FTSHA_ARATH
ID FTSHA_ARATH Reviewed; 813 AA.
AC Q8VZI8; Q0WLM5; Q9LNX5;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=ATP-dependent zinc metalloprotease FTSH 10, mitochondrial;
DE Short=AtFTSH10;
DE EC=3.4.24.-;
DE Flags: Precursor;
GN Name=FTSH10; OrderedLocusNames=At1g07510; ORFNames=F22G5.10, F22G5_9;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 641-813.
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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
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 [7]
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 [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 FUNCTION, AND SUBCELLULAR LOCATION.
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).
CC -!- FUNCTION: Probable ATP-dependent zinc metallopeptidase. Involved in the
CC assembly and/or stability of the complexes I and V of the mitochondrial
CC oxidative phosphorylation system. {ECO:0000269|Ref.9}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:14630971, ECO:0000269|PubMed:14671022,
CC ECO:0000269|Ref.9}; Single-pass membrane protein
CC {ECO:0000269|PubMed:14630971, ECO:0000269|PubMed:14671022,
CC ECO:0000269|Ref.9}; Matrix side {ECO:0000269|PubMed:14630971,
CC ECO:0000269|PubMed:14671022, ECO:0000269|Ref.9}.
CC -!- INDUCTION: By high light. {ECO:0000269|PubMed:15266057}.
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=AAF79577.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC022464; AAF79577.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE28137.1; -; Genomic_DNA.
DR EMBL; AY064138; AAL36045.1; -; mRNA.
DR EMBL; AY124808; AAM70517.1; -; mRNA.
DR EMBL; AK230173; BAF01982.1; -; mRNA.
DR PIR; H86209; H86209.
DR RefSeq; NP_172231.2; NM_100625.4.
DR AlphaFoldDB; Q8VZI8; -.
DR SMR; Q8VZI8; -.
DR BioGRID; 22506; 6.
DR STRING; 3702.AT1G07510.1; -.
DR MEROPS; M41.023; -.
DR PaxDb; Q8VZI8; -.
DR PRIDE; Q8VZI8; -.
DR ProteomicsDB; 228945; -.
DR EnsemblPlants; AT1G07510.1; AT1G07510.1; AT1G07510.
DR GeneID; 837265; -.
DR Gramene; AT1G07510.1; AT1G07510.1; AT1G07510.
DR KEGG; ath:AT1G07510; -.
DR Araport; AT1G07510; -.
DR TAIR; locus:2025052; AT1G07510.
DR eggNOG; KOG0731; Eukaryota.
DR HOGENOM; CLU_000688_23_2_1; -.
DR InParanoid; Q8VZI8; -.
DR OMA; VHHYLSR; -.
DR OrthoDB; 217929at2759; -.
DR PhylomeDB; Q8VZI8; -.
DR BRENDA; 3.4.24.B20; 399.
DR PRO; PR:Q8VZI8; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8VZI8; baseline and differential.
DR Genevisible; Q8VZI8; AT.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; HDA:TAIR.
DR GO; GO:0005745; C:m-AAA complex; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA: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; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0034982; P:mitochondrial protein processing; IBA:GO_Central.
DR GO; GO:0065003; P:protein-containing complex assembly; IBA:GO_Central.
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; Hydrolase; Membrane; Metal-binding; Metalloprotease;
KW Mitochondrion; Mitochondrion inner membrane; Nucleotide-binding; Protease;
KW Reference proteome; Transit peptide; Transmembrane; Transmembrane helix;
KW Zinc.
FT TRANSIT 1..86
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 87..813
FT /note="ATP-dependent zinc metalloprotease FTSH 10,
FT mitochondrial"
FT /id="PRO_0000341335"
FT TRANSMEM 139..157
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 93..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 764..813
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..125
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 776..797
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 593
FT /evidence="ECO:0000250"
FT BINDING 367..374
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 592
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 596
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 668
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT CONFLICT 642
FT /note="D -> N (in Ref. 4; BAF01982)"
FT /evidence="ECO:0000305"
FT CONFLICT 675
FT /note="M -> L (in Ref. 4; BAF01982)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 813 AA; 89555 MW; 149D65CC4DC4C7EC CRC64;
MIFSKLGSSL ARSSRSKGFV YGGGVRSAVF NQGRLRAPQN LEAAVNQVDG GLGFLRRHFA
SFAARKGLEA GDLSRAFANP RLRRFFSSQT PKKKNYENYY PKDSKKAPKN EQKSESRDGS
KKNENENAGD AFSNEYQNML IPLMAIALIL STFSLGSREQ QQISFQEFKN KLLEAGLVDH
IDVSNKEVAK VYVRSSPKSQ TTEEVVQGPG NGVPAKGRGG QYKYYFNIGS VESFEEKLEE
AQEAIGVNSH DFVPVTYVSE TIWYQELLRF APTLLLVATL IFGARRMQGG LGGLGGPGGK
AGRGIFNIGK AQITRADKNS KNKIYFKDVA GCEEAKQEIM EFVHFLQNPK KYEDLGAKIP
KGALLVGPPG TGKTLLAKAT AGESAVPFLS ISGSDFMEMF VGVGPSRVRN LFQEARQCAP
SIIFIDEIDA IGRARGRGGF SGGNDEREST LNQLLVEMDG FGTTAGVVVL AGTNRPDILD
KALLRPGRFD RQITIDKPDI KGRDQIFQIY LKKIKLDHEP SYYSQRLAAL TPGFAGADIA
NVCNEAALIA ARHEGATVTM AHFDSAIDRV IGGLEKKNRV ISKLERRTVA YHESGHAVAG
WFLEHAEPLL KVTIVPRGTA ALGFAQYVPN ENLLMTKEQL FDMTCMTLGG RAAEQVLIGR
ISTGAQNDLE KVTKMTYAQV AVYGFSDKIG LLSFPQREDE FSKPYSNRTG AMIDEEVREW
VGKAYKRTVE LIEEHKEQVA QIAELLLEKE VLHQDDLTKV LGERPFKSGE TTNYDRFKSG
FEESEKESQK ESVPVKPVED DGIPPLEPQV VPT
