FTSH2_ARATH
ID FTSH2_ARATH Reviewed; 695 AA.
AC O80860; Q56Z14; Q94AZ0;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=ATP-dependent zinc metalloprotease FTSH 2, chloroplastic;
DE Short=AtFTSH2;
DE EC=3.4.24.-;
DE AltName: Full=Protein VARIEGATED 2;
DE Flags: Precursor;
GN Name=FTSH2; Synonyms=VAR2; OrderedLocusNames=At2g30950; ORFNames=F7F1.16;
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], FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=10849347; DOI=10.1046/j.1365-313x.2000.00738.x;
RA Chen M., Choi Y., Voytas D.F., Rodermel S.;
RT "Mutations in the Arabidopsis VAR2 locus cause leaf variegation due to the
RT loss of a chloroplast FtsH protease.";
RL Plant J. 22:303-313(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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] OF 306-695.
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 [LARGE SCALE MRNA] OF 499-695.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PROTEIN SEQUENCE OF 209-216, AND SUBCELLULAR LOCATION.
RX PubMed=11719511; DOI=10.1074/jbc.m108575200;
RA Schubert M., Petersson U.A., Haas B.J., Funk C., Schroeder W.P.,
RA Kieselbach T.;
RT "Proteome map of the chloroplast lumen of Arabidopsis thaliana.";
RL J. Biol. Chem. 277:8354-8365(2002).
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 FUNCTION, AND 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 [9]
RP FUNCTION, INTERACTION WITH FTSH5, 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 [10]
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 [11]
RP INDUCTION BY COLD 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 [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 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 [15]
RP INTERACTION WITH CHIP, 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 [16]
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, but not involved in
CC thermotolerance. {ECO:0000269|PubMed:10849347,
CC ECO:0000269|PubMed:11717304, ECO:0000269|PubMed:14630971,
CC ECO:0000269|PubMed:16972866}.
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 FTSH5. Heterohexamers with FTSH1,
CC FTSH5 and FTSH8. May also form homooligomers.
CC {ECO:0000269|PubMed:14630971, ECO:0000269|PubMed:14996218,
CC ECO:0000269|PubMed:16126834, ECO:0000269|PubMed:17714429}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000269|PubMed:11719511, ECO:0000269|PubMed:14630971,
CC ECO:0000269|PubMed:18431481}; Single-pass membrane protein
CC {ECO:0000269|PubMed:11719511, ECO:0000269|PubMed:14630971}; Stromal
CC side {ECO:0000269|PubMed:11719511, 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 -!- DEVELOPMENTAL STAGE: Low expression in cotyledons, increasing with
CC leaves development. {ECO:0000269|PubMed:15918877}.
CC -!- INDUCTION: By cold and high light. {ECO:0000269|PubMed:15266057}.
CC -!- DOMAIN: The conserved lumenal (CL) domain (83-161) is present only in
CC some FtsH homologs from organisms performing oxygenic photosynthesis.
CC -!- PTM: The FTSH2 precursor is ubiquitinated by CHIP in the cytoplasm.
CC {ECO:0000269|PubMed:17714429}.
CC -!- DISRUPTION PHENOTYPE: Leaf-variegated. Mutations can be complemented by
CC overexpression of FTSH8. 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:10849347}.
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=AAK73957.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF135189; AAF65925.1; -; mRNA.
DR EMBL; AC004669; AAC20729.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08466.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM61283.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM61284.1; -; Genomic_DNA.
DR EMBL; AY045599; AAK73957.1; ALT_INIT; mRNA.
DR EMBL; AY093791; AAM10407.1; -; mRNA.
DR EMBL; AK221155; BAD95179.1; -; mRNA.
DR PIR; F84714; F84714.
DR RefSeq; NP_001323510.1; NM_001336310.1.
DR RefSeq; NP_001323511.1; NM_001336311.1.
DR RefSeq; NP_850156.1; NM_179825.3.
DR AlphaFoldDB; O80860; -.
DR SMR; O80860; -.
DR BioGRID; 2995; 8.
DR IntAct; O80860; 2.
DR STRING; 3702.AT2G30950.1; -.
DR MEROPS; M41.005; -.
DR iPTMnet; O80860; -.
DR World-2DPAGE; 0003:O80860; -.
DR PaxDb; O80860; -.
DR PRIDE; O80860; -.
DR EnsemblPlants; AT2G30950.1; AT2G30950.1; AT2G30950.
