FTSH3_ORYSJ
ID FTSH3_ORYSJ Reviewed; 802 AA.
AC Q8S2A7; B7EQ63;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=ATP-dependent zinc metalloprotease FTSH 3, mitochondrial;
DE Short=OsFTSH3;
DE EC=3.4.24.-;
DE Flags: Precursor;
GN Name=FTSH3; OrderedLocusNames=Os01g0842600, LOC_Os01g62500;
GN ORFNames=OsJ_003942, P0406G08.15;
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=12447438; DOI=10.1038/nature01184;
RA Sasaki T., Matsumoto T., Yamamoto K., Sakata K., Baba T., Katayose Y.,
RA Wu J., Niimura Y., Cheng Z., Nagamura Y., Antonio B.A., Kanamori H.,
RA Hosokawa S., Masukawa M., Arikawa K., Chiden Y., Hayashi M., Okamoto M.,
RA Ando T., Aoki H., Arita K., Hamada M., Harada C., Hijishita S., Honda M.,
RA Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., Ito S., Ito T.,
RA Ito Y., Ito Y., Iwabuchi A., Kamiya K., Karasawa W., Katagiri S.,
RA Kikuta A., Kobayashi N., Kono I., Machita K., Maehara T., Mizuno H.,
RA Mizubayashi T., Mukai Y., Nagasaki H., Nakashima M., Nakama Y.,
RA Nakamichi Y., Nakamura M., Namiki N., Negishi M., Ohta I., Ono N., Saji S.,
RA Sakai K., Shibata M., Shimokawa T., Shomura A., Song J., Takazaki Y.,
RA Terasawa K., Tsuji K., Waki K., Yamagata H., Yamane H., Yoshiki S.,
RA Yoshihara R., Yukawa K., Zhong H., Iwama H., Endo T., Ito H., Hahn J.H.,
RA Kim H.-I., Eun M.-Y., Yano M., Jiang J., Gojobori T.;
RT "The genome sequence and structure of rice chromosome 1.";
RL Nature 420:312-316(2002).
RN [2]
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 [3]
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 [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [7]
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: Mitochondrion inner membrane {ECO:0000250};
CC Single-pass membrane protein {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}.
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DR EMBL; AP003240; BAB86453.1; -; Genomic_DNA.
DR EMBL; AP008207; BAF06688.1; -; Genomic_DNA.
DR EMBL; AP014957; BAS75170.1; -; Genomic_DNA.
DR EMBL; CM000138; EAZ14117.1; -; Genomic_DNA.
DR EMBL; AK100245; BAG94510.1; -; mRNA.
DR RefSeq; XP_015626112.1; XM_015770626.1.
DR AlphaFoldDB; Q8S2A7; -.
DR SMR; Q8S2A7; -.
DR STRING; 4530.OS01T0842600-01; -.
DR MEROPS; M41.022; -.
DR PaxDb; Q8S2A7; -.
DR PRIDE; Q8S2A7; -.
DR EnsemblPlants; Os01t0842600-01; Os01t0842600-01; Os01g0842600.
DR GeneID; 4327502; -.
DR Gramene; Os01t0842600-01; Os01t0842600-01; Os01g0842600.
DR KEGG; osa:4327502; -.
DR eggNOG; KOG0731; Eukaryota.
DR HOGENOM; CLU_000688_23_2_1; -.
DR InParanoid; Q8S2A7; -.
DR OMA; VHHYLSR; -.
DR OrthoDB; 217929at2759; -.
DR Proteomes; UP000000763; Chromosome 1.
DR Proteomes; UP000007752; Chromosome 1.
DR Proteomes; UP000059680; Chromosome 1.
DR Genevisible; Q8S2A7; OS.
DR GO; GO:0005745; C:m-AAA complex; IBA:GO_Central.
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; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0034982; P:mitochondrial protein processing; IBA:GO_Central.
DR GO; GO:0065003; P:protein-containing complex assembly; 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 2: Evidence at transcript level;
KW ATP-binding; Hydrolase; Membrane; Metal-binding; Metalloprotease;
KW Mitochondrion; Mitochondrion inner membrane; Nucleotide-binding; Protease;
KW Reference proteome; Transit peptide; Transmembrane; Transmembrane helix;
KW Zinc.
FT TRANSIT 1..21
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 22..802
FT /note="ATP-dependent zinc metalloprotease FTSH 3,
FT mitochondrial"
FT /id="PRO_0000341339"
FT TRANSMEM 133..153
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 85..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 773..802
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..114
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 586
FT /evidence="ECO:0000250"
FT BINDING 360..367
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 585
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 589
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 661
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 802 AA; 88144 MW; 47B9FAD8BA412B8F CRC64;
MSLSSLSRAL ARSARSSRQR QGSLLGGHGG LRASSPPLPC GELGFLRSYV TSVIGNRAAV
ASGAGKGGDW RFLLASRQFR RLFSDKSKKN HGKHSEEENK GKGDESDKSD SKKQSSSGDQ
WNFEESIKQF KDMIAPLFLF GLLLLSASAS SSEQEISFQE FKNKLLEPGL VDHIVVSNKS
IAKVYVRSSP SIDRIQDSDI HITTSHLPGI ESPSSYKYYF NIGSVDSFEE KLQEAQKALE
IDPHYYVPIT YTTEAKWFEE VMKYVPTVLI IGLIYLLGKR IQNGFTVGGG PGKGGRSIFS
IGKVQVTKLD KNSKNKVFFK DVAGCDEAKQ EIMEFVHFLK NPKKYEELGA KIPKGALLVG
PPGTGKTLLA KATAGESGVP FLSISGSDFM EMFVGVGPSR VRNLFQEARQ CSPSIVFIDE
IDAIGRARGR GGFSGGHDER ESTLNQLLVE MDGFGTTSGV VVLAGTNRPD ILDKALLRPG
RFDRQISIDK PDIKGRDQIF RIYLKKLKLD KEPSFYSQRL AALTPGFAGA DIANVCNEAA
LIAARSEGTL ITMQHFESAI DRVIGGLEKK NKVISKLERR TVAYHESGHA VAGWFLEHAE
PLLKVTIVPR GTAALGFAQY VPNDNLLMTK EQLFDMTCMT LGGRAAEEVL IGKISTGAQN
DLEKVTKMTY AQVAVYGFSE KVGLLSFPQR EDGFEMSKPY SSQTASIIDT EVREWVAKAY
EKTVELIKQH KDQVAQIAEL LLEKEVLHQD DLVQVLGERP FKTLEPTNYD RFKQGFQDED
SNRNAELSNA DGASSLGEAV AS
