FTSH5_ORYSJ
ID FTSH5_ORYSJ Reviewed; 715 AA.
AC Q8LQJ8; A0A0P0V4C9; Q656T6;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=ATP-dependent zinc metalloprotease FTSH 5, mitochondrial;
DE Short=OsFTSH5;
DE EC=3.4.24.-;
DE Flags: Precursor;
GN Name=FTSH5; OrderedLocusNames=Os01g0574500, LOC_Os01g39260;
GN ORFNames=B1151A10.26-1, OsJ_002241;
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 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=BAD45191.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP003413; BAB91903.1; -; Genomic_DNA.
DR EMBL; AP003413; BAD45191.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP008207; BAF05299.1; -; Genomic_DNA.
DR EMBL; AP014957; BAS72813.1; -; Genomic_DNA.
DR EMBL; CM000138; EAZ12416.1; -; Genomic_DNA.
DR RefSeq; XP_015615459.1; XM_015759973.1.
DR AlphaFoldDB; Q8LQJ8; -.
DR SMR; Q8LQJ8; -.
DR STRING; 4530.OS01T0574500-01; -.
DR MEROPS; M41.018; -.
DR PaxDb; Q8LQJ8; -.
DR PRIDE; Q8LQJ8; -.
DR EnsemblPlants; Os01t0574500-01; Os01t0574500-01; Os01g0574500.
DR GeneID; 4326311; -.
DR Gramene; Os01t0574500-01; Os01t0574500-01; Os01g0574500.
DR KEGG; osa:4326311; -.
DR eggNOG; KOG0734; Eukaryota.
DR HOGENOM; CLU_000688_9_3_1; -.
DR InParanoid; Q8LQJ8; -.
DR OMA; WHTSYIS; -.
DR OrthoDB; 217929at2759; -.
DR Proteomes; UP000000763; Chromosome 1.
DR Proteomes; UP000007752; Chromosome 1.
DR Proteomes; UP000059680; Chromosome 1.
DR ExpressionAtlas; Q8LQJ8; baseline and differential.
DR Genevisible; Q8LQJ8; OS.
DR GO; GO:0009534; C:chloroplast thylakoid; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; 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; 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; Hydrolase; Metal-binding; Metalloprotease; Mitochondrion;
KW Nucleotide-binding; Protease; Reference proteome; Transit peptide; Zinc.
FT TRANSIT 1..18
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 19..715
FT /note="ATP-dependent zinc metalloprotease FTSH 5,
FT mitochondrial"
FT /id="PRO_0000341341"
FT REGION 665..685
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 490
FT /evidence="ECO:0000250"
FT BINDING 270..277
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 489
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 493
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 567
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 715 AA; 77434 MW; B2A6FCBD71FC5A9C CRC64;
MAWRRVLSQV ARNRSAYAIC NEIIYANPSR ILRGDTIAGG TLRNLHERYQ SSYVGSFARR
MRQMDSPSEA SLLKEIYRSD PERVIQIFES QPSLHSNPSA LAEYVKALVR VDRLEDSTLL
KTLQRGIAAS AREEENLGSV SENLGSVSAF RSAGQVTKDG ILGTANAPIH MVTAETGQFK
EQLWRTFRSI ALTFLLISGI GALIEDRGIS KGLGLNEEVQ PSMESNTKFS DVKGVDEAKA
ELEEIVHYLR DPKRFTRLGG KLPKGVLLVG PPGTGKTMLA RAIAGEAGVP FFSCSGSEFE
EMFVGVGARR VRDLFAAAKK RSPCIIFMDE IDAIGGSRNP KDQQYMKMTL NQLLVELDGF
KQNEGIIVIA ATNFPESLDK ALVRPGRFDR HIVVPNPDVE GRRQILESHM SKVLKSDDVD
LMIIARGTPG FSGADLANLV NVAALKAAMD GAKAVTMNDL EYAKDRIMMG SERKSAVISD
ESRKLTAYHE GGHALVAIHT EGAHPVHKAT IVPRGMALGM VAQLPDKDET SVSRKQMLAR
LDVCMGGRVA EELIFGDSEV TSGASSDFQQ ATAVARAMVT KYGMSKQLGF VSYNYEDDGK
SMSTETRLLI EKEVKCFVEN AYNNAKNILI KHNKELHALA NALLEHETLT GAQIKNILAQ
VNNKQQQEHA IEAPQKTPAV PSSPAASAAA AAAAAAAAAQ QAAAKAKGEI AGIGS