FTSH7_ORYSJ
ID FTSH7_ORYSJ Reviewed; 822 AA.
AC Q6H6R9; A0A0P0VMH6; A3A9L5; Q6H6R8;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=ATP-dependent zinc metalloprotease FTSH 7, chloroplastic;
DE Short=OsFTSH7;
DE EC=3.4.24.-;
DE Flags: Precursor;
GN Name=FTSH7; OrderedLocusNames=Os02g0649700, LOC_Os02g43350;
GN ORFNames=OsJ_007487, P0048B08.24-1, P0048B08.24-2;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [5]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=16040665; DOI=10.1104/pp.105.061234;
RA Yu F., Park S., Rodermel S.R.;
RT "Functional redundancy of AtFtsH metalloproteases in thylakoid membrane
RT complexes.";
RL Plant Physiol. 138:1957-1966(2005).
CC -!- FUNCTION: Probable ATP-dependent zinc metallopeptidase. {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}; Stromal side
CC {ECO:0000250}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the AAA ATPase
CC family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the peptidase M41
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD25581.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP004868; BAD25580.1; -; Genomic_DNA.
DR EMBL; AP004868; BAD25581.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP008208; BAF09498.1; -; Genomic_DNA.
DR EMBL; AP014958; BAS80044.1; -; Genomic_DNA.
DR EMBL; CM000139; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_015625409.1; XM_015769923.1.
DR AlphaFoldDB; Q6H6R9; -.
DR SMR; Q6H6R9; -.
DR STRING; 4530.OS02T0649700-01; -.
DR MEROPS; M41.A04; -.
DR PaxDb; Q6H6R9; -.
DR PRIDE; Q6H6R9; -.
DR EnsemblPlants; Os02t0649700-01; Os02t0649700-01; Os02g0649700.
DR GeneID; 4330159; -.
DR Gramene; Os02t0649700-01; Os02t0649700-01; Os02g0649700.
DR KEGG; osa:4330159; -.
DR eggNOG; KOG0731; Eukaryota.
DR HOGENOM; CLU_000688_23_3_1; -.
DR InParanoid; Q6H6R9; -.
DR OMA; NSSCEHD; -.
DR OrthoDB; 217929at2759; -.
DR Proteomes; UP000000763; Chromosome 2.
DR Proteomes; UP000007752; Chromosome 2.
DR Proteomes; UP000059680; Chromosome 2.
DR ExpressionAtlas; Q6H6R9; differential.
DR Genevisible; Q6H6R9; OS.
DR GO; GO:0009534; C:chloroplast thylakoid; IBA:GO_Central.
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-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0004176; F:ATP-dependent peptidase activity; IBA:GO_Central.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
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; Reference proteome;
KW Thylakoid; Transit peptide; Transmembrane; Transmembrane helix; Zinc.
FT TRANSIT 1..70
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT TRANSIT 71..?
FT /note="Thylakoid"
FT /evidence="ECO:0000255"
FT CHAIN ?..822
FT /note="ATP-dependent zinc metalloprotease FTSH 7,
FT chloroplastic"
FT /id="PRO_0000341343"
FT TRANSMEM 154..174
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 288..308
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 67..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..81
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 612
FT /evidence="ECO:0000250"
FT BINDING 386..393
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 611
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 615
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 694
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 822 AA; 87919 MW; 28652C6D4FF39262 CRC64;
MASASAAAET LAAASLPVAS PSRSLLRPLP RRASAGGGCS ASVRISAVPP RGLGFAVVQR
RVLRRPPAAR ANVEREGDGA EASGPGEASS SSSGDGDRDG AAAAAEAGGD GASTSTTSAA
ATPPQPPSSK RGENKWRRKL IKGGGVGRWL WEPIVQGREM GFLLLQLGFA IFALRMLRPE
IALPGSEPRP QTTYVSVPYS DFLASIDKNQ VKKVEVDGVH IMFRLRPEVE ARAMEQPQVQ
RGTDSVADNA GVPRRIVFTT TRPVDIKTPY EKMVENSVEF GSPDKRSGGL LNSALVALIY
VVLIAVVLQR LPISFSQHSA GQLRNRKNSN SGGAKVSEST DIVTFADVAG VDEAKEELEE
IVEFLRNPER YIRLGARPPR GVLLVGLPGT GKTLLAKAVA GEAEVPFISC SASEFVELYV
GMGAARVRDL FARAKKESPS IIFIDEIDAV AKSRDGRYRI VSNDEREQTL NQLLTEMDGF
DTNSAVIVLG ATNRADVLDP ALRRPGRFDR VVMVEAPDRF GRESILKVHV SRKELPLGKD
VDLSDIAAMT TGFTGADLAN LVNEAALLAG RSNKEIVEKI DFICAVERSI AGIEKKHAKL
KGNEKAVVAR HEVGHAVVGT AVANLLPGQP RVEKLSILPR SGGALGFTYT PPTTEDRYLL
FVDELRGRLV TLLGGRAAEE VVLSGRVSTG ALDDIRRATD MAYKAVAEYG LNQRIGPISV
ATLSNGGLDE SGGSPWGRDQ GHLVDLVQRE VKALLQSALD VALSVVRANP TVLEGLGAYL
EENEKVEGEE LQEWLKSVVA PKELTSFIRG KQEQVLQLEA GS
