FTSH_HETA2
ID FTSH_HETA2 Reviewed; 663 AA.
AC B2XTF7;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 48.
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};
GN OrderedLocusNames=Heak293_Cp148;
OS Heterosigma akashiwo (strain NIES-293 / 8280G21-1).
OG Plastid; Chloroplast.
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; Raphidophyceae; Chattonellales;
OC Chattonellaceae; Heterosigma.
OX NCBI_TaxID=536047;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=18462506; DOI=10.1186/1471-2164-9-211;
RA Cattolico R.A., Jacobs M.A., Zhou Y., Chang J., Duplessis M., Lybrand T.,
RA McKay J., Ong H.C., Sims E., Rocap G.;
RT "Chloroplast genome sequencing analysis of Heterosigma akashiwo CCMP452
RT (West Atlantic) and NIES293 (West Pacific) strains.";
RL BMC Genomics 9:211-211(2008).
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; EU168190; ABV66055.1; -; Genomic_DNA.
DR RefSeq; YP_001936449.1; NC_010772.1.
DR AlphaFoldDB; B2XTF7; -.
DR SMR; B2XTF7; -.
DR MEROPS; M41.017; -.
DR GeneID; 6335642; -.
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..663
FT /note="ATP-dependent zinc metalloprotease FtsH"
FT /id="PRO_0000400420"
FT TOPO_DOM 1..12
FT /note="Stromal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 34..135
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 136..156
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 157..663
FT /note="Stromal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT REGION 165..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 466
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 244..251
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 465
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 469
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 543
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
SQ SEQUENCE 663 AA; 71692 MW; 7C6045C6E66822CC CRC64;
MNKKETNTSW WRIILISLGI SIICILAAFL AMKDGFFVLE NNTKNNNPDS PENKASSKMA
YARLLNYIEK GWIKTIDFYE NGQIAIVEAS SSELSDRPQR LRVEIPAGST SLIGKLKEAN
VDINAHPPKL DIFKTISDTL GSLIVPGLVV AVFYLFLERA NNNNNNNSNG SPFGPGGGPN
QNMRGLGEIK KEIQKEPDTG ITFKDIAGIE EVKEEFEEIV TFLKDPSRFT AVGATIPKGV
LLVGPPGTGK TLLAKAIAGE AKVPFINISG SEFVEMFVGV GAARVRNLFE KAKQDTPCII
FIDEIDAVGR QRGAGVGGGN DEREQTLNQL LTEMDGFEKN KGIVVIAATN RADILDNALL
RPGRFDRQVT VNPPDRAGRV AILAVHARNK KLSPAISLET IAQRTTGFGG AELANLLNEA
AIISAREEKA EIGSKEISLA IERVIAGLEG PSIADNKNKR LVAYHEAGHA MVGTLLRNHD
NVQNVTLVPR GQARGLTWFM PNEDPSLVTR GQIVARIVGA LGGRAAEQSV FGSTEITTGA
SGDLAQVTDL AKQMILRFGM SGIGPVSLSK PGGSFLFVGR GVRPSNEYSE ALAIKIDEQI
RTITELCYNE AVEIMDLNRI SLDLAVTGLI QDEVLTGVSF EKVVADFSKL PTNKIYESKF
PKK
