ID   LON_AQUAE               Reviewed;         795 AA.
AC   O66605;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 136.
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}; OrderedLocusNames=aq_242;
OS   Aquifex aeolicus (strain VF5).
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=224324;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL   Nature 392:353-358(1998).
RN   [2]
RP   SUBUNIT.
RX   PubMed=20600124; DOI=10.1016/j.jmb.2010.06.030;
RA   Duman R.E., Loewe J.;
RT   "Crystal structures of Bacillus subtilis Lon protease.";
RL   J. Mol. Biol. 401:653-670(2010).
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, ECO:0000269|PubMed:20600124}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01973}.
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; AE000657; AAC06568.1; -; Genomic_DNA.
DR   PIR; A70322; A70322.
DR   RefSeq; NP_213165.1; NC_000918.1.
DR   RefSeq; WP_010880103.1; NC_000918.1.
DR   AlphaFoldDB; O66605; -.
DR   SMR; O66605; -.
DR   STRING; 224324.aq_242; -.
DR   MEROPS; S16.001; -.
DR   EnsemblBacteria; AAC06568; AAC06568; aq_242.
DR   KEGG; aae:aq_242; -.
DR   PATRIC; fig|224324.8.peg.197; -.
DR   eggNOG; COG0466; Bacteria.
DR   HOGENOM; CLU_004109_4_3_0; -.
DR   InParanoid; O66605; -.
DR   OMA; GAWQVVD; -.
DR   OrthoDB; 128102at2; -.
DR   Proteomes; UP000000798; Chromosome.
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   1: Evidence at protein level;
KW   ATP-binding; Cytoplasm; Hydrolase; Nucleotide-binding; Protease;
KW   Reference proteome; Serine protease; Stress response.
FT   CHAIN           1..795
FT                   /note="Lon protease"
FT                   /id="PRO_0000076114"
FT   DOMAIN          17..212
FT                   /note="Lon N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT   DOMAIN          605..787
FT                   /note="Lon proteolytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT   ACT_SITE        692
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT   ACT_SITE        735
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT   BINDING         370..377
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
SQ   SEQUENCE   795 AA;  89972 MW;  EC8FDBB7F24EFEFB CRC64;
     MNELFQTPQV EAGIKEYPLM PLRDIVIFPT MVQPLFVGRR FSIRAIEEAN KKDKLIFLVL
     QKDKDVEEPK EEDIYKVGVV AYILRTVPIE DARVKVLVQG LKRGVIKKLE WKEDHYVAQV
     DVIEERDIPP ESQTIEDKAL IKAVKESIDK LVSLGKQIIP DLVVLIKELE EPGKLADMVA
     SILDIKSSQA QEILETFDPR ERLKKVYKFL QDEIGLLEVK QRISEIARER MEKEQREYYL
     RQQLKAIQEE LGEAGGIKAE IEEYTKKFEE VKECMPEEGV KEVEKNIKRL ERLHPESAEA
     GVIRTWLDWV LDLPWCTRTE DNYDLERARE ILDRDHYDLE KVKDRIIEYL AIRKLTQGKE
     APTQILAFVG PPGVGKTSLG RSIAEALGRK FVRIALGGIR DEAEIRGHRR TYVGAMPGRI
     IQAIKQAGTK NPVIMLDEID KLAISFQGDP AAALLEVLDP EQNKKFTDLY IGIPFDLSEV
     IFICTGNRAD TIPTPLLDRM ELIMLSGYSE EEKLFIAKKH LIPKLIPLHG FSPEEIEFTD
     EAILEIIRGY TREAGVRNLQ RQISAVLRKI AVKKLQGEKG PFNITPELVR KLLGVPRYRP
     EREKKPLVGV ATGLAWTEVG GEIMFIEATK MKGKGSLVLT GSLGDIMKES AQAALSYIRS
     KAEDYGIDPD IFSQVDVHVH VPEGAVPKDG PSAGVAIATA LLSLFTDIPV RMDVAMTGEI
     TLRGRVLPVG GLKEKILAAK RAEIYEVILP AKNKDEVMEE LPEYVREKMT LHFVDNLEEV
     FKIALVREPK PLKEA