ID A0A2T7CDI7_9POAL Unreviewed; 1006 AA.
AC A0A2T7CDI7;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Lon protease homolog, mitochondrial {ECO:0000256|HAMAP-Rule:MF_03120};
DE EC=3.4.21.53 {ECO:0000256|HAMAP-Rule:MF_03120};
GN ORFNames=GQ55_9G502600 {ECO:0000313|EMBL:PUZ41410.1};
OS Panicum hallii var. hallii.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Panicodae; Paniceae; Panicinae; Panicum;
OC Panicum sect. Panicum.
OX NCBI_TaxID=1504633 {ECO:0000313|EMBL:PUZ41410.1, ECO:0000313|Proteomes:UP000244336};
RN [1] {ECO:0000313|EMBL:PUZ41410.1, ECO:0000313|Proteomes:UP000244336}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. HAL2 {ECO:0000313|Proteomes:UP000244336};
RA Lovell J., Jenkins J., Lowry D., Mamidi S., Sreedasyam A., Weng X.,
RA Barry K., Bonette J., Campitelli B., Daum C., Gordon S., Gould B.,
RA Lipzen A., MacQueen A., Palacio-Mejia J., Plott C., Shakirov E., Shu S.,
RA Yoshinaga Y., Zane M., Rokhsar D., Grimwood J., Schmutz J., Juenger T.;
RT "WGS assembly of Panicum hallii var. hallii HAL2.";
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: ATP-dependent serine protease that mediates the selective
CC degradation of misfolded, unassembled or oxidatively damaged
CC polypeptides as well as certain short-lived regulatory proteins in the
CC mitochondrial matrix. May also have a chaperone function in the
CC assembly of inner membrane protein complexes. Participates in the
CC regulation of mitochondrial gene expression and in the maintenance of
CC the integrity of the mitochondrial genome. Binds to mitochondrial DNA
CC in a site-specific manner. {ECO:0000256|HAMAP-Rule:MF_03120}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins in presence of ATP.; EC=3.4.21.53;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03120};
CC -!- SUBUNIT: Homohexamer or homoheptamer. Organized in a ring with a
CC central cavity. {ECO:0000256|HAMAP-Rule:MF_03120}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000256|ARBA:ARBA00004305, ECO:0000256|HAMAP-Rule:MF_03120}.
CC -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000256|HAMAP-
CC Rule:MF_03120, ECO:0000256|PROSITE-ProRule:PRU01122,
CC ECO:0000256|RuleBase:RU000591}.
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DR EMBL; CM009757; PUZ41410.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T7CDI7; -.
DR EnsemblPlants; PUZ41410; PUZ41410; GQ55_9G502600.
DR Gramene; PUZ41410; PUZ41410; GQ55_9G502600.
DR Proteomes; UP000244336; Chromosome 9.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0034599; P:cellular response to oxidative stress; IEA:UniProtKB-UniRule.
DR GO; GO:0051131; P:chaperone-mediated protein complex assembly; IEA:UniProtKB-UniRule.
DR GO; GO:0070407; P:oxidation-dependent protein catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IEA:UniProtKB-UniRule.
DR CDD; cd19500; RecA-like_Lon; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 1.20.5.5270; -; 1.
DR Gene3D; 1.20.58.1480; -; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 2.30.130.40; LON domain-like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_03120; lonm_euk; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR004815; Lon_bac/euk-typ.
DR InterPro; IPR008269; Lon_proteolytic.
DR InterPro; IPR027065; Lon_Prtase.
DR InterPro; IPR003111; Lon_prtase_N.
DR InterPro; IPR046336; Lon_prtase_N_sf.
DR InterPro; IPR027503; Lonm_euk.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR008268; Peptidase_S16_AS.
DR InterPro; IPR015947; PUA-like_sf.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR NCBIfam; TIGR00763; lon; 1.
