FTSHC_ARATH
ID FTSHC_ARATH Reviewed; 1008 AA.
AC Q9SAJ3; Q94C56;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=ATP-dependent zinc metalloprotease FTSH 12, chloroplastic;
DE Short=AtFTSH12;
DE EC=3.4.24.-;
DE Flags: Precursor;
GN Name=FTSH12; OrderedLocusNames=At1g79560; ORFNames=T8K14.2;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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 363-1008.
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 SUBCELLULAR LOCATION.
RX PubMed=14630971; DOI=10.1105/tpc.017319;
RA Sakamoto W., Zaltsman A., Adam Z., Takahashi Y.;
RT "Coordinated regulation and complex formation of yellow variegated1 and
RT yellow variegated2, chloroplastic FtsH metalloproteases involved in the
RT repair cycle of photosystem II in Arabidopsis thylakoid membranes.";
RL Plant Cell 15:2843-2855(2003).
RN [5]
RP INDUCTION BY HIGH LIGHT.
RX PubMed=15266057; DOI=10.1104/pp.104.043299;
RA Sinvany-Villalobo G., Davydov O., Ben-Ari G., Zaltsman A., Raskind A.,
RA Adam Z.;
RT "Expression in multigene families. Analysis of chloroplast and
RT mitochondrial proteases.";
RL Plant Physiol. 135:1336-1345(2004).
RN [6]
RP GENE FAMILY, AND NOMENCLATURE.
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).
CC -!- FUNCTION: Probable ATP-dependent zinc metallopeptidase.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000269|PubMed:14630971}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:14630971}; Stromal side
CC {ECO:0000269|PubMed:14630971}.
CC -!- INDUCTION: By high light. {ECO:0000269|PubMed:15266057}.
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 -!- SEQUENCE CAUTION:
CC Sequence=AAD30220.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC007202; AAD30220.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE36264.1; -; Genomic_DNA.
DR EMBL; AY035166; AAK59670.2; -; mRNA.
DR PIR; A96827; A96827.
DR RefSeq; NP_565212.1; NM_106604.4.
DR AlphaFoldDB; Q9SAJ3; -.
DR SMR; Q9SAJ3; -.
DR BioGRID; 29513; 1.
DR STRING; 3702.AT1G79560.1; -.
DR MEROPS; M41.A06; -.
DR iPTMnet; Q9SAJ3; -.
DR PaxDb; Q9SAJ3; -.
DR PRIDE; Q9SAJ3; -.
DR ProteomicsDB; 230002; -.
DR EnsemblPlants; AT1G79560.1; AT1G79560.1; AT1G79560.
DR GeneID; 844294; -.
DR Gramene; AT1G79560.1; AT1G79560.1; AT1G79560.
DR KEGG; ath:AT1G79560; -.
DR Araport; AT1G79560; -.
DR TAIR; locus:2206380; AT1G79560.
DR eggNOG; KOG0731; Eukaryota.
DR HOGENOM; CLU_000688_16_0_1; -.
DR InParanoid; Q9SAJ3; -.
DR OrthoDB; 159038at2759; -.
DR PhylomeDB; Q9SAJ3; -.
DR BRENDA; 3.4.24.B20; 399.
DR PRO; PR:Q9SAJ3; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SAJ3; baseline and differential.
DR Genevisible; Q9SAJ3; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009706; C:chloroplast inner membrane; IDA:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005745; C:m-AAA complex; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
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; ISS:TAIR.
DR GO; GO:0016464; F:chloroplast protein-transporting ATPase activity; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IBA:GO_Central.
DR GO; GO:0034982; P:mitochondrial protein processing; IBA:GO_Central.
DR GO; GO:0045037; P:protein import into chloroplast stroma; IMP:TAIR.
DR GO; GO:0065003; P:protein-containing complex assembly; 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 2: Evidence at transcript level;
KW ATP-binding; Chloroplast; Hydrolase; Membrane; Metal-binding;
KW Metalloprotease; Nucleotide-binding; Plastid; Protease; Reference proteome;
KW Thylakoid; Transit peptide; Transmembrane; Transmembrane helix; Zinc.
FT TRANSIT 1..49
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT TRANSIT 50..?
FT /note="Thylakoid"
FT /evidence="ECO:0000255"
FT CHAIN ?..1008
FT /note="ATP-dependent zinc metalloprotease FTSH 12,
FT chloroplastic"
FT /id="PRO_0000341337"
FT TRANSMEM 154..174
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 427..447
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 770
FT /evidence="ECO:0000250"
FT BINDING 533..540
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 769
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 773
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 849
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1008 AA; 115105 MW; BCCE6457FD590F16 CRC64;
MEIAISYKPN PLISSSTQLL KRSKSFGLVR FPAKYGLGAT RKKQLFRVYA SESSSGSSSN
SDGGFSWVRL AQSIRLGAER IGEKIGESVK TEIGFDSEEA SGRVNEYVAR VKDSVHKGHH
ELTRFKNETV PSFIDWNKWE HWKDIRNWDG KRVAALFIYA FALLLSCQRV YVAIQAPRVE
RERRELTESF MEALIPEPSP GNIEKFKRNM WRKATPKGLK LKRFIEAPDG TLVHDSSYVG
ENAWDDDLET TEGSLKKIIG RNARIQTEAK KKLSQDLGVS GEIGDSVGNW RERLATWKEM
LEREKLSEQL NSSAAKYVVE FDMKEVEKSL REDVIGRTSE TEGTRALWIS KRWWRYRPKL
PYTYFLQKLD SSEVAAVVFT EDLKRLYVTM KEGFPLEYIV DIPLDPYLFE TICNAGVEVD
LLQKRQIHYF MKVFIALLPG ILILWFIRES AMLLLITSKR FLYKKYNQLF DMAYAENFIL
PVGDVSETKS MYKEVVLGGD VWDLLDELMI YMGNPMQYYE KDVAFVRGVL LSGPPGTGKT
LFARTLAKES GLPFVFASGA EFTDSEKSGA AKINEMFSIA RRNAPAFVFV DEIDAIAGRH
ARKDPRRRAT FEALIAQLDG EKEKTGIDRF SLRQAVIFIC ATNRPDELDL EFVRSGRIDR
RLYIGLPDAK QRVQIFGVHS AGKNLAEDID FGKLVFRTVG FSGADIRNLV NEAAIMSVRK
GRSYIYQQDI VDVLDKQLLE GMGVLLTEEE QQKCEQSVSY EKKRLLAVHE AGHIVLAHLF
PRFDWHAFSQ LLPGGKETAV SVFYPREDMV DQGYTTFGYM KMQMVVAHGG RCAERVVFGD
NVTDGGKDDL EKITKIAREM VISPQSARLG LTQLVKKIGM VDLPDNPDGE LIKYRWDHPH
VMPAEMSVEV SELFTRELTR YIEETEELAM NALRANRHIL DLITRELLEK SRITGLEVEE
KMKDLSPLMF EDFVKPFQIN PDDEELLPHK DRVSYQPVDL RAAPLHRS
