FTSH8_ARATH » ATP-dependent zinc metalloprotease FTSH 8, chloroplastic

FTSH8_ARATH » ATP-dependent zinc metalloprotease FTSH 8, chloroplastic
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Topology in Thylakoid membrane
Topologythylakoid lumen
chloroplast stroma
FTSH8_ARATH » ATP-dependent zinc metalloprotease FTSH 8, chloroplastic » AtFTSH8;
Hydrophobic Thickness 29.6 ± 3.9 Å
Tilt Angle 32 ± 4°
ΔGtransfer -19.6 kcal/mol
ΔGfold -9.2 kcal/mol
Links UniProtKB, Pfam, Interpro, iHOP, STRING
Topology Out
TM Segments 161-183 (161-187)
Pathways none
PDB none
OPM none
Complexes none
Interactions none
Domains

AA: 54-153, PDBID: 2LNA, Subunit A, Seq Identity:22%, FtsH Extracellular

AA: 256-389, PDBID: 1LV7, Subunit A, Seq Identity:84%, ATPase family associated with various cellular activities (AAA)

AA: 449-658, PDBID: 1LV7, Subunit A, Seq Identity:42%, Peptidase family M41

UniProt annotation for FTSH8_ARATH » ATP-dependent zinc metalloprotease FTSH 8, chloroplastic
FUNCTION: Part of a complex that function as an ATP-dependent zinc metallopeptidase. Involved in the thylakoid formation and in the removal of damaged D1 in the photosystem II, preventing cell death under high-intensity light conditions.

SUBUNIT: Heterohexamers with FTSH1, FTSH2 and FTSH5. May also form homooligomers.

TISSUE SPECIFICITY: Expressed in cotyledons, cauline and rosette leaves, stems, sepals, flovers and siliques. Very low in roots.

INDUCTION: By heat and high light.

DOMAIN: The conserved lumenal (CL) domain (74-154) is present only in some FtsH homologs from organisms performing oxygenic photosynthesis.

UniProt features for FTSH8_ARATH » ATP-dependent zinc metalloprotease FTSH 8, chloroplastic
TRANSIT 1 37 Chloroplast (Potential).
TRANSIT 38 73 Thylakoid (Probable).
CHAIN 74 685 ATP-dependent zinc metalloprotease FTSH 8, chloroplastic.
ACT_SITE 482 482 By similarity.
Amino Acid Sequence for FTSH8_ARATH » ATP-dependent zinc metalloprotease FTSH 8, chloroplastic
MAASSACLLG NGLSVYTTKQ RFQKLGLDRT SKVTVVKASL DEKKHEGRRG FFKLLLGNAA AGVGLLASGN ANADEQGQGV SSSRMSYSRF LEYLDKGRVE KVDLYENGTI AIVEAVSPEL GNRIQRVRVQ LPGLSQELLQ KLRAKNIDFA AHNAQEDQGS PILNLIGNLA FPVILIGGLF LLSRRSSGGM GGPGGPGFPL QIGQSKAKFQ MEPNTGVTFD DVAGVDEAKQ DFMEVVEFLK KPERFTAVGA RIPKGVLLVG PPGTGKTLLA KAIAGEAGVP FFSISGSEFV EMFVGVGASR VRDLFKKAKE NAPCIVFVDE IDAVGRQRGT GIGGGNDERE QTLNQLLTEM DGFEGNTGVI VVAATNRADI LDSALLRPGR FDRQVSVDVP DVKGRTDILK VHSGNKKFES GVSLEVIAMR TPGFSGADLA NLLNEAAILA GRRGKTAISS KEIDDSIDRI VAGMEGTVMT DGKSKSLVAY HEVGHAICGT LTPGHDAVQK VTLIPRGQAR GLTWFIPSDD PTLISKQQLF ARIVGGLGGR AAEEVIFGES EVTTGAVSDL QQITGLAKQM VTTFGMSEIG PWSLMDSSEQ SDVIMRMMAR NSMSEKLAND IDTAVKTLSD KAYEIALSQI RNNREAMDKI VEILLEKETM SGDEFRAILS EFTEIPPENR VASSTSTSTP TPASV