ID   LON_BRECH               Reviewed;         779 AA.
AC   P36772;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Lon protease {ECO:0000255|HAMAP-Rule:MF_01973};
DE            EC=3.4.21.53 {ECO:0000255|HAMAP-Rule:MF_01973};
DE   AltName: Full=ATP-dependent protease La {ECO:0000255|HAMAP-Rule:MF_01973};
GN   Name=lon {ECO:0000255|HAMAP-Rule:MF_01973};
OS   Brevibacillus choshinensis.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX   NCBI_TaxID=54911;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=HPD31;
RX   PubMed=1551846; DOI=10.1128/jb.174.7.2281-2287.1992;
RA   Ito K., Udaka S., Yamagata H.;
RT   "Cloning, characterization, and inactivation of the Bacillus brevis lon
RT   gene.";
RL   J. Bacteriol. 174:2281-2287(1992).
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:0000255|HAMAP-Rule:MF_01973}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of proteins in presence of ATP.; EC=3.4.21.53;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01973};
CC   -!- SUBUNIT: Homohexamer. Organized in a ring with a central cavity.
CC       {ECO:0000255|HAMAP-Rule:MF_01973}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- INDUCTION: By heat shock. {ECO:0000255|HAMAP-Rule:MF_01973}.
CC   -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000255|HAMAP-
CC       Rule:MF_01973}.
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DR   EMBL; D00863; BAA00737.1; -; Genomic_DNA.
DR   AlphaFoldDB; P36772; -.
DR   SMR; P36772; -.
DR   STRING; 54911.AN963_02960; -.
DR   MEROPS; S16.001; -.
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   Gene3D; 2.30.130.40; -; 1.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 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_S5_D2-typ_fold.
DR   InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR   PANTHER; PTHR10046; PTHR10046; 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   SMART; SM00382; AAA; 1.
DR   SMART; SM00464; LON; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   SUPFAM; SSF88697; SSF88697; 1.
DR   TIGRFAMs; TIGR00763; lon; 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; Cytoplasm; Hydrolase; Nucleotide-binding; Protease;
KW   Serine protease; Stress response.
FT   CHAIN           1..779
FT                   /note="Lon protease"
FT                   /id="PRO_0000076120"
FT   DOMAIN          10..201
FT                   /note="Lon N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT   DOMAIN          591..772
FT                   /note="Lon proteolytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT   ACT_SITE        678
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT   ACT_SITE        721
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT   BINDING         355..362
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
SQ   SEQUENCE   779 AA;  87422 MW;  625E0DA9B98941B5 CRC64;
     MGERSGKREL PLLPLRGLLV YPTMVLHLDV GREKSIRALE QAMVDDNKIL LATQEEVHIE
     EPDAEQIYSI GTVARVKQML KLPNGTIRVL VEGLQRAKIE EYLQKEDYFV VSITYLKEEK
     AEENEVEALM RSLLTHFEQY IKLSKKVSPE TLTSVQDIEE PGRLADVIAS HLPLKMKDKQ
     EILETVNIQE RLEILLTILN NEREVLELER KIGNRVKKQM ERTQKEYYLR EQMKAIQKEL
     GDKDGRQGEV DELRAQLEKS DAPERIKAKI EKELERLEKM PSTSAEGSVI RTYIDTLFAL
     PWTKTTEDNL DIKHAEEVLD EDHYGLEKPK ERVLEYLAVQ KLVNSMRGPI LCLVGPPGVG
     KTSLARSVAR ALGREFVRIS LGGVRDEAEI RGHRRTYVGA LPGRIIQGMK QAGTINPVFL
     LDEIDKLASD FRGDPASALL EVLDPNQNDK FSDHYIEETY DLTNVMFITT ANSLDTIPRP
     LLDRMEVISI SGYTELEKLN ILRGYLLPKQ MEDHGLGKDK LQMNEDAMLK LVRLYTREAG
     VRNLNREAAN VCRKAAKIIV GGEKKRVVVT AKTLEALLGK PRYRYGLAEK KDQVGSVTGL
     AWTQAGGDTL NVEVSILAGK GKLTLTGQLG DVMKESAQAA FSYIRSRASE WGIDPEFHEK
     NDIHIHVPEG AIPKDGPSAG ITMATALVSA LTGIPVKKEV GMTGEITLRG RVLPIGGLKE
     KCMSAHRAGL TTIILPKDNE KDIEDIPESV REALTFYPVE HLDEVLRHAL TKQPVGDKK