DR PANTHER; PTHR43718; LON PROTEASE; 1.
DR PANTHER; PTHR43718:SF7; LON PROTEASE HOMOLOG, MITOCHONDRIAL; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF05362; Lon_C; 1.
DR Pfam; PF02190; LON_substr_bdg; 1.
DR PRINTS; PR00830; ENDOLAPTASE.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00464; LON; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF88697; PUA domain-like; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR PROSITE; PS51787; LON_N; 1.
DR PROSITE; PS51786; LON_PROTEOLYTIC; 1.
DR PROSITE; PS01046; LON_SER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_03120}; DNA-binding {ECO:0000256|HAMAP-Rule:MF_03120};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_03120, ECO:0000256|PROSITE-
KW ProRule:PRU01122};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128, ECO:0000256|HAMAP-
KW Rule:MF_03120};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03120,
KW ECO:0000256|RuleBase:RU000591};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|HAMAP-Rule:MF_03120};
KW Reference proteome {ECO:0000313|Proteomes:UP000244336};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|HAMAP-
KW Rule:MF_03120}.
FT DOMAIN 103..312
FT /note="Lon N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51787"
FT DOMAIN 815..999
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT REGION 63..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 146..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 905
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03120,
FT ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 948
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03120,
FT ECO:0000256|PROSITE-ProRule:PRU01122"
FT BINDING 469..476
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03120"
SQ SEQUENCE 1006 AA; 110571 MW; 5CEAA41F812939B4 CRC64;
MLRAAATAGF PARLAAKRPR AATAATRVVV VGAEVRSMLF GALRCGPVPV PRRKACFCSN
ADARSGPEAV EGAEATGGEE GEGENASSAI VPAAFRPEDC HMVIALPLLQ RPLFPGFYMP
IHVKDPKLLQ ALVENSKRSG PYAGAFLVKD DEGTNPNTVT SSESDNSIHD LKGKELLKRL
HDVGTLAQIT RIQGDLVVLL GHHRVRKTEM VAEDPLIVKV DHLKEMPYDK DDDVIKATSF
EVISTLRDVL KTNSLWKDQV QTYTQHMGDF NYPRLADFGA AISGANKLLC QEVLEELDVC
KRLKLTLELV KRELEISKLQ ESIAKTIEEK VTGEQRRYLL NELLKAIKKE LGLETDDKTA
LSEKFRERIE AKKDKCPPHV LQVIEEELTK LQLLEASSSE FSVTRNYLDW LTLLPWRDYS
DENFDVYHAQ CILDEDHYGL ANVKERILEF IAVGKLRGSS QGKIICLSGP PGVGKTSIGR
SIARALNRKF YRFSVGGLAD VAEIKGHRRT YVGAMPGKMA QCLKSVGTAN PLVLIDEIDK
LGRGHSGDPA SALLELLDPE QNANFLDHYL DVPIDLSKVL FVCTANVIEM IPNPLLDRME
IISIAGYITD EKMHIARDYL EKNTREVSGI KPEQVEVTDD ALLALIENYC QEAGVRNLQK
HIEKIYRKIA LKLVRQGVSN GPPRDITIVE AKEDLASFDV AIKVEDEKSK DSLAKDASVD
VNPIDSSLEN INAIPLTTES EIDHNEHSNE DPIEKNLQET TKVFNTSSAP EANKSAQRTT
EALADKSVEK IIVNASNLGD FVGKPVFQTE RIYDQTPVGV VMGLAWNSMG GSTLYIETAK
VEESEGKGAL VVTGQLGDVM KESAQIAHTV CRAVLLEKEP NNPFFAKLKL HLHVPAGAIP
KDGPSAGCTM VTSMLSLAMG KSVKKDLAMT GEVTLTGRVL PIGGVKEKTI AARRSGVKTI
IFPSANRRDF DELASNVKEG LEVHFVDTYN EIYDIAFASD AETQES
//
