FTSH_CYAM1
ID FTSH_CYAM1 Reviewed; 603 AA.
AC Q9TJ83;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 114.
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};
DE AltName: Full=FtsHCP;
GN Name=ftsH {ECO:0000255|HAMAP-Rule:MF_01458};
OS Cyanidioschyzon merolae (strain NIES-3377 / 10D) (Unicellular red alga).
OG Plastid; Chloroplast.
OC Eukaryota; Rhodophyta; Bangiophyceae; Cyanidiales; Cyanidiaceae;
OC Cyanidioschyzon.
OX NCBI_TaxID=280699;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10598100; DOI=10.1023/a:1006369104530;
RA Itoh R., Takano H., Ohta N., Miyagishima S.-Y., Kuroiwa H., Kuroiwa T.;
RT "Two ftsH-family genes encoded in the nuclear and chloroplast genomes of
RT the primitive red alga Cyanidioschyzon merolae.";
RL Plant Mol. Biol. 41:321-337(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-3377 / 10D;
RX PubMed=12755171; DOI=10.1093/dnares/10.2.67;
RA Ohta N., Matsuzaki M., Misumi O., Miyagishima S.-Y., Nozaki H., Tanaka K.,
RA Shin-i T., Kohara Y., Kuroiwa T.;
RT "Complete sequence and analysis of the plastid genome of the unicellular
RT red alga Cyanidioschyzon merolae.";
RL DNA Res. 10:67-77(2003).
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; AB024399; BAA88165.1; -; Genomic_DNA.
DR EMBL; AB002583; BAC76202.1; -; Genomic_DNA.
DR RefSeq; NP_849040.1; NC_004799.1.
DR AlphaFoldDB; Q9TJ83; -.
DR SMR; Q9TJ83; -.
DR STRING; 45157.CMV129CT; -.
DR MEROPS; M41.017; -.
DR EnsemblPlants; CMV129CT; CMV129CT; CMV129C.
DR GeneID; 844888; -.
DR Gramene; CMV129CT; CMV129CT; CMV129C.
DR KEGG; cme:CymeCp108; -.
DR eggNOG; KOG0731; Eukaryota.
DR HOGENOM; CLU_000688_16_2_1; -.
DR Proteomes; UP000007014; Chloroplast.
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; Reference proteome;
KW Thylakoid; Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..603
FT /note="ATP-dependent zinc metalloprotease FtsH"
FT /id="PRO_0000084658"
FT TOPO_DOM 1..2
FT /note="Stromal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 24..101
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 123..603
FT /note="Stromal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT ACT_SITE 416
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 194..201
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 415
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 419
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 493
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
SQ SEQUENCE 603 AA; 66300 MW; BE9C375D3033CA71 CRC64;
MKNLWIWSLP LIVLAFIGWQ ELANQMPVAT SRMTYGRLLE YMQMGWVKRI DVYDRTALIE
ASSPETGWQW IRVDLPANSS DWLEQAKTLH IDVDVHAVSN WINVASNWII PLIIIGVVIW
LLSRSASSNT TGALNFGKSK ARFQMVAKTG IMFDDVAGIE EAKEELAEVV AFLKNPSKFL
AVGASIPKGV LLVGPPGTGK TLLAKAIAGE ASVPFFSISG SEFVEMFVGV GASRVRDLFK
KAKQNAPCLV FIDEIDAVGR QRGAGIGGGN DEREQTLNQL LTEMDGFEGN TGVIVIAATN
RVDVLDAALL RPGRFDRQIM VSMPDVKSRI AILKVHANQK KLHPQVSLEA VARRTAGFAG
ADLANLLNEA AILAVRRGLK QITWKEIDDA IDRVIAGMEG TPIMDGKIKR LIAYHETGHA
LTATLLPNHP PVQKVTLIPR RQAKGLTWFM QDNERDLLSK SQLMSMIMVA LGGRAAEEAV
FGNAEVTTGA SNDLQQVTNL ARQMVTRFGM SSLGPLCLET GNEEIFLGRD MRLMPEVSEE
VIAQIDAQVR GMIEACYEKV LELMQANRVV MDRIVEELME KETLDGKEFR QLVSQAARLT
AVN