DR EnsemblPlants; AT2G30950.2; AT2G30950.2; AT2G30950.
DR EnsemblPlants; AT2G30950.3; AT2G30950.3; AT2G30950.
DR GeneID; 817646; -.
DR Gramene; AT2G30950.1; AT2G30950.1; AT2G30950.
DR Gramene; AT2G30950.2; AT2G30950.2; AT2G30950.
DR Gramene; AT2G30950.3; AT2G30950.3; AT2G30950.
DR KEGG; ath:AT2G30950; -.
DR Araport; AT2G30950; -.
DR TAIR; locus:2052806; AT2G30950.
DR eggNOG; KOG0731; Eukaryota.
DR HOGENOM; CLU_000688_16_0_1; -.
DR InParanoid; O80860; -.
DR PhylomeDB; O80860; -.
DR BRENDA; 3.4.24.B20; 399.
DR PRO; PR:O80860; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O80860; baseline and differential.
DR Genevisible; O80860; 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:0005777; C:peroxisome; HDA:TAIR.
DR GO; GO:0009579; C:thylakoid; 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:0008237; F:metallopeptidase activity; ISS:TAIR.
DR GO; GO:0009658; P:chloroplast organization; IGI:TAIR.
DR GO; GO:0010205; P:photoinhibition; IMP:TAIR.
DR GO; GO:0048564; P:photosystem I assembly; IMP:TAIR.
DR GO; GO:0010206; P:photosystem II repair; 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 GO; GO:0072593; P:reactive oxygen species metabolic process; IDA:TAIR.
DR GO; GO:0010027; P:thylakoid membrane organization; IMP: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; Direct protein sequencing;
KW Hydrolase; Membrane; Metal-binding; Metalloprotease; Nucleotide-binding;
KW Plastid; Protease; Reference proteome; Thylakoid; Transit peptide;
KW Transmembrane; Transmembrane helix; Ubl conjugation; Zinc.
FT TRANSIT 1..47
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT TRANSIT 48..82
FT /note="Thylakoid"
FT /evidence="ECO:0000305"
FT CHAIN 83..695
FT /note="ATP-dependent zinc metalloprotease FTSH 2,
FT chloroplastic"
FT /id="PRO_0000341328"
FT TOPO_DOM 83..167
FT /note="Lumenal, thylakoid"
FT /evidence="ECO:0000255"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 189..695
FT /note="Stromal"
FT /evidence="ECO:0000255"
FT REGION 673..695
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 674..695
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 489
FT /evidence="ECO:0000250"
FT BINDING 267..274
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 488
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 492
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 566
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 695 AA; 74157 MW; 4F949DCD8E738A0E CRC64;
MAASSACLVG NGLSVNTTTK QRLSKHFSGR QTSFSSVIRT SKVNVVKASL DGKKKQEGRR
DFLKILLGNA GVGLVASGKA NADEQGVSSS RMSYSRFLEY LDKDRVNKVD LYENGTIAIV
EAVSPELGNR VERVRVQLPG LSQELLQKLR AKNIDFAAHN AQEDQGSVLF NLIGNLAFPA
LLIGGLFLLS RRSGGGMGGP GGPGNPLQFG QSKAKFQMEP NTGVTFDDVA GVDEAKQDFM
EVVEFLKKPE RFTAVGAKIP KGVLLIGPPG TGKTLLAKAI AGEAGVPFFS ISGSEFVEMF
VGVGASRVRD LFKKAKENAP CIVFVDEIDA VGRQRGTGIG GGNDEREQTL NQLLTEMDGF
EGNTGVIVVA ATNRADILDS ALLRPGRFDR QVSVDVPDVK GRTDILKVHA GNKKFDNDVS
LEIIAMRTPG FSGADLANLL NEAAILAGRR ARTSISSKEI DDSIDRIVAG MEGTVMTDGK
SKSLVAYHEV GHAVCGTLTP GHDAVQKVTL IPRGQARGLT WFIPSDDPTL ISKQQLFARI
VGGLGGRAAE EIIFGDSEVT TGAVGDLQQI TGLARQMVTT FGMSDIGPWS LMDSSAQSDV
IMRMMARNSM SEKLAEDIDS AVKKLSDSAY EIALSHIKNN REAMDKLVEV LLEKETIGGD
EFRAILSEFT EIPPENRVPS STTTTPASAP TPAAV
