FTSH_CYACA
ID FTSH_CYACA Reviewed; 614 AA.
AC O19922;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 101.
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};
OS Cyanidium caldarium (Red alga).
OG Plastid; Chloroplast.
OC Eukaryota; Rhodophyta; Bangiophyceae; Cyanidiales; Cyanidiaceae; Cyanidium.
OX NCBI_TaxID=2771;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RK-1;
RX PubMed=11040290; DOI=10.1007/s002390010101;
RA Gloeckner G., Rosenthal A., Valentin K.-U.;
RT "The structure and gene repertoire of an ancient red algal plastid
RT genome.";
RL J. Mol. Evol. 51:382-390(2000).
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; AF022186; AAB82667.1; -; Genomic_DNA.
DR PIR; T11990; T11990.
DR RefSeq; NP_045094.1; NC_001840.1.
DR AlphaFoldDB; O19922; -.
DR SMR; O19922; -.
DR MEROPS; M41.017; -.
DR GeneID; 800206; -.
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..614
FT /note="ATP-dependent zinc metalloprotease FtsH"
FT /id="PRO_0000084657"
FT TOPO_DOM 1..7
FT /note="Stromal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 29..116
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 117..137
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 138..614
FT /note="Stromal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT ACT_SITE 433
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 211..218
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 432
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 436
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 510
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
SQ SEQUENCE 614 AA; 68245 MW; 5AEE98454AA9ECF6 CRC64;
MKKQWKKIVL FVLPVIITLI TLSSFLFYNQ DVVHNWSSSR MTYGRFLEYI DMNWVKKVDL
YDNARTAIVD IINPDIKGEE QLVRVELPTF SSELVSKLKN KLIDFDAHPS SSNVNLVSWL
SNLLLPLILI ITLFFFFRRG NKSSSGPGQA FNFGKAKARF HMEAKTGIVF EDVAGIEEAK
EELQEIVAFL KDSRKFTNVG ATIPKGVLLV GPPGTGKTLL AKAIAGEASA PFFSISGSEF
VEMFVGVGAS RVRDLFKKAK EKAPCIVFID EIDAVGRQRG VGIGGGNDER EQTLNQLLTE
MDGFSGDTGV IVVAATNRID VLDSALLRPG RFDRQIMVSL PNINGRLAIL KVHSKKKKIH
KDVLLEVIAR RTPGFSGADL ANLLNEAAIL TVRRGKVEIT MKEIEDSIDK IIAGLEGSPL
ADSRIKRLIA YHEAGHAVAA TFLPHHDPVQ KVTLIPRRQA KGLTWFLPND DQFLVSKSQI
LSKIIAALAG RAMEEIVFGL PEVTIGAAND IKQVTFMARQ MVTKFGMSKV GPICLENSSS
EVFIGRDLMG RHELSEEMVA KVDLEVRSIL KDCYIQARTI LSQNRKLIDR VVNELVEKET
IEAKEFMRIV EERV
