FTSH1_ARATH
ID FTSH1_ARATH Reviewed; 716 AA.
AC Q39102; O04172; Q9SX43;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 13-DEC-2001, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=ATP-dependent zinc metalloprotease FTSH 1, chloroplastic;
DE Short=AtFTSH1;
DE EC=3.4.24.-;
DE Flags: Precursor;
GN Name=FTSH1; Synonyms=AAA, FTSH; OrderedLocusNames=At1g50250;
GN ORFNames=F14I3.14;
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 [MRNA], AND SUBCELLULAR LOCATION.
RX PubMed=8910594; DOI=10.1074/jbc.271.46.29329;
RA Lindahl M., Tabak S., Cseke L., Pichersky E., Andersson B., Adam Z.;
RT "Identification, characterization, and molecular cloning of a homologue of
RT the bacterial FtsH protease in chloroplasts of higher plants.";
RL J. Biol. Chem. 271:29329-29334(1996).
RN [2]
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 [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 70-702.
RA Mink M.;
RT "Arabidopsis thaliana cDNA encoding a homologue to prokaryotic and
RT eukaryotic ATPases.";
RL (er) Plant Gene Register PGR97-085(1997).
RN [6]
RP FUNCTION.
RX PubMed=10715327; DOI=10.2307/3870946;
RA Lindahl M., Spetea C., Hundal T., Oppenheim A.B., Adam Z., Andersson B.;
RT "The thylakoid FtsH protease plays a role in the light-induced turnover of
RT the photosystem II D1 protein.";
RL Plant Cell 12:419-431(2000).
RN [7]
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 [8]
RP SUBUNIT, 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 [9]
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 [10]
RP SUBUNIT, 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 [11]
RP INTERACTION WITH FTSH2 AND FTSH8, AND TISSUE SPECIFICITY.
RX PubMed=16040665; DOI=10.1104/pp.105.061234;
RA Yu F., Park S., Rodermel S.R.;
RT "Functional redundancy of AtFtsH metalloproteases in thylakoid membrane
RT complexes.";
RL Plant Physiol. 138:1957-1966(2005).
RN [12]
RP DEVELOPMENTAL STAGE.
RX PubMed=15918877; DOI=10.1111/j.1365-313x.2005.02401.x;
RA Zaltsman A., Feder A., Adam Z.;
RT "Developmental and light effects on the accumulation of FtsH protease in
RT Arabidopsis chloroplasts -- implications for thylakoid formation and
RT photosystem II maintenance.";
RL Plant J. 42:609-617(2005).
RN [13]
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 [14]
RP INTERACTION WITH CHIP AND HSP70, AND UBIQUITINATION.
RX PubMed=17714429; DOI=10.1111/j.1365-313x.2007.03239.x;
RA Shen G., Adam Z., Zhang H.;
RT "The E3 ligase AtCHIP ubiquitylates FtsH1, a component of the chloroplast
RT FtsH protease, and affects protein degradation in chloroplasts.";
RL Plant J. 52:309-321(2007).
RN [15]
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. {ECO:0000269|PubMed:10715327}.
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: Interacts with CHIP and HSP70. Heterohexamers with FTSH2,
CC FTSH5 and FTSH8. {ECO:0000269|PubMed:14630971,
CC ECO:0000269|PubMed:14996218, ECO:0000269|PubMed:16040665,
CC ECO:0000269|PubMed:16126834, ECO:0000269|PubMed:17714429}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000269|PubMed:14630971, ECO:0000269|PubMed:18431481,
CC ECO:0000269|PubMed:8910594}; Single-pass membrane protein
CC {ECO:0000269|PubMed:14630971, ECO:0000269|PubMed:8910594}; Stromal side
CC {ECO:0000269|PubMed:14630971, ECO:0000269|PubMed:8910594}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:16040665}.
CC -!- DEVELOPMENTAL STAGE: Low expression in cotyledons, increasing with
CC leaves development. {ECO:0000269|PubMed:15918877}.
CC -!- INDUCTION: By high light. {ECO:0000269|PubMed:15266057}.
CC -!- PTM: The FTSH1 precursor is ubiquitinated by CHIP in the cytoplasm.
CC {ECO:0000269|PubMed:17714429}.
CC -!- DISRUPTION PHENOTYPE: No visible changes in phenotype, probably due to
CC a complementation by FTSH5. 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA73318.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X99808; CAA68141.1; -; mRNA.
DR EMBL; AC007980; AAD50055.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32528.1; -; Genomic_DNA.
DR EMBL; AY091095; AAM14046.1; -; mRNA.
DR EMBL; AY123034; AAM67567.1; -; mRNA.
DR EMBL; Y12780; CAA73318.1; ALT_FRAME; mRNA.
DR PIR; G96538; G96538.
DR RefSeq; NP_564563.1; NM_103909.4.
DR AlphaFoldDB; Q39102; -.
DR SMR; Q39102; -.
DR BioGRID; 26672; 10.
DR STRING; 3702.AT1G50250.1; -.
DR MEROPS; M41.020; -.
