FTSI3_ARATH
ID FTSI3_ARATH Reviewed; 622 AA.
AC Q9M895; Q8LBL6;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Probable inactive ATP-dependent zinc metalloprotease FTSHI 3, chloroplastic;
DE Short=AtFTSHI3 {ECO:0000303|PubMed:12185496};
DE AltName: Full=Protein FTSH INACTIVE PROTEASE 3 {ECO:0000303|PubMed:12185496};
DE Flags: Precursor;
GN Name=FTSHI3 {ECO:0000303|PubMed:12185496};
GN OrderedLocusNames=At3g02450 {ECO:0000312|Araport:AT3G02450};
GN ORFNames=F16B3.8 {ECO:0000312|EMBL:AAF32452.1};
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP IDENTIFICATION, AND NOMENCLATURE.
RX PubMed=12185496; DOI=10.1007/s00294-002-0309-8;
RA Sokolenko A., Pojidaeva E., Zinchenko V., Panichkin V., Glaser V.M.,
RA Herrmann R.G., Shestakov S.V.;
RT "The gene complement for proteolysis in the cyanobacterium Synechocystis
RT sp. PCC 6803 and Arabidopsis thaliana chloroplasts.";
RL Curr. Genet. 41:291-310(2002).
RN [6]
RP IDENTIFICATION.
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-86, AND IDENTIFICATION BY
RP 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).
RN [8]
RP GENE FAMILY, AND REVIEW.
RX PubMed=22121866; DOI=10.1111/j.1399-3054.2011.01548.x;
RA Wagner R., Aigner H., Funk C.;
RT "FtsH proteases located in the plant chloroplast.";
RL Physiol. Plantarum 145:203-214(2012).
RN [9]
RP DISRUPTION PHENOTYPE.
RX PubMed=24964212; DOI=10.1371/journal.pone.0099741;
RA Lu X., Zhang D., Li S., Su Y., Liang Q., Meng H., Shen S., Fan Y., Liu C.,
RA Zhang C.;
RT "FtsHi4 is essential for embryogenesis due to its influence on chloroplast
RT development in Arabidopsis.";
RL PLoS ONE 9:E99741-E99741(2014).
CC -!- FUNCTION: Might be involved in chaperone functions or play a structural
CC role in the thylakoid FtsH complex. {ECO:0000303|PubMed:12185496}.
CC -!- SUBUNIT: Oligomer. {ECO:0000250|UniProtKB:O80860}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane {ECO:0000255};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Embryo defective. {ECO:0000269|PubMed:24964212}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
CC -!- CAUTION: Lacks the conserved zinc-binding motif HEXXH, which presumably
CC renders it inactive for proteolysis. {ECO:0000303|PubMed:14996218}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC021640; AAF32452.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE73809.1; -; Genomic_DNA.
DR EMBL; AY062811; AAL32889.1; -; mRNA.
DR EMBL; BT008384; AAP37743.1; -; mRNA.
DR EMBL; AY087136; AAM64694.1; -; mRNA.
DR RefSeq; NP_186894.1; NM_111112.4.
DR AlphaFoldDB; Q9M895; -.
DR SMR; Q9M895; -.
DR STRING; 3702.AT3G02450.1; -.
DR iPTMnet; Q9M895; -.
DR PaxDb; Q9M895; -.
DR PRIDE; Q9M895; -.
DR ProteomicsDB; 230535; -.
DR EnsemblPlants; AT3G02450.1; AT3G02450.1; AT3G02450.
DR GeneID; 821139; -.
DR Gramene; AT3G02450.1; AT3G02450.1; AT3G02450.
DR KEGG; ath:AT3G02450; -.
DR Araport; AT3G02450; -.
DR TAIR; locus:2076929; AT3G02450.
DR eggNOG; KOG0731; Eukaryota.
DR HOGENOM; CLU_000688_21_11_1; -.
DR InParanoid; Q9M895; -.
DR OMA; WPCYARR; -.
DR OrthoDB; 1227956at2759; -.
DR PRO; PR:Q9M895; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M895; baseline and differential.
DR Genevisible; Q9M895; AT.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009534; C:chloroplast thylakoid; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
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; 3.40.50.300; -; 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; IPR027417; P-loop_NTPase.
DR InterPro; IPR011546; Pept_M41_FtsH_extracell.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF06480; FtsH_ext; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00674; AAA; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Chloroplast; Hydrolase; Membrane; Nucleotide-binding;
KW Phosphoprotein; Plastid; Protease; Reference proteome; Transit peptide;
KW Transmembrane; Transmembrane helix.
FT TRANSIT 1..42
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 43..622
FT /note="Probable inactive ATP-dependent zinc metalloprotease
FT FTSHI 3, chloroplastic"
FT /id="PRO_0000434642"
FT TRANSMEM 147..167
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 291..311
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 600..622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 374..381
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 86
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT CONFLICT 246
FT /note="V -> I (in Ref. 4; AAM64694)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 622 AA; 69410 MW; 1E22381B11D4A6A8 CRC64;
MATFNVLCSN RFRFNGGYSP EKFNRKVSSR SSELNVCVSR IRTQSFSCRR LGGFMEIGET
RLGVIRVHGD SRNRFSCNSE IKRLVTGDYG DKETRIGENG RNKGKRRRFS LRLRPRLRLV
RMRLGRFDFR ASMEDFRYFL KKNLKRVILS TGVALIFGLC YLFLRLTAVP SPSIVPYSDF
VTNLRGGSVS KVLLEEGSRR IYYNTDENVE VVDDVHKSET LEDPAIQIDG GTVTEAVTKD
DTPRKVRALP PVWKYVTRKV DHDEKFLLSL MREKGITYSS APQSALMSMR TTLITIISLW
IPLTPLMWLL YRQLSASNSP AKKRRSKNPT VGFDDVEGVD SAKDELVEIV SCLQGSINYK
KLGARLPRGV LLVGPPGTGK TLLARAVAGE AGVPFFSVSA SEFVELFVGR GAARIRDLFN
AARKNSPSII FIDELDAVGG KRGRSFNDER DQTLNQLLTE MDGFESDTKV IVIAATNRPE
ALDSALCRPG RFSRKVLVAE PDQEGRRKIL AIHLRDVPLE EDAFLICDLV ASLTPGFVGA
DLANIVNEAA LLAARRGGEA VAREDIMEAI ERAKFGINDK EARPRTLGNE LSKMFPWMPS
LARRNGPDQD GLQGPLGYQT LS
