FTSH_PORPU
ID FTSH_PORPU Reviewed; 628 AA.
AC P51327;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 109.
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 Porphyra purpurea (Red seaweed) (Ulva purpurea).
OG Plastid; Chloroplast.
OC Eukaryota; Rhodophyta; Bangiophyceae; Bangiales; Bangiaceae; Porphyra.
OX NCBI_TaxID=2787;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Avonport;
RA Reith M.E., Munholland J.;
RT "Complete nucleotide sequence of the Porphyra purpurea chloroplast
RT genome.";
RL Plant Mol. Biol. Rep. 13:333-335(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; U38804; AAC08213.1; -; Genomic_DNA.
DR PIR; S73248; S73248.
DR RefSeq; NP_053937.1; NC_000925.1.
DR AlphaFoldDB; P51327; -.
DR SMR; P51327; -.
DR MEROPS; M41.017; -.
DR GeneID; 809956; -.
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; IPR011546; Pept_M41_FtsH_extracell.
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; PF06480; FtsH_ext; 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..628
FT /note="ATP-dependent zinc metalloprotease FtsH"
FT /id="PRO_0000084661"
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..118
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 119..139
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 140..628
FT /note="Stromal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT ACT_SITE 435
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 213..220
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 434
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 438
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 512
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
SQ SEQUENCE 628 AA; 68495 MW; EDBB205E4DEC6A4D CRC64;
MKLSWKTLLL WSLPIFVVGF FFWQGFLGPT TTDVGSNIAS SRMTYGRFLE YLDMGWVKRV
DLYENNHTAI VEAVGPELGN RVQRIRVELP ASAPELITKL RKANVDLDAH PPKSTSAVWG
LLGNLLFPLI LVGGLAFLFR RSNNASGGPG QAMSFGKSKA LFQMEAKTGV VFNDVAGVEE
AKEEFQEVVT FLKQPESFTA VGAKIPKGVL LVGPPGTGKT LLAKAIAGEA GVPFFSISGS
EFVEMFVGVG ASRVRDLFKK AKDNAPCIVF IDEIDAVGRQ RGTGVGGGND EREQTLNQLL
TEMDGFEGNT GVIVIAATNR ADILDSALLR PGRFDRQVSV DVPDFRGRLA ILEVHAKNKK
MESKVSLETI ARRTPGFSGA DLANLLNEAA ILTARRRKSA MTMSEIDTSI DRVVAGLEGT
PLIDSKSKRL IAYHEVGHAI IGSLLEHHDP VQKVTLIPRG QARGLTWFTP SDDQSLISRS
QILARIVGAL GGRAAEEIIF GDAEVTTGAS NDLQQVTSMA RQMVTRFGMS KIGPLSLESQ
GSDPFLGRGM GGGSEYSDEV ATNIDKQVRE IVSECYKEAK KIVKDNRVVM DRLVDLLIEK
ETIEGNEFRH IVKEYTAIPE KNYYISQF
