FTSH_VAULI
ID FTSH_VAULI Reviewed; 644 AA.
AC B7T1V0;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 46.
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 Vaucheria litorea (Yellow-green alga).
OG Plastid; Chloroplast.
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; PX clade; Xanthophyceae;
OC Vaucheriales; Vaucheriaceae; Vaucheria.
OX NCBI_TaxID=109269;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP2940;
RX PubMed=19004808; DOI=10.1073/pnas.0804968105;
RA Rumpho M.E., Worful J.M., Lee J., Kannan K., Tyler M.S., Bhattacharya D.,
RA Moustafa A., Manhart J.R.;
RT "Horizontal gene transfer of the algal nuclear gene psbO to the
RT photosynthetic sea slug Elysia chlorotica.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:17867-17871(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; EU912438; ACF70915.1; -; Genomic_DNA.
DR RefSeq; YP_002327499.1; NC_011600.1.
DR AlphaFoldDB; B7T1V0; -.
DR SMR; B7T1V0; -.
DR MEROPS; M41.017; -.
DR GeneID; 7056008; -.
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..644
FT /note="ATP-dependent zinc metalloprotease FtsH"
FT /id="PRO_0000400421"
FT TOPO_DOM 1..5
FT /note="Stromal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 27..119
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 120..140
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 141..644
FT /note="Stromal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT ACT_SITE 437
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 215..222
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
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 440
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 514
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
SQ SEQUENCE 644 AA; 71111 MW; F9E189EDC2FA002A CRC64;
MKSWSVNKII MLISLFLLEV IDSQIISNNI INNFNTKQNS NNIKMTYGRF LEYLDMGWIK
KVDFYDNGRI AIIEASSPEL GDRLQKIRVE IPVGDSPLIV KLRTAKVDFT AHSTINSKGI
FTQLSNIFIP LIIIIGLIFL FRRSTNFMSG PGQLMSFRKA RAKVQTEINT DVVFDDVAGI
DEVKEEFEEV VTFLRKPQRF LSVGAKIPKG VILIGPPGTG KTLLAKAIAG EAGVPFISIS
GSEFVEMFVG IGASRVRDLF KTAQQNAPCI VFIDEIDAVG RQRGAGIGGG NDEREQTLNQ
ILTEMDGFKE NTGIIVIAAT NRVDVLDGAL LRPGRFDRQV SINLPDIKGR LEILKVHAKN
KKLDSNISLG LIAQRTPGFS GADLANLLNE SAILTARRNK FAITMSEVNT AIDRLLAGLE
GTSLTDTKNK RLIAYHEIGH AVIGTLLKYH DEVQKVTLIP RGQARGLTWF IPNDEQALIS
RGQLVARIIG TLGGRAAEEV VFGSSEITTG ASNDLQQITN LTRQMVTRLG MSTVGPISLD
ANVEQVFIGR GIKNNNEFSA SVANKIDDQV KIIIKHCYDQ AVNIIKQNRF LIDQLVNTLI
QEETISGNDF REQINNYTKL PKKLSTLSEK NNVNPKITES FVVF
