ID A0A087SGR0_AUXPR Unreviewed; 799 AA.
AC A0A087SGR0;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=ATP-dependent zinc metalloprotease FTSH 11, chloroplastic/mitochondrial {ECO:0000313|EMBL:KFM24914.1};
GN ORFNames=F751_1793 {ECO:0000313|EMBL:KFM24914.1};
OS Auxenochlorella protothecoides (Green microalga) (Chlorella
OS protothecoides).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC Chlorellales; Chlorellaceae; Auxenochlorella.
OX NCBI_TaxID=3075 {ECO:0000313|EMBL:KFM24914.1, ECO:0000313|Proteomes:UP000028924};
RN [1] {ECO:0000313|EMBL:KFM24914.1, ECO:0000313|Proteomes:UP000028924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0710 {ECO:0000313|EMBL:KFM24914.1,
RC ECO:0000313|Proteomes:UP000028924};
RX PubMed=25012212; DOI=10.1186/1471-2164-15-582;
RA Gao C., Wang Y., Shen Y., Yan D., He X., Dai J., Wu Q.;
RT "Oil accumulation mechanisms of the oleaginous microalga Chlorella
RT protothecoides revealed through its genome, transcriptomes, and
RT proteomes.";
RL BMC Genomics 15:582-582(2014).
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; KL662111; KFM24914.1; -; Genomic_DNA.
DR RefSeq; XP_011397802.1; XM_011399500.1.
DR AlphaFoldDB; A0A087SGR0; -.
DR STRING; 3075.A0A087SGR0; -.
DR MEROPS; M41.018; -.
DR GeneID; 23613184; -.
DR KEGG; apro:F751_1793; -.
DR eggNOG; KOG0734; Eukaryota.
DR OrthoDB; 9585at2759; -.
DR Proteomes; UP000028924; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
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: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; IPR000642; Peptidase_M41.
DR InterPro; IPR037219; Peptidase_M41-like.
DR PANTHER; PTHR23076:SF128; ATP-DEPENDENT ZINC METALLOPROTEASE FTSH 11, CHLOROPLASTIC_MITOCHONDRIAL; 1.
DR PANTHER; PTHR23076; METALLOPROTEASE M41 FTSH; 1.
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; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000313|EMBL:KFM24914.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:KFM24914.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000028924}.
FT DOMAIN 407..544
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 69..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 115..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 270..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..158
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 799 AA; 83536 MW; 6EFFC606A5572FD0 CRC64;
MQHTRAVLPR QSLLQGPTFR RTSASRQALN ILFKGVRPVL ASSLPSGPPR IGVAQRQHRL
LVPRRLRALE GESAEDQSAV QAGERGDGTL DEPAETVDVS ATSAAAAEAV TDVDAGASRV
TSDPSASSIA SSAASPSVAS DPGAVASTTS SPTAASAPTD TAGADPAPAP SRHPAVMLAA
ALAAGVSELT RLTLLVPLRW LLLSAVRWVL ARTGLLALNA RREFRLLEVA NAAGRLDGRQ
VAAVMAHVSR QQPEVTVEWF ERACLGQGAG GGSGGGGSAG PDRPGPARPP VEVSAAGARE
YLAALVAMGR LRDYGDAPPS GLVTFLHSAL SFGLTLALLG FISVLGLRAT QRAAGVNSSA
AMGEALAETS VKSFEDVKGC DEALTELQEI VTYLKTPEKF TRLGGKLPKG VLLTGPPGTG
KTLLARAVAG EAGVPFFYKA GSEFDEMFVG VGSRRVRNLF AAAKAKSPCI VFIDEVDAVG
GKRTNWEASG GSRKTLNQLL TEMDGFEENS GVVVMAATNL PETLDPALTR PGRFDRQVAV
PLPDVHGRRA ILDLYFKGKP LAADVDSDSL ARRTPGFSGA QLSNLVNEAA LLAARTGRDC
VDAGLLDEAR DKILMGSPRA LSQTLEARRL TAYHESGHAL VALFTPGARP IHKATIIPRG
HALGMVSQLP DRDEYSTTKQ QLLAQIDVCM GGKAAEELIF GEEFVTTGAT SDLSAATRTA
RHMVEDCGMS ARIGPLSLSD KLGSETRKVA DAEVSDILKA SYERVRGLLT AHQAGLHALA
ASLLEQETLT QSQIKEVTA
//
