FTSH6_ARATH
ID FTSH6_ARATH Reviewed; 688 AA.
AC Q1PDW5; Q9LXF7;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=ATP-dependent zinc metalloprotease FTSH 6, chloroplastic;
DE Short=AtFTSH6;
DE EC=3.4.24.-;
DE Flags: Precursor;
GN Name=FTSH6; OrderedLocusNames=At5g15250; ORFNames=F8M21.140;
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT "Simultaneous high-throughput recombinational cloning of open reading
RT frames in closed and open configurations.";
RL Plant Biotechnol. J. 4:317-324(2006).
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 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 [6]
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 [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 FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
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).
CC -!- FUNCTION: Probable ATP-dependent zinc metallopeptidase. Involved in the
CC degradation of the light-harvesting complex of photosystem II (LHC II)
CC during senescence or high light acclimation.
CC {ECO:0000269|PubMed:16157880}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000305};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000269|PubMed:14630971, ECO:0000269|PubMed:16157880}; Single-pass
CC membrane protein {ECO:0000269|PubMed:14630971,
CC ECO:0000269|PubMed:16157880}; Stromal side
CC {ECO:0000269|PubMed:14630971, ECO:0000269|PubMed:16157880}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q1PDW5-1; Sequence=Displayed;
CC -!- DOMAIN: The conserved lumenal (CL) domain (84-162) is present only in
CC some FtsH homologs from organisms performing oxygenic photosynthesis.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:16157880}.
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=CAB89335.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL353993; CAB89335.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED92136.1; -; Genomic_DNA.
DR EMBL; DQ446953; ABE66158.1; -; mRNA.
DR PIR; T49960; T49960.
DR RefSeq; NP_568311.2; NM_121529.2. [Q1PDW5-1]
DR AlphaFoldDB; Q1PDW5; -.
DR SMR; Q1PDW5; -.
DR STRING; 3702.AT5G15250.2; -.
DR MEROPS; M41.019; -.
DR PaxDb; Q1PDW5; -.
DR PRIDE; Q1PDW5; -.
DR EnsemblPlants; AT5G15250.1; AT5G15250.1; AT5G15250. [Q1PDW5-1]
DR GeneID; 831377; -.
DR Gramene; AT5G15250.1; AT5G15250.1; AT5G15250. [Q1PDW5-1]
DR KEGG; ath:AT5G15250; -.
DR Araport; AT5G15250; -.
DR eggNOG; KOG0731; Eukaryota.
DR HOGENOM; CLU_000688_16_0_1; -.
DR InParanoid; Q1PDW5; -.
DR OMA; QVMQFGQ; -.
DR OrthoDB; 217929at2759; -.
DR PhylomeDB; Q1PDW5; -.
DR BRENDA; 3.4.24.B20; 399.
DR PRO; PR:Q1PDW5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q1PDW5; baseline and differential.
DR Genevisible; Q1PDW5; AT.
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: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:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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; 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 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Chloroplast; Hydrolase; Membrane;
KW Metal-binding; Metalloprotease; Nucleotide-binding; Plastid; Protease;
KW Reference proteome; Thylakoid; Transit peptide; Transmembrane;
KW Transmembrane helix; Zinc.
FT TRANSIT 1..75
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT TRANSIT 76..83
FT /note="Thylakoid"
FT /evidence="ECO:0000250"
FT CHAIN 84..688
FT /note="ATP-dependent zinc metalloprotease FTSH 6,
FT chloroplastic"
FT /id="PRO_0000341331"
FT TOPO_DOM 84..168
FT /note="Lumenal, thylakoid"
FT /evidence="ECO:0000255"
FT TRANSMEM 169..189
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 190..688
FT /note="Stromal"
FT /evidence="ECO:0000255"
FT REGION 25..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 486
FT /evidence="ECO:0000250"
FT BINDING 264..271
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 485
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 489
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 563
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 688 AA; 74515 MW; DEE8705995F716A6 CRC64;
MKMASSSSAL SFPLSNIPTC SKKSQQFQKP ASLSKSSHTH KPSLKTQILH HKFTKRNLLS
LTTALGFTSA LGTVLAHPAK AEPEAPIEAT SNRMSYSRFL QHLKENEVKK VDLIENGTVA
IVEISNPVVG KIQRVRVNLP GLPVDLVREM KEKNVDFAAH PMNVNWGAFL LNFLGNLGFP
LILLVSLLLT SSSRRNPAGP NLPFGLGRSK AKFQMEPNTG ITFEDVAGVD EAKQDFEEIV
EFLKTPEKFS ALGAKIPKGV LLTGPPGTGK TLLAKAIAGE AGVPFFSLSG SEFIEMFVGV
GASRARDLFN KAKANSPCIV FIDEIDAVGR MRGTGIGGGN DEREQTLNQI LTEMDGFAGN
TGVIVIAATN RPEILDSALL RPGRFDRQVS VGLPDIRGRE EILKVHSRSK KLDKDVSLSV
IAMRTPGFSG ADLANLMNEA AILAGRRGKD KITLTEIDDS IDRIVAGMEG TKMIDGKSKA
IVAYHEVGHA ICATLTEGHD PVQKVTLVPR GQARGLTWFL PGEDPTLVSK QQLFARIVGG
LGGRAAEDVI FGEPEITTGA AGDLQQVTEI ARQMVTMFGM SEIGPWALTD PAVKQNDVVL
RMLARNSMSE KLAEDIDSCV KKIIGDAYEV AKKHVRNNRE AIDKLVDVLL EKETLTGDEF
RAILSEYTDQ PLNTDGDVRI RINDLISV
