FTSI4_ARATH
ID FTSI4_ARATH Reviewed; 855 AA.
AC F4KF14; Q8RXW9; Q9FLG0;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Probable inactive ATP-dependent zinc metalloprotease FTSHI 4, chloroplastic;
DE Short=AtFTSHI4 {ECO:0000303|PubMed:12185496};
DE AltName: Full=Protein EMBRYO DEFECTIVE 3144 {ECO:0000303|PubMed:21139083};
DE AltName: Full=Protein FTSH INACTIVE PROTEASE 4 {ECO:0000303|PubMed:12185496};
DE Flags: Precursor;
GN Name=FTSHI4 {ECO:0000303|PubMed:12185496};
GN Synonyms=EMB3144 {ECO:0000303|PubMed:21139083};
GN OrderedLocusNames=At5g64580 {ECO:0000312|Araport:AT5G64580};
GN ORFNames=MUB3.10 {ECO:0000312|EMBL:BAB11425.1};
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=9628582; DOI=10.1093/dnares/5.1.41;
RA Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT features of the regions of 1,456,315 bp covered by nineteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:41-54(1998).
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 517-855.
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 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 [5]
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 [6]
RP IDENTIFICATION, AND DISRUPTION PHENOTYPE.
RX PubMed=21139083; DOI=10.1104/pp.110.168120;
RA Bryant N., Lloyd J., Sweeney C., Myouga F., Meinke D.;
RT "Identification of nuclear genes encoding chloroplast-localized proteins
RT required for embryo development in Arabidopsis.";
RL Plant Physiol. 155:1678-1689(2011).
RN [7]
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 [8]
RP DISRUPTION PHENOTYPE, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP INTERACTION WITH FTSI2, 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: Functions in chloroplast biogenesis and chloroplast division.
CC 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 FtsHi2.
CC {ECO:0000269|PubMed:24964212}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000269|PubMed:24964212}; Single-pass membrane protein
CC {ECO:0000269|PubMed:24964212}.
CC -!- TISSUE SPECIFICITY: Ubiquitous but preferentially expressed in young
CC leaves. {ECO:0000269|PubMed:24964212}.
CC -!- DISRUPTION PHENOTYPE: Embryo defective (PubMed:24964212,
CC PubMed:21139083). Impaired plastid biogenesis and thylakoid
CC differentiation in embryo. Defects in the photosystem II protein
CC complex formation (PubMed:24964212). {ECO:0000269|PubMed:24964212,
CC ECO:0000303|PubMed:21139083}.
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 -!- SEQUENCE CAUTION:
CC Sequence=BAB11425.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB010076; BAB11425.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED97923.1; -; Genomic_DNA.
DR EMBL; AY080633; AAL85979.1; -; mRNA.
DR RefSeq; NP_201263.2; NM_125854.4.
DR AlphaFoldDB; F4KF14; -.
DR SMR; F4KF14; -.
DR IntAct; F4KF14; 1.
DR STRING; 3702.AT5G64580.1; -.
DR PaxDb; F4KF14; -.
DR PRIDE; F4KF14; -.
DR ProMEX; F4KF14; -.
DR ProteomicsDB; 230536; -.
DR EnsemblPlants; AT5G64580.1; AT5G64580.1; AT5G64580.
DR GeneID; 836579; -.
DR Gramene; AT5G64580.1; AT5G64580.1; AT5G64580.
DR KEGG; ath:AT5G64580; -.
DR Araport; AT5G64580; -.
DR TAIR; locus:2174819; AT5G64580.
DR eggNOG; KOG0731; Eukaryota.
DR HOGENOM; CLU_000688_19_0_1; -.
DR InParanoid; F4KF14; -.
DR OMA; DEYMRFS; -.
DR OrthoDB; 163817at2759; -.
DR PRO; PR:F4KF14; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; F4KF14; baseline and differential.
DR Genevisible; F4KF14; 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:0009535; C:chloroplast thylakoid membrane; IDA:UniProtKB.
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:0009793; P:embryo development ending in seed dormancy; 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; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR037219; Peptidase_M41-like.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF140990; SSF140990; 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; Plastid;
KW Protease; Reference proteome; Thylakoid; Transit peptide; Transmembrane;
KW Transmembrane helix.
FT TRANSIT 1..78
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 79..855
FT /note="Probable inactive ATP-dependent zinc metalloprotease
FT FTSHI 4, chloroplastic"
FT /id="PRO_0000434643"
FT TRANSMEM 242..262
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 356..363
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CONFLICT 582..583
FT /note="LR -> FI (in Ref. 3; AAL85979)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 855 AA; 96854 MW; 32CC3BD4702B5AE0 CRC64;
MTFYISSSLT PTHFSKPLNP SNTLFPSQFR GSLSSFVRRR KPTEAKLSSK FNLFPSRRNG
LITCCSTSSF ESTESSVSQE EDAESNRLFE KLRETERERL SNMEELERKA NVQLERQLVM
ASDWSRTLLT MRGKLKGTEW DPETSHRINF SDFMKLLDSN SVQYMEYSNY GQTISVILPY
YKDGEPLGEE EDSKKEIIFR RHIVDRMPID GWNDVWKKLH QQIVNVEVFN VDVVPAEVYT
TVATFVVWSM RLALFVSLYV WIDSITRPIY AKLIPCDLGT PTKKIRQPLK RQALGSLGKS
RAKFISAEEK TGVTFDDFAG QEYIKRELQE IVRILKNDEE FQNKGIYCPK GVLLHGPPGT
GKTLLAKAIA GEAGLPFFAA NGTDFVEMFV GVAASRVKDL FASSRSYAPS IIFIDEIDAI
GSKRGGPDIG GGGAEREQGL LQILTEMDGF KVTTSQVLVI GATNRLDILD PALLRKGRFD
KIIRVGLPSK DGRLAILKVH ARNKFFRSED EKEELLQEVA ENTEDFTGAE LQNVLNEAGI
LTARKDLDYI GREELLEALK RQKGTFETGQ EDSTEVPEEL KLRLAYREAA VAVLACYLPD
QYRPISETDI NSIRSQPNMR YSETSGRVFA RKSDYVNSII RACAPRVVEE EMFGIENLCW
ISAKSTLEAS QRAEFLILQT GMTAFGKAYY RNQRDLVPNL VPKLEALRDE YMRFAVEKCS
SILQEYQSAL EEITDVLLEK GEIKADEIWN IYNTAPRIPQ KPVRPVDEYG ALIYAGRWGI
HGVSLPGRVT FSPGNIGFAT FGAPRPMETQ IISDDTWKLV DEIWDKKVEE IKAEAVIQIE
EEKKKPQILM ATHFF
