FTSH_TRICV
ID FTSH_TRICV Reviewed; 644 AA.
AC P49825;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=ATP-dependent zinc metalloprotease FtsH {ECO:0000255|HAMAP-Rule:MF_01458};
DE EC=3.4.24.- {ECO:0000255|HAMAP-Rule:MF_01458};
GN Name=ftsH {ECO:0000255|HAMAP-Rule:MF_01458}; Synonyms=ycf25;
OS Trieres chinensis (Marine centric diatom) (Odontella sinensis).
OG Plastid; Chloroplast.
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta; Mediophyceae;
OC Biddulphiophycidae; Eupodiscales; Parodontellaceae; Trieres.
OX NCBI_TaxID=1514140;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Kowallik K.V., Stoebe B., Schaffran I., Kroth-Pancic P., Freier U.;
RT "The chloroplast genome of a chlorophyll a+c-containing alga, Odontella
RT sinensis.";
RL Plant Mol. Biol. Rep. 13:336-342(1995).
CC -!- FUNCTION: Acts as a processive, ATP-dependent zinc metallopeptidase.
CC {ECO:0000255|HAMAP-Rule:MF_01458}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01458};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01458};
CC -!- SUBUNIT: Homohexamer. {ECO:0000255|HAMAP-Rule:MF_01458}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000255|HAMAP-Rule:MF_01458}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_01458}; Stromal side {ECO:0000255|HAMAP-
CC Rule:MF_01458}.
CC -!- SIMILARITY: In the central section; belongs to the AAA ATPase family.
CC {ECO:0000255|HAMAP-Rule:MF_01458}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the peptidase M41
CC family. {ECO:0000255|HAMAP-Rule:MF_01458}.
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DR EMBL; Z67753; CAA91674.1; -; Genomic_DNA.
DR PIR; S78301; S78301.
DR AlphaFoldDB; P49825; -.
DR SMR; P49825; -.
DR MEROPS; M41.017; -.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030163; P:protein catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.20.58.760; -; 1.
DR Gene3D; 3.40.50.300; -; 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 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.
DR TIGRFAMs; TIGR01241; FtsH_fam; 1.
DR PROSITE; PS00674; AAA; 1.
PE 3: Inferred from homology;
KW ATP-binding; Chloroplast; Hydrolase; Membrane; Metal-binding;
KW Metalloprotease; Nucleotide-binding; Plastid; Protease; Thylakoid;
KW Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..644
FT /note="ATP-dependent zinc metalloprotease FtsH"
FT /id="PRO_0000084660"
FT TOPO_DOM 1..11
FT /note="Stromal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 33..128
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 129..149
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 150..644
FT /note="Stromal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT ACT_SITE 448
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 226..233
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 447
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 451
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 525
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
SQ SEQUENCE 644 AA; 70148 MW; 6FB94B2DAD461F66 CRC64;
MNDNKNNTVR NLLIGIALLS GISLTAKKFD LIGVQGSESG KNINQVNPNV ISSKMTYGRF
LEYLEMGWVN QVDLYDNSRN AIVQASSPEL GNRPQTIRVE IPVGASQLIQ KLKEYNIDFD
AHPAEQKNIF VNILSNILLP IIFITGLVYL FQNSENFGGG SGQSPMSLGK STARFERRPD
TGVSFKDIAG IDEAKTEFEE IVSFLKEPDK YTIVGAKIPK GILLVGPPGT GKTLLAKAIA
NEADVPFFSV AGSEFVEMFI GIGAARVRDL FKKASENAPC IVFIDEIDAV GRERGAGVGG
GNDEREQTLN QLLTEMDGFK ENKGVIVVGA TNRADILDAA LLRPGRFDRQ VTVNLPDRLG
RVGILKVHAR NKPLGEDVSL VQLANRTPGF SGADLANLLN EAAILATRYK KSSITKNEVN
EAADRIIGGI AGAPMEDTKN KRLIAYHEVG HAITGSVLKS HDEVEKITLT PRGGAKGLTW
FTPEEDQSLL SRSALLARII TTLGGRAAEQ VIFGEPEVTT GASSDLQQVT NLARQMVTRF
GMSNIGPLAL EDESTGQVFL GGNMASGSEY AENIADRIDD EVRKIITYCY EKAIEIVLDN
RVVIDLIVEK LLDKETMDGD EFRELLSTYT ILPNKNIPYV SKFN
