FTSI5_ARATH
ID FTSI5_ARATH Reviewed; 1320 AA.
AC F4J3N2; Q9M8Z0;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Probable inactive ATP-dependent zinc metalloprotease FTSHI 5, chloroplastic;
DE Short=AtFTSHI5 {ECO:0000303|PubMed:22121866};
DE AltName: Full=Protein EMBRYO DEFECTIVE 2458 {ECO:0000303|PubMed:21286311};
DE AltName: Full=Protein FTSH INACTIVE PROTEASE 5 {ECO:0000303|PubMed:22121866};
DE Flags: Precursor;
GN Name=FTSHI5 {ECO:0000303|PubMed:22121866};
GN Synonyms=EMB2458 {ECO:0000303|PubMed:21286311};
GN OrderedLocusNames=At3g04340 {ECO:0000312|Araport:AT3G04340};
GN ORFNames=T6K12.4 {ECO:0000312|EMBL:AAF26780.1};
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] OF 299-1320.
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 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 [5]
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 [6]
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: 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 (Probable).
CC {ECO:0000269|PubMed:24964212, ECO:0000305}.
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 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:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF26780.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AY080629; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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; AC016829; AAF26780.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE74068.1; -; Genomic_DNA.
DR EMBL; AY080629; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_187084.6; NM_111305.7.
DR AlphaFoldDB; F4J3N2; -.
DR SMR; F4J3N2; -.
DR STRING; 3702.AT3G04340.1; -.
DR PaxDb; F4J3N2; -.
DR PRIDE; F4J3N2; -.
DR ProteomicsDB; 247379; -.
DR EnsemblPlants; AT3G04340.1; AT3G04340.1; AT3G04340.
DR GeneID; 819589; -.
DR Gramene; AT3G04340.1; AT3G04340.1; AT3G04340.
DR KEGG; ath:AT3G04340; -.
DR Araport; AT3G04340; -.
DR TAIR; locus:2103055; AT3G04340.
DR eggNOG; KOG0731; Eukaryota.
DR HOGENOM; CLU_004637_0_0_1; -.
DR InParanoid; F4J3N2; -.
DR OMA; VSWFATF; -.
DR OrthoDB; 81008at2759; -.
DR PRO; PR:F4J3N2; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; F4J3N2; baseline and differential.
DR Genevisible; F4J3N2; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009706; C:chloroplast inner membrane; IDA:TAIR.
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:0009506; C:plasmodesma; 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:0045454; P:cell redox homeostasis; IMP:TAIR.
DR GO; GO:0009658; P:chloroplast organization; IMP:TAIR.
DR GO; GO:0045037; P:protein import into chloroplast stroma; IDA:TAIR.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR GO; GO:0080093; P:regulation of photorespiration; IMP:TAIR.
DR Gene3D; 1.20.58.760; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
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; PF01434; Peptidase_M41; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF140990; SSF140990; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Chloroplast; Hydrolase; Membrane; Nucleotide-binding; Plastid;
KW Protease; Reference proteome; Transit peptide; Transmembrane;
KW Transmembrane helix.
FT TRANSIT 1..43
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 44..1320
FT /note="Probable inactive ATP-dependent zinc metalloprotease
FT FTSHI 5, chloroplastic"
FT /id="PRO_0000434644"
FT TRANSMEM 571..591
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 633..653
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 695..715
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 824..831
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1320 AA; 152258 MW; 0EFE8F5F15CBF8F6 CRC64;
MDFISASSLS SPFSTQLSPI YLSSGIVSLK PRHRVKNRNF GSRESNNKSR KIVPIRGCFG
FSGSFLRSKQ SDYGSEAVSE SLRLCGEGNE LVLSSEYNSA KTRESVIQFV TKPLVYALFC
IAIGLSPIRS FQAPALAVPF VSDVIWKKKK ERVREKEVVL KAVDHEFSDY TRRLLETVSV
LLKTIEIVRK ENGEVAEVGA ALDAVKVEKE KLQKEIMSGL YRDMRRLRKE RDLLMKRADK
IVDEALSLKK QSEKLLRKGA REKMEKLEES VDIMESEYNK IWERIDEIDD IILKKETTTL
SFGVRELIFI ERECVELVKS FNRELNQKSF ESVPESSITK LSRSEIKQEL VNAQRKHLEQ
MILPNVLELE EVDPFFDRDS VDFSLRIKKR LEESKKLQRD LQNRIRKRMK KFGEEKLFVQ
KTPEGEAVKG FPEAEVKWMF GEKEVVVPKA IQLHLRHGWK KWQEEAKADL KQKLLEDVDF
GKQYIAQRQE QVLLDRDRVV SKTWYNEDKS RWEMDPMAVP YAVSRKLIDS ARIRHDYAVM
YVALKGDDKE FYVDIKEYEM LFEKFGGFDA LYLKMLACGI PTSVHLMWIP MSELSLQQQF
LLVTRVVSRV FNALRKTQVV SNAKDTVLEK IRNINDDIMM AVVFPVIEFI IPYQLRLRLG
MAWPEEIEQT VGSTWYLQWQ SEAEMNFKSR NTEDFQWFLW FLIRSSIYGF VLYHVFRFLK
RKVPRLLGYG PFRRDPNVRK FWRVKSYFTY RKRRIKQKRK AGIDPIKTAF DRMKRVKNPP
IPLKNFASIE SMREEINEVV AFLQNPKAFQ EMGARAPRGV LIVGERGTGK TSLALAIAAE
ARVPVVNVEA QELEAGLWVG QSAANVRELF QTARDLAPVI IFVEDFDLFA GVRGKFVHTK
QQDHESFINQ LLVELDGFEK QDGVVLMATT RNHKQIDEAL RRPGRMDRVF HLQSPTEMER
ERILHNAAEE TMDRELVDLV DWRKVSEKTT LLRPIELKLV PMALESSAFR SKFLDTDELL
SYVSWFATFS HIVPPWLRKT KVAKTMGKML VNHLGLNLTK DDLENVVDLM EPYGQISNGI
ELLNPTVDWT RETKFPHAVW AAGRALITLL IPNFDVVENL WLEPSSWEGI GCTKITKVTS
GGSAIGNTES RSYLEKKLVF CFGSHIASQM LLPPGDENFL SSSEITKAQE IATRMVLQYG
WGPDDSPAVY YATNAVSALS MGNNHEYEMA GKVEKIYDLA YEKAKGMLLK NRRVLEKITE
ELLEFEILTH KDLERIVHEN GGIREKEPFF LSGTNYNEAL SRSFLDVGDP PETALLSAPT
