FTSH5_ARATH
ID FTSH5_ARATH Reviewed; 704 AA.
AC Q9FH02;
DT 13-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=ATP-dependent zinc metalloprotease FTSH 5, chloroplastic;
DE Short=AtFTSH5;
DE EC=3.4.24.-;
DE AltName: Full=Protein VARIEGATED 1;
DE Flags: Precursor;
GN Name=FTSH5; Synonyms=FTSH2, VAR1; OrderedLocusNames=At5g42270;
GN ORFNames=K5J14.7;
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=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(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 FUNCTION, SUBCELLULAR LOCATION, INDUCTION BY LIGHT, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=12167156; DOI=10.1046/j.1365-2443.2002.00558.x;
RA Sakamoto W., Tamura T., Hanba-Tomita Y., Sodmergen X., Murata M.;
RT "The VAR1 locus of Arabidopsis encodes a chloroplastic FtsH and is
RT responsible for leaf variegation in the mutant alleles.";
RL Genes Cells 7:769-780(2002).
RN [6]
RP FUNCTION, INTERACTION WITH FTSH2, AND 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 [7]
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 [8]
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 [9]
RP SUBUNIT, 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 [10]
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 [11]
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 [12]
RP FUNCTION.
RX PubMed=16157880; DOI=10.1073/pnas.0503472102;
RA Zelisko A., Garcia-Lorenzo M., Jackowski G., Jansson S., Funk C.;
RT "AtFtsH6 is involved in the degradation of the light-harvesting complex II
RT during high-light acclimation and senescence.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:13699-13704(2005).
RN [13]
RP FUNCTION.
RX PubMed=16972866; DOI=10.1111/j.1365-313x.2006.02855.x;
RA Chen J., Burke J.J., Velten J., Xin Z.;
RT "FtsH11 protease plays a critical role in Arabidopsis thermotolerance.";
RL Plant J. 48:73-84(2006).
RN [14]
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).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
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. Not involved in the degradation
CC of the light-harvesting complex of photosystem II (LHC II) or in
CC thermotolerance. {ECO:0000269|PubMed:12167156,
CC ECO:0000269|PubMed:14630971, ECO:0000269|PubMed:16157880,
CC ECO:0000269|PubMed:16972866}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000305};
CC -!- SUBUNIT: Heterohexamers with FTSH1, FTSH2 and FTSH8.
CC {ECO:0000269|PubMed:14996218, ECO:0000269|PubMed:16040665,
CC ECO:0000269|PubMed:16126834}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000269|PubMed:12167156, ECO:0000269|PubMed:14630971,
CC ECO:0000269|PubMed:18431481}; Single-pass membrane protein
CC {ECO:0000269|PubMed:12167156, ECO:0000269|PubMed:14630971}; Stromal
CC side {ECO:0000269|PubMed:12167156, ECO:0000269|PubMed:14630971}.
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:12167156,
CC ECO:0000269|PubMed:15266057}.
CC -!- DISRUPTION PHENOTYPE: Leaf-variegated. Mutations can be complemented by
CC overexpression of FTSH1. The presence of both FTSH1 or FTSH5 (subunit
CC type A) and FTSH2 or FTSH8 (subunit type B) is essential for an active
CC complex formation. {ECO:0000269|PubMed:12167156}.
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; AB023032; BAB10200.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94790.1; -; Genomic_DNA.
DR EMBL; AY126987; AAM83215.1; -; mRNA.
DR RefSeq; NP_568604.1; NM_123592.4.
DR AlphaFoldDB; Q9FH02; -.
DR SMR; Q9FH02; -.
DR BioGRID; 19482; 3.
DR STRING; 3702.AT5G42270.1; -.
DR MEROPS; M41.024; -.
DR iPTMnet; Q9FH02; -.
DR PaxDb; Q9FH02; -.
DR PRIDE; Q9FH02; -.
DR ProteomicsDB; 228918; -.
DR EnsemblPlants; AT5G42270.1; AT5G42270.1; AT5G42270.
DR GeneID; 834232; -.
DR Gramene; AT5G42270.1; AT5G42270.1; AT5G42270.
DR KEGG; ath:AT5G42270; -.
DR Araport; AT5G42270; -.
DR TAIR; locus:2157637; AT5G42270.
DR eggNOG; KOG0731; Eukaryota.
DR HOGENOM; CLU_000688_16_2_1; -.
DR InParanoid; Q9FH02; -.
DR OMA; FGQNVLM; -.
DR OrthoDB; 217929at2759; -.
DR PhylomeDB; Q9FH02; -.
DR BRENDA; 3.4.24.B20; 399.
DR PRO; PR:Q9FH02; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FH02; baseline and differential.
DR Genevisible; Q9FH02; 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; IDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
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; IDA:TAIR.
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:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0010205; P:photoinhibition; IMP:TAIR.
DR GO; GO:0048564; P:photosystem I assembly; IMP:TAIR.
DR GO; GO:0030163; P:protein catabolic process; IDA: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; Zinc.
FT TRANSIT 1..58
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT TRANSIT 59..76
FT /note="Thylakoid"
FT /evidence="ECO:0000305"
FT CHAIN 77..704
FT /note="ATP-dependent zinc metalloprotease FTSH 5,
FT chloroplastic"
FT /id="PRO_0000000244"
FT TRANSMEM 193..213
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 513
FT /evidence="ECO:0000250"
FT BINDING 290..297
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 512
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 516
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 593
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 704 AA; 75232 MW; F536A13BD9A45DAD CRC64;
MATTSSNPLL LSSNFLGSQI IISAPTPKTT TKSLPFSVIS RKRYQISQSE KLMKSLPSQA
ALAALLFSSS SPQALAVNEP VQPPAPTITA EAQSPNLSTF GQNVLMTAPN PQAQSSDLPD
GTQWRYSEFL NAVKKGKVER VKFSKDGSVL QLTAVDNRRA TVIVPNDPDL IDILAMNGVD
ISVSEGEGGN GLFDFIGNLL FPLLAFGGLF YLFRGGQGGA GGPGGLGGPM DFGRSKSKFQ
EVPETGVTFG DVAGADQAKL ELQEVVDFLK NPDKYTALGA KIPKGCLLVG PPGTGKTLLA
RAVAGEAGVP FFSCAASEFV ELFVGVGASR VRDLFEKAKS KAPCIVFIDE IDAVGRQRGA
GMGGGNDERE QTINQLLTEM DGFSGNSGVI VLAATNRPDV LDSALLRPGR FDRQVTVDRP
DVAGRVQILK VHSRGKAIGK DVDYEKVARR TPGFTGADLQ NLMNEAAILA ARRELKEISK
DEISDALERI IAGPEKKNAV VSEEKKRLVA YHEAGHALVG ALMPEYDPVA KISIIPRGQA
GGLTFFAPSE ERLESGLYSR SYLENQMAVA LGGRVAEEVI FGDENVTTGA SNDFMQVSRV
ARQMVERFGF SKKIGQVAVG GAGGNPFLGQ SMSSQKDYSM ATADVVDAEV RELVEKAYVR
AKEIITTQID ILHKLAQLLI EKETVDGEEF MSLFIDGQAE LYVS
