FTSHB_ARATH
ID FTSHB_ARATH Reviewed; 806 AA.
AC Q9FGM0;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=ATP-dependent zinc metalloprotease FTSH 11, chloroplastic/mitochondrial;
DE Short=AtFTSH11;
DE EC=3.4.24.-;
DE Flags: Precursor;
GN Name=FTSH11; OrderedLocusNames=At5g53170; ORFNames=MFH8.11;
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;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
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 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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=14671022; DOI=10.1105/tpc.016055;
RA Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J.,
RA Millar A.H.;
RT "Experimental analysis of the Arabidopsis mitochondrial proteome highlights
RT signaling and regulatory components, provides assessment of targeting
RT prediction programs, and indicates plant-specific mitochondrial proteins.";
RL Plant Cell 16:241-256(2004).
RN [6]
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).
RN [7]
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 [8]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=16247555; DOI=10.1007/s11103-005-8766-3;
RA Urantowka A., Knorpp C., Olczak T., Kolodziejczak M., Janska H.;
RT "Plant mitochondria contain at least two i-AAA-like complexes.";
RL Plant Mol. Biol. 59:239-252(2005).
RN [9]
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 [10]
RP FUNCTION, AND MUTAGENESIS OF GLY-564.
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 [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX DOI=10.1111/j.1399-3054.2006.00835.x;
RA Kolodziejczak M., Gibala M., Urantowka A., Janska H.;
RT "The significance of Arabidopsis AAA proteases for activity and
RT assembly/stability of mitochondrial OXPHOS complexes.";
RL Physiol. Plantarum 129:135-142(2007).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [13]
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: Probable ATP-dependent zinc metallopeptidase. Involved in the
CC assembly and/or stability of the complexes I and V. Involved in
CC thermotolerance but not in high light stress resistance or in the
CC assembly/stability of the complexes I and V of the mitochondrial
CC oxidative phosphorylation system. {ECO:0000269|PubMed:16157880,
CC ECO:0000269|PubMed:16972866, ECO:0000269|Ref.11}.
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: Homooligomer. {ECO:0000305|PubMed:16247555}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass
CC membrane protein; Intermembrane side. Plastid, chloroplast thylakoid
CC membrane; Single-pass membrane protein; Stromal side.
CC -!- INDUCTION: By high light. {ECO:0000269|PubMed:15266057}.
CC -!- MISCELLANEOUS: In contrast to fungi and metazoa, plant mitochondria
CC have more than one i-AAA-like complexes.
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; AB025622; BAB08420.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96317.1; -; Genomic_DNA.
DR EMBL; AY091086; AAM13906.1; -; mRNA.
DR EMBL; AY123027; AAM67560.1; -; mRNA.
DR RefSeq; NP_568787.1; NM_124696.4.
DR AlphaFoldDB; Q9FGM0; -.
DR SMR; Q9FGM0; -.
DR STRING; 3702.AT5G53170.1; -.
DR MEROPS; M41.018; -.
DR iPTMnet; Q9FGM0; -.
DR PaxDb; Q9FGM0; -.
DR PRIDE; Q9FGM0; -.
DR ProteomicsDB; 230001; -.
DR EnsemblPlants; AT5G53170.1; AT5G53170.1; AT5G53170.
DR GeneID; 835398; -.
DR Gramene; AT5G53170.1; AT5G53170.1; AT5G53170.
DR KEGG; ath:AT5G53170; -.
DR Araport; AT5G53170; -.
DR TAIR; locus:2163736; AT5G53170.
DR eggNOG; KOG0734; Eukaryota.
DR HOGENOM; CLU_000688_9_3_1; -.
DR InParanoid; Q9FGM0; -.
DR OMA; KACLFKL; -.
DR OrthoDB; 217929at2759; -.
DR PhylomeDB; Q9FGM0; -.
DR BRENDA; 3.4.24.B20; 399.
DR PRO; PR:Q9FGM0; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FGM0; baseline and differential.
DR Genevisible; Q9FGM0; 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; IBA:GO_Central.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
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; IBA:GO_Central.
DR GO; GO:0010304; P:PSII associated light-harvesting complex II catabolic process; TAS:TAIR.
DR GO; GO:0009408; P:response to heat; 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; Hydrolase; Membrane; Metal-binding;
KW Metalloprotease; Mitochondrion; Mitochondrion inner membrane;
KW Nucleotide-binding; Plastid; Protease; Reference proteome; Thylakoid;
KW Transit peptide; Transmembrane; Transmembrane helix; Zinc.
FT TRANSIT 1..63
FT /note="Chloroplast and mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 64..806
FT /note="ATP-dependent zinc metalloprotease FTSH 11,
FT chloroplastic/mitochondrial"
FT /id="PRO_0000341336"
FT TRANSMEM 301..321
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 106..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 621
FT /evidence="ECO:0000250"
FT BINDING 402..409
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 620
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 624
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 698
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT MUTAGEN 564
FT /note="G->A: In atts244; loss of thermotolerance."
FT /evidence="ECO:0000269|PubMed:16972866"
SQ SEQUENCE 806 AA; 88717 MW; 63C1B733C583D974 CRC64;
MSSSTLQASL FLRPPLHTSS FKLYPCLFSS SSLSFCPQSL SSFYRLSSVL HNSRFRPLPC
SLRQDNVASD SDFIPKDSAF EVTDSAESNR LVSDTEVSEL ETNDRFVGGE ETKSGGEEAE
VSNGVTEGKE EDQKKSKFRI VVLMMALWAA IKRAIEKVME WEWLSWWPFS RQEKRLEKLI
AEADANPKDA ALQGALLAEL NKHIPEAVVQ RFEQREHTVD SRGVAEYIRA LVITNAISEY
LPDEQTGKPS SLPALLQELK HRASGNMDES FVNPGISEKQ PLHVTMVNPK VSNKSRFAQE
LVSTILFTVA VGLVWIMGAA ALQKYIGSLG GIGTSGVGSS SSYSPKELNK EITPEKNVKT
FKDVKGCDDA KQELEEVVEY LKNPSKFTRL GGKLPKGILL TGAPGTGKTL LAKAIAGEAG
VPFFYRAGSE FEEMFVGVGA RRVRSLFQAA KKKAPCIIFI DEIDAVGSTR KQWEGHTKKT
LHQLLVEMDG FEQNEGIIVM AATNLPDILD PALTRPGRFD RHIVVPSPDV RGREEILELY
LQGKPMSEDV DVKAIARGTP GFNGADLANL VNIAAIKAAV EGAEKLSSEQ LEFAKDRIVM
GTERKTMFVS EDSKKLTAYH ESGHAIVALN TKGAHPIHKA TIMPRGSALG MVTQLPSNDE
TSVSKRQLLA RLDVCMGGRV AEELIFGLDH ITTGASSDLS QATELAQYMV SSCGMSEAIG
PVHIKERPSS DMQSRIDAEV VKLLREAYER VKSLLKRHEK QLHTLANALL EYETLTAEDI
KRILLPKQEG EKFEEQQQEE GDLVLA
