ID A0A2P6R9Z7_ROSCH Unreviewed; 815 AA.
AC A0A2P6R9Z7;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Putative ATPase, AAA-type, core, peptidase, FtsH, peptidase M41, FtsH extracellular {ECO:0000313|EMBL:PRQ43244.1};
GN ORFNames=RchiOBHm_Chr3g0466351 {ECO:0000313|EMBL:PRQ43244.1};
OS Rosa chinensis (China rose).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Rosoideae; Rosoideae incertae sedis;
OC Rosa.
OX NCBI_TaxID=74649 {ECO:0000313|EMBL:PRQ43244.1, ECO:0000313|Proteomes:UP000238479};
RN [1] {ECO:0000313|EMBL:PRQ43244.1, ECO:0000313|Proteomes:UP000238479}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Old Blush {ECO:0000313|Proteomes:UP000238479};
RA Bendahmane M.;
RT "The Rosa genome provides new insights in the design of modern roses.";
RL Nat. Genet. 0:0-0(2018).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: In the C-terminal section; belongs to the peptidase M41
CC family. {ECO:0000256|ARBA:ARBA00010044}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the AAA ATPase
CC family. {ECO:0000256|ARBA:ARBA00010550}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PRQ43244.1}.
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DR EMBL; PDCK01000041; PRQ43244.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P6R9Z7; -.
DR STRING; 74649.A0A2P6R9Z7; -.
DR EnsemblPlants; PRQ43244; PRQ43244; RchiOBHm_Chr3g0466351.
DR Gramene; PRQ43244; PRQ43244; RchiOBHm_Chr3g0466351.
DR OMA; FQEEFPF; -.
DR OrthoDB; 9585at2759; -.
DR Proteomes; UP000238479; Chromosome 3.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:UniProt.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd19501; RecA-like_FtsH; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 3.40.1690.20; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.20.58.760; Peptidase M41; 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 NCBIfam; TIGR01241; FtsH_fam; 1.
DR PANTHER; PTHR43655; ATP-DEPENDENT PROTEASE; 1.
DR PANTHER; PTHR43655:SF33; WRKY DOMAIN-CONTAINING PROTEIN; 1.
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; FtsH protease domain-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00674; AAA; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000238479};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 359..499
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 83..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 769..815
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..116
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 769..805
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 815 AA; 89943 MW; AC6CFCE60A8C514D CRC64;
MIFSSGGRLL SRPARSAFQK SVIWVNYNGR AALRHEPPTP LGGNAGISGG LGLLRGYLTY
SGAGKQLVSN TYMSNLKSAL ANPRTRRLFS SERPGKKNYE NYYPKDKKEI PKGNDQKSGS
KEGAGDQGNA QGNFSKQIQD LITPLLFMGF IFISLFLTPQ KHKQISFQEF KNKLLEPGLV
DHIEVANKSV AKVFVRSSPR TQDVSSDDFV KGPENSSPSG GNLSQYKYYF NIGSVDSFEE
KLEEAQEALG IDRHDFVPVI YVAQINWFQE LMKYAPTMLL LGALWFTGRK MPGIGGTGGK
GGRGIFNIGK AQITKVDKNA KNKVFFKDVA GCDEAKQEIM EFVHFLKNPK KYEELGAKIP
KGALLVGPPG TGKTLIAKAT AGESGVPFLS ISGSDFMEMF VGVGPSRVRS LFQEARQCAP
SIIFIDEIDA IGRARGRGGF SGGNDEREST LNQLLVEMDG FGTTAGVVVL AGTNRPDILD
KALLRPGRFD RQITIDKPDI KGRNQIFQIY LKKLKLDREP SHYSERLAAL TPGFAGADIA
NVCNEAALIA ARNESAKITM KHFEAAIDRV IGGLEKKNKV ISKLERRTVA YHEAGHAVAG
WFLEHAEPLL KVTIVPRGTA ALGFAQYVPN ENLLMTKEQL FDMTCMTLGG RASEEVLLGK
ISTGAQNDLE KVTKMTYAQV AVYGFSDKVG LLSFPQRDEF EMTKPYSSKT GAIIDSEVRE
WVAKAYTRTI ELIEEHKEHV GQIAELLLEK EVLHQEDFIR VLGERPWKSE EPTNYDRFKQ
GFQEEEDKEA KETTTEGKDV KDGRSPPLQP DAVPA
//