ID A0A1J7H7X4_LUPAN Unreviewed; 866 AA.
AC A0A1J7H7X4;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=AAA+ ATPase domain-containing protein {ECO:0000259|SMART:SM00382};
GN ORFNames=TanjilG_24021 {ECO:0000313|EMBL:OIW02570.1};
OS Lupinus angustifolius (Narrow-leaved blue lupine).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC genistoids sensu lato; core genistoids; Genisteae; Lupinus.
OX NCBI_TaxID=3871 {ECO:0000313|EMBL:OIW02570.1, ECO:0000313|Proteomes:UP000188354};
RN [1] {ECO:0000313|EMBL:OIW02570.1, ECO:0000313|Proteomes:UP000188354}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Tanjil {ECO:0000313|Proteomes:UP000188354};
RC TISSUE=Whole plant {ECO:0000313|EMBL:OIW02570.1};
RX PubMed=27557478; DOI=10.1111/pbi.12615;
RA Hane J.K., Ming Y., Kamphuis L.G., Nelson M.N., Garg G., Atkins C.A.,
RA Bayer P.E., Bravo A., Bringans S., Cannon S., Edwards D., Foley R.,
RA Gao L.L., Harrison M.J., Huang W., Hurgobin B., Li S., Liu C.W.,
RA McGrath A., Morahan G., Murray J., Weller J., Jian J., Singh K.B.;
RT "A comprehensive draft genome sequence for lupin (Lupinus angustifolius),
RT an emerging health food: insights into plant-microbe interactions and
RT legume evolution.";
RL Plant Biotechnol. J. 15:318-330(2017).
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}.
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DR EMBL; CM007371; OIW02570.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J7H7X4; -.
DR STRING; 3871.A0A1J7H7X4; -.
DR EnsemblPlants; OIW02570; OIW02570; TanjilG_24021.
DR Gramene; OIW02570; OIW02570; TanjilG_24021.
DR OMA; QPRIHGF; -.
DR Proteomes; UP000188354; Chromosome LG11.
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; 3.40.50.300; 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 PANTHER; PTHR23076:SF125; ATP-DEPENDENT ZINC METALLOPROTEASE FTSH PROTEIN; 1.
DR PANTHER; PTHR23076; METALLOPROTEASE M41 FTSH; 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:UP000188354};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 378..518
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 76..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 319..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..121
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 866 AA; 94550 MW; 2A7B9DA992186354 CRC64;
MSTLEYLSPL THTKTYLNFH HWRNSPTSFR QNATRFVPYS VPNRVLRPAN SAIDFGSFRF
DLWLGFKRGY CAATKASSSS SGQESDSGEK SEAKTGEGQG VEKGEPGPGS NRRREKEGKG
GWWWFGSKSK RGGGGNGGKW RWQPIVQAQE VGFLLLQLGI VIFVMRLLRP GIPLPGSEPR
VTTSFVSVPY SEFLSRINSD QVQKVEVDGV HIMFKLKPGV VGTSGQDSGE VASGTSSSRL
QDSELAIKSV APTKRIVYTT TRPSDIRTPY EKMLDNEVEF GSPDKRSGGF FNSALIAMFY
VAVLAGLLHR FPVSFSQHTA GQIRNRKSGT PAGTKSSDQG EAITFADVAG VDEAKEELEE
IVEFLRNPDR YVRLGARPPR GVLLVGLPGT GKTLLAKAVA GEADVPFISC SASEFVELYV
GMGASRVRDL FARAKKEAPS IIFIDEIDAV AKSRDGKFRM VSNDEREQTL NQLLTEMDGF
DSNSQVIVLG ATNRSDVLDP ALRRPGRFDR VVMVETPDRI GRESILKVHI KKKELPLAKD
VEVADVAFMT TGFTGADLAN LVNEAALLAG RQNKVVVEKI DFIQAVERSI AGIEKKTARL
QGSEKAVVAR HEAGHAVVGT AVAKLLLGQP RVEDITVMLL ICELRNCLTD NSVPYYLVYA
ITNKAYLFII QQKLSILPRS GGALGFTYIP PTTEDRYLLF IDELYGRLVT LLGGRAAEEV
IYSGRVSTGA LDDIRRATDM AYKAIAEYGL NQTIGPMSIS TLSNGGMDES GSGLWGKDQG
HLVDLVQGEV KALLQSAMEV SLSVVRANPT VLEGLGAHLE EKEKVEGEEL QKWLRLVVAP
TELAIFIKGK QESLLPLQTI PLQTSS
//
