FTSI1_ARATH
ID FTSI1_ARATH Reviewed; 946 AA.
AC O22993;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Probable inactive ATP-dependent zinc metalloprotease FTSHI 1, chloroplastic;
DE Short=AtFTSHI1 {ECO:0000303|PubMed:12185496};
DE AltName: Full=Protein ACCUMULATION AND REPLICATION OF CHLOROPLASTS 1 {ECO:0000303|PubMed:16668963};
DE Short=Protein ARC1 {ECO:0000303|PubMed:16668963};
DE AltName: Full=Protein FTSH INACTIVE PROTEASE 1 {ECO:0000303|PubMed:12185496};
DE Flags: Precursor;
GN Name=FTSHI1 {ECO:0000303|PubMed:12185496};
GN Synonyms=ARC1 {ECO:0000303|PubMed:16668963};
GN OrderedLocusNames=At4g23940 {ECO:0000312|Araport:AT4G23940};
GN ORFNames=T19F6.22 {ECO:0000312|EMBL:AAB63626.1},
GN T32A16.10 {ECO:0000312|EMBL:CAB43894.1};
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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 MUTANT ARC1.
RX PubMed=16668963; DOI=10.1104/pp.99.3.1005;
RA Pyke K.A., Leech R.M.;
RT "Chloroplast division and expansion is radically altered by nuclear
RT mutations in Arabidopsis thaliana.";
RL Plant Physiol. 99:1005-1008(1992).
RN [4]
RP MUTAGENESIS OF SER-524.
RX PubMed=12232072; DOI=10.1104/pp.104.1.201;
RA Pyke K.A., Leech R.M.;
RT "A genetic analysis of chloroplast division and expansion in Arabidopsis
RT thaliana.";
RL Plant Physiol. 104:201-207(1994).
RN [5]
RP FUNCTION.
RX PubMed=10417716; DOI=10.1046/j.1365-313x.1999.00500.x;
RA Marrison J.L., Rutherford S.M., Robertson E.J., Lister C., Dean C.,
RA Leech R.M.;
RT "The distinctive roles of five different ARC genes in the chloroplast
RT division process in Arabidopsis.";
RL Plant J. 18:651-662(1999).
RN [6]
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 [7]
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 [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 MUTAGENESIS OF SER-524, FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=22900897; DOI=10.1111/tpj.12001;
RA Kadirjan-Kalbach D.K., Yoder D.W., Ruckle M.E., Larkin R.M.,
RA Osteryoung K.W.;
RT "FtsHi1/ARC1 is an essential gene in Arabidopsis that links chloroplast
RT biogenesis and division.";
RL Plant J. 72:856-867(2012).
RN [10]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
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: Functions in chloroplast biogenesis and chloroplast division
CC (PubMed:10417716, PubMed:22900897). Required for plastid development
CC during embryogenesis (PubMed:22900897, PubMed:24964212). Might be
CC involved in chaperone functions or play a structural role in the
CC thylakoid FtsH complex (PubMed:12185496). {ECO:0000269|PubMed:10417716,
CC ECO:0000269|PubMed:22900897, ECO:0000269|PubMed:24964212,
CC ECO:0000303|PubMed:12185496}.
CC -!- SUBUNIT: Oligomer. {ECO:0000250|UniProtKB:O80860}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast inner membrane
CC {ECO:0000269|PubMed:22900897}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:22900897}.
CC -!- DISRUPTION PHENOTYPE: Embryo defective. {ECO:0000269|PubMed:22900897,
CC ECO:0000269|PubMed:24964212}.
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}.
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DR EMBL; AC002343; AAB63626.1; -; Genomic_DNA.
DR EMBL; AL078468; CAB43894.1; -; Genomic_DNA.
DR EMBL; AL161560; CAB81312.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84830.1; -; Genomic_DNA.
DR PIR; T08913; T08913.
DR RefSeq; NP_567691.1; NM_118526.3.
DR AlphaFoldDB; O22993; -.
DR SMR; O22993; -.
DR STRING; 3702.AT4G23940.1; -.
DR PaxDb; O22993; -.
DR PRIDE; O22993; -.
DR ProteomicsDB; 228920; -.
DR EnsemblPlants; AT4G23940.1; AT4G23940.1; AT4G23940.
DR GeneID; 828494; -.
