FTSH8_ORYSJ
ID FTSH8_ORYSJ Reviewed; 822 AA.
AC Q0DHL4; A0A0P0WNE6; A3B4S3; Q65XF9;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=ATP-dependent zinc metalloprotease FTSH 8, mitochondrial;
DE Short=OsFTSH8;
DE EC=3.4.24.-;
DE Flags: Precursor;
GN Name=FTSH8; OrderedLocusNames=Os05g0458400, LOC_Os05g38400;
GN ORFNames=OJ1362_D02.8, OsJ_018045;
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=16261349; DOI=10.1007/s00438-005-0039-y;
RA Cheng C.-H., Chung M.C., Liu S.-M., Chen S.-K., Kao F.Y., Lin S.-J.,
RA Hsiao S.-H., Tseng I.C., Hsing Y.-I.C., Wu H.-P., Chen C.-S., Shaw J.-F.,
RA Wu J., Matsumoto T., Sasaki T., Chen H.-C., Chow T.-Y.;
RT "A fine physical map of the rice chromosome 5.";
RL Mol. Genet. Genomics 274:337-345(2005).
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 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 {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=AAU44017.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC105770; AAU44017.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP008211; BAF17659.1; -; Genomic_DNA.
DR EMBL; AP014961; BAS94386.1; -; Genomic_DNA.
DR EMBL; CM000142; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_015639995.1; XM_015784509.1.
DR AlphaFoldDB; Q0DHL4; -.
DR SMR; Q0DHL4; -.
DR STRING; 4530.OS05T0458400-01; -.
DR MEROPS; M41.023; -.
DR PaxDb; Q0DHL4; -.
DR PRIDE; Q0DHL4; -.
DR EnsemblPlants; Os05t0458400-01; Os05t0458400-01; Os05g0458400.
DR GeneID; 4339002; -.
DR Gramene; Os05t0458400-01; Os05t0458400-01; Os05g0458400.
DR KEGG; osa:4339002; -.
DR eggNOG; KOG0731; Eukaryota.
DR HOGENOM; CLU_000688_23_2_1; -.
DR InParanoid; Q0DHL4; -.
DR OMA; DEAYKQC; -.
DR OrthoDB; 217929at2759; -.
DR Proteomes; UP000000763; Chromosome 5.
DR Proteomes; UP000007752; Chromosome 5.
DR Proteomes; UP000059680; Chromosome 5.
DR Genevisible; Q0DHL4; 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 3: Inferred from homology;
KW ATP-binding; Hydrolase; Metal-binding; Metalloprotease; Mitochondrion;
KW Nucleotide-binding; Protease; Reference proteome; Transit peptide; Zinc.
FT TRANSIT 1..93
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 94..822
FT /note="ATP-dependent zinc metalloprotease FTSH 8,
FT mitochondrial"
FT /id="PRO_0000341344"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 103..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 202..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 781..822
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..127
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 789..805
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 601
FT /evidence="ECO:0000250"
FT BINDING 375..382
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 600
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 604
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 676
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT CONFLICT 373
FT /note="L -> P (in Ref. 5; CM000142)"
FT /evidence="ECO:0000305"
FT CONFLICT 394
FT /note="V -> L (in Ref. 5; CM000142)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 822 AA; 90074 MW; 7F115F14E7804ACD CRC64;
MSLASLARAL SRRSAPSSSR ARQGFSLGGL GGTTRSPPPP SSPLPSLHGG EGGGLGLGFV
RGYLTAALGR PAAVKAGTDW RSILANPQFR RLFSDGSKKN YENYYPKGKK EAPKGDGSNK
SDSKQDSSTD DQWNFQETAS KQLQNFLAPL LFLGLMLSSL SSSSSDQKEI SFQEFKNKLL
EPGLVDRIVV SNKSVAKVYV RSSPQSNSQG QNTDAIITTN DVPSKHTPSR YKYYFNIGSV
DSFEEKLEEA QEALGVDPHD FVPVTYVAEV NWFQEVMRFA PTVFLVGLIY LMSKRMQSGF
NIGGGPGKGG RGIFNIGKAQ VTKMDKNSKN KVFFKDVAGC DEAKQEIMEF VHFLKNPKKY
EELGAKIPKG ALLVGPPGTG KTLLAKATAG ESGVPFLSIS GSDFMEMFVG VGPSRVRNLF
QEARQCAPSI IFIDEIDAIG RARGRGGFSG SNDERESTLN QLLVEMDGFG TTSGVVVLAG
TNRPDILDKA LLRPGRFDRQ ITIDKPDIKG RDQIFRIYLK KLKLDNEPSF YSQRLAALTP
GFAGADIANV CNEAALIAAR SEETQITMQH FESAIDRIIG GLEKKNKVIS KLERRTVAYH
ESGHAVAGWF LEHAEPLLKV TIVPRGTAAL GFAQYVPNEN LLMTKEQLFD MTCMTLGGRA
AEEVLIGRIS TGAQNDLEKV TKMTYAQVAV YGFSEKVGLL SFPQRDDGFE MTKPYSNQTA
SIIDDEVREW VGKAYKKTVE LITEHKEQVA KIAEMLLEKE VLHQDDLVRV LGERPFKASE
PTNYDLFKQG FQDEEDSKNQ EAAKTPQPDD DGTPSLGEVV PT
