FTSH_NEOYE
ID FTSH_NEOYE Reviewed; 628 AA.
AC Q1XDF9;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 68.
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 Neopyropia yezoensis (Susabi-nori) (Pyropia yezoensis).
OG Plastid; Chloroplast.
OC Eukaryota; Rhodophyta; Bangiophyceae; Bangiales; Bangiaceae; Neopyropia.
OX NCBI_TaxID=2788;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=U-51;
RA Kunimoto M., Morishima K., Yoshikawa M., Fukuda S., Kobayashi T.,
RA Kobayashi M., Okazaki T., Ohara I., Nakayama I.;
RT "Whole genome sequence of Porphyra yezoensis chloroplast.";
RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
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; AP006715; BAE92452.1; -; Genomic_DNA.
DR RefSeq; YP_537009.1; NC_007932.1.
DR AlphaFoldDB; Q1XDF9; -.
DR SMR; Q1XDF9; -.
DR MEROPS; M41.017; -.
DR PRIDE; Q1XDF9; -.
DR GeneID; 3978983; -.
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_0000277305"
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; 68445 MW; B6D59C56D333A5B8 CRC64;
MKLSWKTLLL WSLPIFVIGF FFWQGFLGPT TTDVGSNIAS SRMTYGRFLE YLDMGWVKRV
DLYENNHTAI VEAVGPELGN RVQRIRVELP ASAPELITKL RKANVDLDAH PPKSTSAVWG
LLGNLLFPLL LVGGLAFLFR RSNNASGGPG QAMSFGKSKA LFQMEAKTGV VFNDVAGVEE
AKEEFQEVVT FLKQPESFTA VGAKIPKGVL LVGPPGTGKT LLAKAIAGEA SVPFFSISGS
EFVEMFVGVG ASRVRDLFKK AKDNAPCIVF IDEIDAVGRQ RGTGVGGGND EREQTLNQLL
TEMDGFEGNT GVIVIAATNR ADILDSALLR PGRFDRQVSV DVPDFKGRLA ILEVHAKNKK
MEPKVSLETI ARRTPGFSGA DLANLLNEAA ILTARRRKNA MTMSEIDTSI DRVVAGMEGT
PLIDSKSKRL IAYHEVGHAI IGSLLEHHDP VQKVTLIPRG QARGLTWFTP SDDQSLISRS
QILARIVGAL GGRAAEEIIF GDAEVTTGAS NDLQQVTSMA RQMVTRFGMS KIGPLSLESQ
GGDPFLGRGM GGGSEYSDEV ATNIDKQVRE IVSECYAQAK HIIIDNRVVI DRLVDLLIEK
ETIEGNEFRD IVKEYTAIPE KNYYISQF
