ID A0A399EYE0_9DEIN Unreviewed; 792 AA.
AC A0A399EYE0;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Lon protease {ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|PIRNR:PIRNR001174};
DE EC=3.4.21.53 {ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|PIRNR:PIRNR001174};
DE AltName: Full=ATP-dependent protease La {ECO:0000256|HAMAP-Rule:MF_01973};
GN Name=lon1_1 {ECO:0000313|EMBL:RIH88615.1};
GN Synonyms=lon {ECO:0000256|HAMAP-Rule:MF_01973};
GN ORFNames=Mlute_00576 {ECO:0000313|EMBL:RIH88615.1};
OS Meiothermus luteus.
OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Meiothermus.
OX NCBI_TaxID=2026184 {ECO:0000313|EMBL:RIH88615.1, ECO:0000313|Proteomes:UP000265800};
RN [1] {ECO:0000313|EMBL:RIH88615.1, ECO:0000313|Proteomes:UP000265800}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 52599 {ECO:0000313|EMBL:RIH88615.1,
RC ECO:0000313|Proteomes:UP000265800};
RA Da Costa M.S., Albuquerque L., Raposo P., Froufe H.J.C., Barroso C.S.,
RA Egas C.;
RT "Meiothermus luteus KCTC 52599 genome sequencing project.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: ATP-dependent serine protease that mediates the selective
CC degradation of mutant and abnormal proteins as well as certain short-
CC lived regulatory proteins. Required for cellular homeostasis and for
CC survival from DNA damage and developmental changes induced by stress.
CC Degrades polypeptides processively to yield small peptide fragments
CC that are 5 to 10 amino acids long. Binds to DNA in a double-stranded,
CC site-specific manner. {ECO:0000256|HAMAP-Rule:MF_01973}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins in presence of ATP.; EC=3.4.21.53;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01973,
CC ECO:0000256|PIRNR:PIRNR001174, ECO:0000256|PROSITE-ProRule:PRU01122};
CC -!- SUBUNIT: Homohexamer. Organized in a ring with a central cavity.
CC {ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|PIRNR:PIRNR001174}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|PIRNR:PIRNR001174}.
CC -!- INDUCTION: By heat shock. {ECO:0000256|HAMAP-Rule:MF_01973}.
CC -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000256|HAMAP-
CC Rule:MF_01973, ECO:0000256|PIRNR:PIRNR001174, ECO:0000256|PROSITE-
CC ProRule:PRU01122, ECO:0000256|RuleBase:RU000591}.
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:RIH88615.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; QWKZ01000011; RIH88615.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A399EYE0; -.
DR OrthoDB; 9803599at2; -.
DR Proteomes; UP000265800; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; 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:0034605; P:cellular response to heat; 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_01973; lon_bact; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR027543; Lon_bac.
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; 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; PTHR10046; ATP DEPENDENT LON PROTEASE FAMILY MEMBER; 1.
DR PANTHER; PTHR10046:SF56; LON PROTEASE; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF05362; Lon_C; 1.
DR Pfam; PF02190; LON_substr_bdg; 1.
DR PIRSF; PIRSF001174; Lon_proteas; 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 2: Evidence at transcript level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01973};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|PIRNR:PIRNR001174};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|PIRNR:PIRNR001174};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01973,
KW ECO:0000256|PIRNR:PIRNR001174};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|HAMAP-Rule:MF_01973};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|HAMAP-
KW Rule:MF_01973};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_01973}.
FT DOMAIN 5..198
FT /note="Lon N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51787"
FT DOMAIN 591..772
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT ACT_SITE 678
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01973,
FT ECO:0000256|PIRSR:PIRSR001174-1"
FT ACT_SITE 721
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01973,
FT ECO:0000256|PIRSR:PIRSR001174-1"
FT BINDING 355..362
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01973,
FT ECO:0000256|PIRSR:PIRSR001174-2"
SQ SEQUENCE 792 AA; 88470 MW; ED8F4C076C742559 CRC64;
MRLELPVIPL RNTVILPHTT TPVDVGRAKS KRAVEEAMGA DRLIFLVAQR DPEVDDPAPA
DLYTWGVQAV IKQAMRLPDG TLQVVVEARA RAEIKDYLMG PYLRARGEVH TEVLPADEAV
VRVLVDELKE AFDKYVANHK SLRLDRYQLE AVRATSDPAV LADTIAYHAT WTVAEKQEIL
ELVDLEARLR RVLSLLTRDL ERFELDRRVA QRVKEQMDTN QREYYLREQM KAIQKELGGE
DAYNDLEALR KKIEEVGMPE PVKTKALKEL DRLERMQQGS PEATVARTYL DWLTEVPWTK
ADPEVLDIAH TRAVLDEDHY GLKDVKERIL EYLAVRQLTQ GQEVRNKAPI LLLVGPPGVG
KTSLGRSIAR SMNRKFHRIS LGGVRDEAEI RGHRRTYIGA MPGKIIHAMK QVGVINPVIL
LDEIDKMSSD WRGDPASAML EVLDPEQNNT FTDHYLDVPY DLSRVFFITT ANSLQTIPRP
LLDRMEVIEI PGYTNLEKSA IARQYLWPKQ RKESGMEGRM EVTDAAILRV ITEYTREAGV
RGLERELGKI ARKGAKLWLE APWEGVRTVD APDLPAYLGI PRYRPDRAET EPQVGTAQGL
AWTPVGGTLL TIEVAAVPGT GKLNLTGQLG EVMKESAQAA LTYLRAHSAE WGLPEEFHAK
YDLHVHVPDG ATPKDGPSAG ITMATAIASA LTRRPARMDV AMTGEVSLRG KVLPIGGVKE
KLLAAHQAGI HKVVLPKDNE PQLEELPKEV LEGLEIKLVE DVGEVLRYLL LPEPAMPPVR
PGENRQQPGA GA
//
