FTSI2_ARATH
ID FTSI2_ARATH Reviewed; 876 AA.
AC A8MPR5;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Probable inactive ATP-dependent zinc metalloprotease FTSHI 2, chloroplastic;
DE Short=AtFTSHI2 {ECO:0000303|PubMed:12185496};
DE AltName: Full=Protein EMBRYO DEFECTIVE 2083 {ECO:0000303|PubMed:21286311};
DE AltName: Full=Protein FTSH INACTIVE PROTEASE 2 {ECO:0000303|PubMed:12185496};
DE Flags: Precursor;
GN Name=FTSHI2 {ECO:0000303|PubMed:12185496};
GN Synonyms=EMB2083 {ECO:0000303|PubMed:21286311};
GN OrderedLocusNames=At3g16290 {ECO:0000312|Araport:AT3G16290};
GN ORFNames=MYA6.12 {ECO:0000312|EMBL:BAB01269.1},
GN T2O4.19 {ECO:0000312|EMBL:AAB63647.1};
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=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 412-876.
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
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 IDENTIFICATION, AND DISRUPTION PHENOTYPE.
RX PubMed=21286311; DOI=10.2174/138920210791616716;
RA Hsu S.C., Belmonte M.F., Harada J.J., Inoue K.;
RT "Indispensable roles of plastids in arabidopsis thaliana embryogenesis.";
RL Curr. Genomics 11:338-349(2010).
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, FUNCTION, INTERACTION WITH FTSI4, AND SUBUNIT.
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: Required for plastid development during embryogenesis
CC (PubMed:24964212). Might be involved in chaperone functions or play a
CC structural role in the thylakoid FtsH complex (PubMed:12185496).
CC {ECO:0000269|PubMed:24964212, ECO:0000303|PubMed:12185496}.
CC -!- SUBUNIT: Homooligomer. Interacts with FtsHi4.
CC {ECO:0000269|PubMed:24964212}.
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 ECO:0000303|PubMed:21286311}.
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 -!- CAUTION: Lacks the conserved zinc-binding motif HEXXH, which presumably
CC renders it inactive for proteolysis. {ECO:0000303|PubMed:14996218}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB63647.1; Type=Erroneous gene model prediction; Note=The predicted gene has been split into 2 genes: At3g16290 and At3g16300.; Evidence={ECO:0000305};
CC Sequence=BAB01269.1; Type=Erroneous gene model prediction; Note=The predicted gene has been split into 2 genes: At3g16290 and At3g16300.; Evidence={ECO:0000305};
CC Sequence=BX823945; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB023046; BAB01269.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC001645; AAB63647.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE75794.1; -; Genomic_DNA.
DR EMBL; BX823945; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_566541.1; NM_112500.3.
DR AlphaFoldDB; A8MPR5; -.
DR SMR; A8MPR5; -.
DR IntAct; A8MPR5; 1.
DR STRING; 3702.AT3G16290.1; -.
DR PaxDb; A8MPR5; -.
DR PRIDE; A8MPR5; -.
DR ProteomicsDB; 228889; -.
DR EnsemblPlants; AT3G16290.1; AT3G16290.1; AT3G16290.
DR GeneID; 820876; -.
DR Gramene; AT3G16290.1; AT3G16290.1; AT3G16290.
DR KEGG; ath:AT3G16290; -.
DR Araport; AT3G16290; -.
DR TAIR; locus:2094892; AT3G16290.
DR eggNOG; KOG0731; Eukaryota.
DR HOGENOM; CLU_000688_5_1_1; -.
DR InParanoid; A8MPR5; -.
DR OMA; CINAYTP; -.
DR OrthoDB; 729589at2759; -.
DR PhylomeDB; A8MPR5; -.
DR PRO; PR:A8MPR5; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; A8MPR5; baseline and differential.
DR Genevisible; A8MPR5; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; IDA:TAIR.
DR GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
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:0062091; C:Ycf2/FtsHi complex; 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:0016464; F:chloroplast protein-transporting ATPase activity; IDA:TAIR.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0045037; P:protein import into chloroplast stroma; IDA: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 InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR003959; ATPase_AAA_core.
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.
PE 1: Evidence at protein level;
KW ATP-binding; Chloroplast; Hydrolase; Membrane; Nucleotide-binding; Plastid;
KW Protease; Reference proteome; Transit peptide; Transmembrane;
KW Transmembrane helix.
FT TRANSIT 1..32
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 33..876
FT /note="Probable inactive ATP-dependent zinc metalloprotease
FT FTSHI 2, chloroplastic"
FT /id="PRO_0000434641"
FT TRANSMEM 59..79
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 304..324
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 256..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 350..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 450..457
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 876 AA; 99864 MW; 35F2747DBAD955AF CRC64;
MACRFPLHSS SPSQFLSPEN RQRLPRNYPS ISCQNNSATN VVHEDGDDND KAKTNQVNLL
AIPITLTIIS ASLAKPSFAA AKVTERKRTQ KKPQEALTLE QLKAWSKDLP VVSNRIPYTD
ILSLKAEGKL KHVIKPPNLS LRQKAEPVLV VLEDSRVLRT VLPSLEGNKR FWEQWDELGI
DVQCVNAYTP PVKRPPVPSP YLGFLWKVPA YMLTWVKPKK ESKRAAELKR MREDFKRQRK
EEIETMKEER VMMEKTMKAQ KKQQERKKRK AVRKKKYEES LREARKNYRD MADMWARLAQ
DPNVATALGL VFFYIFYRVV VLNYRKQKKD YEDRLKIEKA EADERKKMRE LEREMEGIEE
EDEEVEEGTG EKNPYLQMAM QFMKSGARVR RASNKRLPEY LERGVDVKFT DVAGLGKIRL
ELEEIVKFFT HGEMYRRRGV KIPGGILLCG PPGVGKTLLA KAVAGEAGVN FFSISASQFV
EIYVGVGASR VRALYQEARE NAPSVVFIDE LDAVGRERGL IKGSGGQERD ATLNQLLVSL
DGFEGRGEVI TIASTNRPDI LDPALVRPGR FDRKIFIPKP GLIGRMEILQ VHARKKPMAE
DLDYMAVASM TDGMVGAELA NIVEIAAINM MRDGRTELTT DDLLQAAQIE ERGMLDRKDR
SLETWRQVAI NEAAMAVVAV NFPDMKNIEF LTINPRAGRE LGYVRVKMDH IKFKEGMLSR
QSILDHITVQ LAPRAADELW YGEDQLSTIW AETSDNARSA ARSLVLGGLS DKHHGLNNFW
VADRINDIDV EALRILNMCY ERAKEILGRN RTLMDEVVEK LVQKKSLTKQ EFFTLVELYG
SSKPMPPSIL ELRKIKRLEL EEMVLKLDMT TARNSS
