; KOG0731; Eukaryota.
DR HOGENOM; CLU_000688_16_2_1; -.
DR InParanoid; Q8W585; -.
DR OMA; PNSATAC; -.
DR OrthoDB; 217929at2759; -.
DR PhylomeDB; Q8W585; -.
DR BRENDA; 3.4.24.B20; 399.
DR PRO; PR:Q8W585; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8W585; baseline and differential.
DR Genevisible; Q8W585; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009534; C:chloroplast thylakoid; HDA:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; HDA:TAIR.
DR GO; GO:0005576; C:extracellular region; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009579; C:thylakoid; 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:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR GO; GO:0010304; P:PSII associated light-harvesting complex II catabolic process; TAS:TAIR.
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; IPR011546; Pept_M41_FtsH_extracell.
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; PF06480; FtsH_ext; 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 1: Evidence at protein level;
KW ATP-binding; Chloroplast; Developmental protein; Hydrolase; Membrane;
KW Metal-binding; Metalloprotease; Nucleotide-binding; Plastid; Protease;
KW Reference proteome; Thylakoid; Transit peptide; Transmembrane;
KW Transmembrane helix; Zinc.
FT TRANSIT 1..37
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT TRANSIT 38..73
FT /note="Thylakoid"
FT /evidence="ECO:0000305"
FT CHAIN 74..685
FT /note="ATP-dependent zinc metalloprotease FTSH 8,
FT chloroplastic"
FT /id="PRO_0000341333"
FT TOPO_DOM 38..161
FT /note="Lumenal, thylakoid"
FT /evidence="ECO:0000255"
FT TRANSMEM 162..182
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 183..685
FT /note="Stromal"
FT /evidence="ECO:0000255"
FT ACT_SITE 482
FT /evidence="ECO:0000250"
FT BINDING 260..267
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 481
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 485
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 559
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 685 AA; 73198 MW; FF935260BD3E0FBD CRC64;
MAASSACLLG NGLSVYTTKQ RFQKLGLDRT SKVTVVKASL DEKKHEGRRG FFKLLLGNAA
AGVGLLASGN ANADEQGQGV SSSRMSYSRF LEYLDKGRVE KVDLYENGTI AIVEAVSPEL
GNRIQRVRVQ LPGLSQELLQ KLRAKNIDFA AHNAQEDQGS PILNLIGNLA FPVILIGGLF
LLSRRSSGGM GGPGGPGFPL QIGQSKAKFQ MEPNTGVTFD DVAGVDEAKQ DFMEVVEFLK
KPERFTAVGA RIPKGVLLVG PPGTGKTLLA KAIAGEAGVP FFSISGSEFV EMFVGVGASR
VRDLFKKAKE NAPCIVFVDE IDAVGRQRGT GIGGGNDERE QTLNQLLTEM DGFEGNTGVI
VVAATNRADI LDSALLRPGR FDRQVSVDVP DVKGRTDILK VHSGNKKFES GVSLEVIAMR
TPGFSGADLA NLLNEAAILA GRRGKTAISS KEIDDSIDRI VAGMEGTVMT DGKSKSLVAY
HEVGHAICGT LTPGHDAVQK VTLIPRGQAR GLTWFIPSDD PTLISKQQLF ARIVGGLGGR
AAEEVIFGES EVTTGAVSDL QQITGLAKQM VTTFGMSEIG PWSLMDSSEQ SDVIMRMMAR
NSMSEKLAND IDTAVKTLSD KAYEIALSQI RNNREAMDKI VEILLEKETM SGDEFRAILS
EFTEIPPENR VASSTSTSTP TPASV
