ID FTSH_MEDSA Reviewed; 706 AA.
AC Q9BAE0;
DT 13-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 27-MAR-2024, entry version 95.
DE RecName: Full=ATP-dependent zinc metalloprotease FTSH, chloroplastic;
DE EC=3.4.24.-;
DE Flags: Precursor;
GN Name=FTSH;
OS Medicago sativa (Alfalfa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Trifolieae; Medicago.
OX NCBI_TaxID=3879;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Ivashuta S., Imai R., Uchiyama K., Gau M., Shimamoto Y.;
RT "Full length cDNA of alfalfa chloroplast FtsH protease.";
RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Seems to act as an ATP-dependent zinc metallopeptidase.
CC {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000305};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000305}.
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}.
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DR EMBL; AF332134; AAK15322.1; -; mRNA.
DR AlphaFoldDB; Q9BAE0; -.
DR SMR; Q9BAE0; -.
DR MEROPS; M41.020; -.
DR GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
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; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd19501; RecA-like_FtsH; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 3.30.720.210; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.20.58.760; Peptidase M41; 1.
DR HAMAP; MF_01458; FtsH; 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; IPR005936; FtsH.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000642; Peptidase_M41.
DR InterPro; IPR037219; Peptidase_M41-like.
DR NCBIfam; TIGR01241; FtsH_fam; 1.
DR PANTHER; PTHR23076:SF97; ATP-DEPENDENT ZINC METALLOPROTEASE FTSH 2, CHLOROPLASTIC-RELATED; 1.
DR PANTHER; PTHR23076; METALLOPROTEASE M41 FTSH; 1.
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; FtsH protease domain-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00674; AAA; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell cycle; Cell division; Chloroplast; Hydrolase; Membrane;
KW Metal-binding; Metalloprotease; Nucleotide-binding; Plastid; Protease;
KW Transit peptide; Transmembrane; Transmembrane helix; Zinc.
FT TRANSIT 1..?
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN ?..706
FT /note="ATP-dependent zinc metalloprotease FTSH,
FT chloroplastic"
FT /id="PRO_0000000246"
FT TRANSMEM 54..74
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 196..216
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 74..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..89
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 516
FT /evidence="ECO:0000250"
FT BINDING 293..300
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 515
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 519
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 595
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 706 AA; 75680 MW; 3645111C5929A010 CRC64;
MAFSTSSLLS TNFLGARNIP TPKTTKPSIS LPLFFKTKFF NSQNDNNNNN SEPIKSAAVS
ALILSSMFTP AALAADNLPP PPPPVLEAQP NQLNPANSTS PFSQNISLTA PKPQAQSSTD
LPDGSQWRYS EFLNAVKKGK VERVRFSKDG SVLQLTAVDG RRANVIVPND PDLIDILAMN
GVDISVSEGE QGNGLFSFVG SLLLPFLAFA GLFLIFRRGQ GGPGGPGGLG GPMDFGRSKS
KFQEVPETGV TFADVAGADQ AKLELQEVVD FLKNPDKYTA LGAKIPKGCL LVGPPGTGKT
LLARAVAGEA GTPFFSCAAS EFVELFVGVG ASRVRDLFEK AKSKAPCIVF IDEIDAVGRQ
RGAGLGGGND EREQTINQLL TEMDGFSGNS GVIVLAATNR PDVLDSALLR PGRFDRQVTV
DRPDVAGRVK ILQVHSRGKA LAKDVDFDKI ARRTPGFTGV DLQNLMNEAA ILAARRDLKE
ISKDEIADAL ERIIAGPEKK NAVVSEEKKK LVAYHEAGHA LVGALMPEYD PVAKISIIPR
GQAGGLTFFA PSEERLESGL YSRSYLENQM AVALGGRVAE EVFGQDNVTT GASNDFMQVS
RVARQMVERF GFSKKIGQVA IGGGGGNPFL GQQMSSQKDY SMATADIVDK EVRELVDKAY
ERATQIINTH IDILHKLAQL LIEKETVDGE EFMSLFIDGK AELYVS
//