DR iPTMnet; Q39102; -.
DR PaxDb; Q39102; -.
DR PRIDE; Q39102; -.
DR ProteomicsDB; 228885; -.
DR EnsemblPlants; AT1G50250.1; AT1G50250.1; AT1G50250.
DR GeneID; 841447; -.
DR Gramene; AT1G50250.1; AT1G50250.1; AT1G50250.
DR KEGG; ath:AT1G50250; -.
DR Araport; AT1G50250; -.
DR TAIR; locus:2011952; AT1G50250.
DR eggNOG; KOG0731; Eukaryota.
DR HOGENOM; CLU_000688_16_2_1; -.
DR InParanoid; Q39102; -.
DR OMA; QYGMTER; -.
DR OrthoDB; 217929at2759; -.
DR PhylomeDB; Q39102; -.
DR BRENDA; 3.4.24.B20; 399.
DR PRO; PR:Q39102; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q39102; baseline and differential.
DR Genevisible; Q39102; 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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0031977; C:thylakoid lumen; 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:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0010206; P:photosystem II repair; TAS:TAIR.
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; 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 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; Ubl conjugation; Zinc.
FT TRANSIT 1..48
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT TRANSIT 49..86
FT /note="Thylakoid"
FT /evidence="ECO:0000305"
FT CHAIN 87..716
FT /note="ATP-dependent zinc metalloprotease FTSH 1,
FT chloroplastic"
FT /id="PRO_0000000243"
FT TRANSMEM 204..224
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 525
FT /evidence="ECO:0000250"
FT BINDING 302..309
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 524
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 528
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 605
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT CONFLICT 70..73
FT /note="LAAI -> YVRV (in Ref. 5; CAA73318)"
FT /evidence="ECO:0000305"
FT CONFLICT 213
FT /note="P -> S (in Ref. 5; CAA73318)"
FT /evidence="ECO:0000305"
FT CONFLICT 326..329
FT /note="CAAS -> SRPQ (in Ref. 1; CAA68141)"
FT /evidence="ECO:0000305"
FT CONFLICT 362..363
FT /note="EI -> RV (in Ref. 5; CAA73318)"
FT /evidence="ECO:0000305"
FT CONFLICT 422
FT /note="R -> K (in Ref. 5; CAA73318)"
FT /evidence="ECO:0000305"
FT CONFLICT 463
FT /note="T -> S (in Ref. 5; CAA73318)"
FT /evidence="ECO:0000305"
FT CONFLICT 486..487
FT /note="EL -> DV (in Ref. 1; CAA68141)"
FT /evidence="ECO:0000305"
FT CONFLICT 531..535
FT /note="VGALM -> GGCSY (in Ref. 5; CAA73318)"
FT /evidence="ECO:0000305"
FT CONFLICT 539
FT /note="D -> N (in Ref. 5; CAA73318)"
FT /evidence="ECO:0000305"
FT CONFLICT 581..582
FT /note="VA -> CS (in Ref. 5; CAA73318)"
FT /evidence="ECO:0000305"
FT CONFLICT 698
FT /note="D -> A (in Ref. 5; CAA73318)"
FT /evidence="ECO:0000305"
FT CONFLICT 701..702
FT /note="EF -> DS (in Ref. 5; CAA73318)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 716 AA; 76759 MW; 37C1A7140D1F99B2 CRC64;
MASNSLLRSS SNFFLGSHII ISSPTPKTTR KPSFPFSFVS RAKYQITRSS QDENSPNGKP
NSPFSSQVAL AAILLSSISS SPLALAVVDE PASPSVVIES QAVKPSTPSP LFIQNEILKA
PSPKSSDLPE GSQWRYSEFL NAVKKGKVER VRFSKDGSVV QLTAVDNRRA SVIVPNDPDL
IDILAMNGVD ISVSEGESSG NDLFTVIGNL IFPLLAFGGL FLLFRRAQGG PGGGPGGLGG
PMDFGRSKSK FQEVPETGVS FADVAGADQA KLELQEVVDF LKNPDKYTAL GAKIPKGCLL
VGPPGTGKTL LARAVAGEAG VPFFSCAASE FVELFVGVGA SRVRDLFEKA KSKAPCIVFI
DEIDAVGRQR GAGMGGGNDE REQTINQLLT EMDGFSGNSG VIVLAATNRP DVLDSALLRP
GRFDRQVTVD RPDVAGRVKI LQVHSRGKAL GKDVDFDKVA RRTPGFTGAD LQNLMNEAAI
LAARRELKEI SKDEISDALE RIIAGPEKKN AVVSEEKKRL VAYHEAGHAL VGALMPEYDP
VAKISIIPRG QAGGLTFFAP SEERLESGLY SRSYLENQMA VALGGRVAEE VIFGDENVTT
GASNDFMQVS RVARQMIERF GFSKKIGQVA VGGPGGNPFM GQQMSSQKDY SMATADIVDA
EVRELVEKAY KRATEIITTH IDILHKLAQL LIEKETVDGE EFMSLFIDGQ AELYIS
