FTSH4_ARATH
ID FTSH4_ARATH Reviewed; 717 AA.
AC O80983; Q56ZW8;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=ATP-dependent zinc metalloprotease FTSH 4, mitochondrial;
DE Short=AtFTSH4;
DE EC=3.4.24.-;
DE Flags: Precursor;
GN Name=FTSH4; OrderedLocusNames=At2g26140; ORFNames=T19L18.5;
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=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 [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] OF 666-717.
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 [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 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 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 [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 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, 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).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND CLEAVAGE OF TRANSIT PEPTIDE AFTER
RP GLN-53.
RX PubMed=25732537; DOI=10.1093/jxb/erv064;
RA Carrie C., Venne A.S., Zahedi R.P., Soll J.;
RT "Identification of cleavage sites and substrate proteins for two
RT mitochondrial intermediate peptidases in Arabidopsis thaliana.";
RL J. Exp. Bot. 66:2691-2708(2015).
CC -!- FUNCTION: Probable ATP-dependent zinc metallopeptidase. Involved in the
CC assembly and/or stability of the complex 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 -!- SUBUNIT: Homooligomer. The complex formed by FTSH4 does not contain
CC FTSH11. {ECO:0000269|PubMed:16247555}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:14630971, ECO:0000269|PubMed:16247555,
CC ECO:0000269|Ref.9, ECO:0000305|PubMed:25732537}; Single-pass membrane
CC protein {ECO:0000269|PubMed:14630971, ECO:0000269|PubMed:16247555,
CC ECO:0000269|Ref.9}; Intermembrane side {ECO:0000269|PubMed:14630971,
CC ECO:0000269|PubMed:16247555, ECO:0000269|Ref.9}.
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; AC004747; AAC31223.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC07799.1; -; Genomic_DNA.
DR EMBL; AK220842; BAD94171.1; -; mRNA.
DR PIR; T02610; T02610.
DR RefSeq; NP_565616.1; NM_128172.4.
DR AlphaFoldDB; O80983; -.
DR SMR; O80983; -.
DR BioGRID; 2506; 2.
DR STRING; 3702.AT2G26140.1; -.
DR MEROPS; M41.018; -.
DR SwissPalm; O80983; -.
DR PaxDb; O80983; -.
DR PRIDE; O80983; -.
DR ProteomicsDB; 228957; -.
DR EnsemblPlants; AT2G26140.1; AT2G26140.1; AT2G26140.
DR GeneID; 817154; -.
DR Gramene; AT2G26140.1; AT2G26140.1; AT2G26140.
DR KEGG; ath:AT2G26140; -.
DR Araport; AT2G26140; -.
DR TAIR; locus:2057386; AT2G26140.
DR eggNOG; KOG0734; Eukaryota.
DR HOGENOM; CLU_000688_9_3_1; -.
DR InParanoid; O80983; -.
DR OMA; YTDMTEQ; -.
DR OrthoDB; 217929at2759; -.
DR PhylomeDB; O80983; -.
DR BRENDA; 3.4.24.B19; 399.
DR BRENDA; 3.4.24.B20; 399.
DR PRO; PR:O80983; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O80983; baseline and differential.
DR Genevisible; O80983; AT.
DR GO; GO:0009534; C:chloroplast thylakoid; IBA:GO_Central.
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; 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; 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:0010073; P:meristem maintenance; IMP:TAIR.
DR GO; GO:0006508; P:proteolysis; 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; 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; 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..53
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:25732537"
FT CHAIN 54..717
FT /note="ATP-dependent zinc metalloprotease FTSH 4,
FT mitochondrial"
FT /id="PRO_0000341330"
FT TRANSMEM 181..201
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 487
FT /evidence="ECO:0000250"
FT BINDING 267..274
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 486
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 490
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 564
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 717 AA; 77275 MW; F9110BCB88428CAD CRC64;
MAWRRIITKV SSHERELSSL RSLLVRAYSS FPRVGVTGAV GGGGASLPRT RFQSSYVGSF
ARRVRDREEV NEVAHLRELI RRNDPEAVIR MFESQPSLHA NASALSEYIK ALVKVDRLDQ
SELVRTLQRG IAGVAREEET FGGLGAFRNV GKPTKDGVLG TASAPIHTIS TERTHFKEQL
WSTIRTIGVG FLLISGIGAL IEDRGIGKGL GLHEEVQPSM DSSTKFSDVK GVDEAKAELE
EIVHYLRDPK RFTRLGGKLP KGVLLVGPPG TGKTMLARAI AGEAGVPFFS CSGSEFEEMF
VGVGARRVRD LFSAAKKCSP CIIFIDEIDA IGGSRNPKDQ QYMKMTLNQM LVELDGFKQN
EGIIVVAATN FPESLDKALV RPGRFDRHIV VPNPDVEGRR QILESHMSKV LKAEDVDLMI
IARGTPGFSG ADLANLVNVA ALKAAMDGSK DVTMSDLEFA KDRIMMGSER KSAVISDESR
KLTAFHEGGH ALVAIHTEGA LPVHKATIVP RGMALGMVSQ LPDKDETSIS RKQMLARLDV
CMGGRVAEEL IFGESEVTSG ASSDLEQATK LARAMVTKFG MSKEVGLVAH NYDDNGKSMS
TETRLLIESE VKQLLEKAYN NAKTILTVYN KELHALANAL LQHETLSGKQ IKELLTDLNS
PLLQKRQEVV TKQSNPVPPS TPSSASSAAA AAAAAAAAAA AAAATAATKG KDMAPVS