DR Gramene; AT4G23940.1; AT4G23940.1; AT4G23940.
DR KEGG; ath:AT4G23940; -.
DR Araport; AT4G23940; -.
DR TAIR; locus:2138146; AT4G23940.
DR eggNOG; KOG0731; Eukaryota.
DR HOGENOM; CLU_000688_24_1_1; -.
DR InParanoid; O22993; -.
DR OMA; IEPPLNF; -.
DR OrthoDB; 251379at2759; -.
DR PhylomeDB; O22993; -.
DR PRO; PR:O22993; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O22993; baseline and differential.
DR Genevisible; O22993; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; IDA:TAIR.
DR GO; GO:0009706; C:chloroplast inner membrane; IDA:UniProtKB.
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:0009536; C:plastid; HDA:TAIR.
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:0010020; P:chloroplast fission; IMP:UniProtKB.
DR GO; GO:0009658; P:chloroplast organization; IMP:UniProtKB.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:UniProtKB.
DR GO; GO:0043572; P:plastid fission; IMP:UniProtKB.
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 Plastid inner membrane; Protease; Reference proteome; Transit peptide;
KW Transmembrane; Transmembrane helix.
FT TRANSIT 1..54
FT /note="Chloroplast"
FT /evidence="ECO:0000305"
FT CHAIN 55..946
FT /note="Probable inactive ATP-dependent zinc metalloprotease
FT FTSHI 1, chloroplastic"
FT /evidence="ECO:0000255"
FT /id="PRO_0000434640"
FT TRANSMEM 289..309
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 320..340
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 369..389
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 470..477
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MUTAGEN 524
FT /note="S->P: In arcl/ftsHi1-1; Pale seedlings. Smaller and
FT more numerous chloroplasts with abnormal thylakoid
FT morphology."
FT /evidence="ECO:0000269|PubMed:12232072,
FT ECO:0000269|PubMed:22900897"
SQ SEQUENCE 946 AA; 105543 MW; 2426A066CB7C1859 CRC64;
MASIDNVFSL GTRFSIPENP KRSILKHATT SSFSARTQTR WRAPILRRSF TVLCELKTGS
SSSGETNNSP AADDFVTRVL KENPSQVEPR YRVGDKLYNL KEREDLSKGT NAATGAFEFI
KRKFDSKKKT ETDKSEESVY LSDILREYKG KLYVPEQVFG PELSEEEEFE KNVKDLPKMS
LEDFRKAMEN DKVKLLTSKE VSGVSYTSGY RGFIVDLKEI PGVKSLQRTK WSMKLEVGEA
QALLKEYTGP QYEIERHMTS WVGKVADFPN PVASSISSRV MVELGMVTAV IAAAAVVVGG
FLASAVFAVT SFAFVTTVYV VWPIAKPFLK LFVGVFLGVL EKSWDYIVDV LADGGIFSRI
SDFYTFGGVA SSLEMLKPIL LVVMTMVLLV RFTLSRRPKN FRKWDLWQGI AFSQSKAEAR
VDGSTGVKFA DVAGIDEAVD ELQELVKYLK NPDLFDKMGI KPPHGVLLEG PPGCGKTLVA
KAIAGEAGVP FYQMAGSEFV EVLVGVGSAR IRDLFKRAKV NKPSVIFIDE IDALATRRQG
IFKENSDQLY NAATQERETT LNQLLIELDG FDTGKGVIFL GATNRRDLLD PALLRPGRFD
RKIRVRPPNA KGRLDILKIH ASKVKMSDSV DLSSYASNLP GWSGAKLAQL VQEAALVAVR
KTHNSILQSD MDDAVDRLTV GPTRIGLELG HQGQCRRATT EVGVAITSHL LLRYENAKIE
RCDRVSIIPR GQTLSQVVFH RLDDESYMFG RLPQLLHRLQ VLLGGRAAEE VIYGSDTSKA
SVDYLSDASW LARKILTIWN LENPMVIHGE PPPWRKRPQF VGPRLDFEGS LYDDYDLVEP
PVNFNMDDEV AHRSEELISQ MYNKTVSLLR QNQTALLKTV KVLLNQKEIS GEAIDFILDH
YPPQTPLNSL LQEQNPGSLP FVPEHLRRES GDFVLVNHST DVNAQV
