FTSH_ECTSI
ID FTSH_ECTSI Reviewed; 661 AA.
AC D1J722;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 19-JAN-2010, sequence version 1.
DT 03-AUG-2022, entry version 44.
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}; ORFNames=Es_cpDNA_67;
OS Ectocarpus siliculosus (Brown alga) (Conferva siliculosa).
OG Plastid; Chloroplast.
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; PX clade; Phaeophyceae;
OC Ectocarpales; Ectocarpaceae; Ectocarpus.
OX NCBI_TaxID=2880;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ec32 / CCAP1310/4;
RX PubMed=19835607; DOI=10.1186/1471-2148-9-253;
RA Le Corguille G., Pearson G., Valente M., Viegas C., Gschloessl B.,
RA Corre E., Bailly X., Peters A.F., Jubin C., Vacherie B., Cock J.M.,
RA Leblanc C.;
RT "Plastid genomes of two brown algae, Ectocarpus siliculosus and Fucus
RT vesiculosus: further insights on the evolution of red-algal derived
RT plastids.";
RL BMC Evol. Biol. 9:253-253(2009).
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; FP102343; CAT18723.1; -; Genomic_DNA.
DR EMBL; FP102296; CAV31206.1; -; Genomic_DNA.
DR RefSeq; YP_003289175.1; NC_013498.1.
DR AlphaFoldDB; D1J722; -.
DR SMR; D1J722; -.
DR STRING; 2880.D1J722; -.
DR MEROPS; M41.017; -.
DR GeneID; 8594825; -.
DR eggNOG; KOG0731; Eukaryota.
DR InParanoid; D1J722; -.
DR Proteomes; UP000002630; 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..661
FT /note="ATP-dependent zinc metalloprotease FtsH"
FT /id="PRO_0000400419"
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..140
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 141..161
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 162..661
FT /note="Stromal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT ACT_SITE 457
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 235..242
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 456
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 460
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 533
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
SQ SEQUENCE 661 AA; 73227 MW; 379CFA651562E0FC CRC64;
MKNQTTKNII LVFVGLALLS GFVYLKWDNF TDVGTNLINL KNSHPTQMVS YDTFLHYLEN
GAIKKVDLYE NAELAVFDAF ESLDQNLLKP VPLLSSDTLF GILNSDEFRP IGVKIPVRNS
SLILTLRDYK IDFTAYPIVN FDSIWPILSV LLIPVLLIVV YRLFFSEGSN YDFFGNLRKA
RAKIQLDADT GVLFSDVAGI DEAKQEFEEF VSFLKMPQLF TAVGANPPKG VIIVGPPGTG
KTLLAKAIAG EAGVPFISIS GSEFVEMFVG IGASRVRDLF ETAERNSPCI LFIDEIDAIG
RQRGTGVGGT NDEREQTLNQ ILTEMDGFKP TSGIIVIAAT NRADVLDSAL LRPGRFDRQI
TVYLPNIYGR IEILKVHSRN KNIDSKTSLK FIAQRTAGFS GADLANILNE AAILTARANL
ETITIKQIYT AIERIIAGLE GVLLNDSRNK RLVAYHEVGH ALTGTLLKNH DDVQKVTLIP
RGRAQGLTWF TPDEQPLMTR GQLSSRLIGT LGGRAAEKVI FGKMEITSGA SNDFFKVNSL
ARQMVTRFGM SSLTPMAMEL PKPTIFFGRS VQTRPDCFLD IADKIDLQII EMVEDGFEKA
CITLERNRLL LDQLATLLTQ IETIDGKEFE QFVSTYTGLP KKPQLKIVKA KENKNKVKAP
V
