FTSH4_ORYSJ
ID FTSH4_ORYSJ Reviewed; 709 AA.
AC Q8LQJ9; A0A0P0V4D2;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=ATP-dependent zinc metalloprotease FTSH 4, mitochondrial;
DE Short=OsFTSH4;
DE EC=3.4.24.-;
DE Flags: Precursor;
GN Name=FTSH4; OrderedLocusNames=Os01g0574400, LOC_Os01g39250;
GN ORFNames=B1151A10.24-2, OsJ_002240;
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}.
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DR EMBL; AP003413; BAB91902.1; -; Genomic_DNA.
DR EMBL; AP008207; BAF05298.1; -; Genomic_DNA.
DR EMBL; AP014957; BAS72810.1; -; Genomic_DNA.
DR EMBL; CM000138; EAZ12415.1; -; Genomic_DNA.
DR RefSeq; XP_015621656.1; XM_015766170.1.
DR AlphaFoldDB; Q8LQJ9; -.
DR SMR; Q8LQJ9; -.
DR STRING; 4530.OS01T0574400-01; -.
DR MEROPS; M41.026; -.
DR PaxDb; Q8LQJ9; -.
DR PRIDE; Q8LQJ9; -.
DR EnsemblPlants; Os01t0574400-01; Os01t0574400-01; Os01g0574400.
DR GeneID; 4326310; -.
DR Gramene; Os01t0574400-01; Os01t0574400-01; Os01g0574400.
DR KEGG; osa:4326310; -.
DR eggNOG; KOG0734; Eukaryota.
DR HOGENOM; CLU_000688_9_3_1; -.
DR InParanoid; Q8LQJ9; -.
DR OMA; YTDMTEQ; -.
DR OrthoDB; 217929at2759; -.
DR Proteomes; UP000000763; Chromosome 1.
DR Proteomes; UP000007752; Chromosome 1.
DR Proteomes; UP000059680; Chromosome 1.
DR ExpressionAtlas; Q8LQJ9; baseline and differential.
DR Genevisible; Q8LQJ9; 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..15
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 16..709
FT /note="ATP-dependent zinc metalloprotease FTSH 4,
FT mitochondrial"
FT /id="PRO_0000341340"
FT REGION 655..682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 483
FT /evidence="ECO:0000250"
FT BINDING 263..270
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 482
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 486
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 560
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 709 AA; 76786 MW; 8FB3656FEA1F7240 CRC64;
MAWRRVLSQL ARSRPASTIY NELITSRPSW LLRGDVNGGG TLKNLNERYQ SSFVGSLARR
VQNLDVPSEA SLLKEIYKSD PERVIQIFES QPWLHSNRLA LSEYVKALVK VDRLDDSTLL
KTLRRGMAVS GGEGERVGSS SALKSAGQAT KDGILGTANA PIHMVTSETG HFKDQIWRTF
RSLALTFLVI SGIGALIEDR GISKGLGLSQ EVQPIMDSKT KFSDVKGVDE AKAELEEIVH
YLRDPKRFTH LGGKLPKGVL LVGPPGTGKT MLARAVAGEA GVPFFSCSGS EFEEMFVGVG
ARRVRDLFAA AKKRSPCIIF MDEIDAIGGS RNPKDQQYMR MTLNQLLVEL DGFKQNEGII
VIAATNFPQS LDKALVRPGR FDRHIVVPNP DVEGRRQILE SHMLKVLKSD DVDLMIIARG
TPGFSGADLA NLVNVAALKA AMDGAKAVTM NDLEYAKDRI MMGSERKSAV ISDESRKLTA
YHEGGHALVA IHTEGARPVH KATIVPRGRT LGMVSQLPEK DETSFSRKQM LAWLDVSMAG
RVAEELIFGD SEVTSGASSD FQNATKMARA MVTKYGMSKQ LGFVSYNYED DGKSMSTETR
LLIEQEVKSL LENAYNNAKT ILTKHSKEHH VLAQALLEHE TLTGAQIKKI LAQANSTQQQ
QEHAVEAPRK TPAAPSSPAA SAAAAAAATA AAAAKQAAAK AKGVAGIGS
