ID   LON_ROSCS               Reviewed;         802 AA.
AC   A7NM80;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 86.
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=Rcas_2557;
OS   Roseiflexus castenholzii (strain DSM 13941 / HLO8).
OC   Bacteria; Chloroflexi; Chloroflexia; Chloroflexales; Roseiflexineae;
OC   Roseiflexaceae; Roseiflexus.
OX   NCBI_TaxID=383372;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13941 / HLO8;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Thompson L.S., Brettin T., Bruce D., Detter J.C.,
RA   Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Bryant D.A., Hanada S., Tsukatani Y., Richardson P.;
RT   "Complete sequence of Roseiflexus castenholzii DSM 13941.";
RL   Submitted (AUG-2007) 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: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 {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}.
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; CP000804; ABU58635.1; -; Genomic_DNA.
DR   RefSeq; WP_012121059.1; NC_009767.1.
DR   AlphaFoldDB; A7NM80; -.
DR   SMR; A7NM80; -.
DR   STRING; 383372.Rcas_2557; -.
DR   MEROPS; S16.001; -.
DR   EnsemblBacteria; ABU58635; ABU58635; Rcas_2557.
DR   KEGG; rca:Rcas_2557; -.
DR   eggNOG; COG0466; Bacteria.
DR   HOGENOM; CLU_004109_4_3_0; -.
DR   OMA; GAWQVVD; -.
DR   OrthoDB; 128102at2; -.
DR   Proteomes; UP000000263; 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   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Hydrolase; Nucleotide-binding; Protease;
KW   Serine protease; Stress response.
FT   CHAIN           1..802
FT                   /note="Lon protease"
FT                   /id="PRO_0000396595"
FT   DOMAIN          17..207
FT                   /note="Lon N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT   DOMAIN          599..780
FT                   /note="Lon proteolytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT   ACT_SITE        686
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT   ACT_SITE        729
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT   BINDING         363..370
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
SQ   SEQUENCE   802 AA;  88113 MW;  668675AF263E7949 CRC64;
     MSTPLPTQDP PDIPEVLPIL PLNNVVLFPG MFLPLVVSGD TWVKLVDEAA LATKMVGVFM
     RTQPGEGFDP LALARTGAVA LIVRMLRLPH GAVQILVQGQ ARIQIRQLIV TEPYPQARVA
     IHRDPAVLSV EVSGLARAAL AAFQQIIQLS PTLPDELAIV AANTAQPGML ADLIAANLNL
     KPEDQQLVLD TLDVQERLRQ VLSFLERERE ILTIGRKAQE EMSKSQREYV LRQQLEAIKR
     ELGETDDHAA EIAELRRRLE AANLPEEARK EAEREISRLE RMPPGAAEYV VARTYLDWLL
     DLPWNVSTED NLDLTQARQV LDEDHYDLER IKERIIEYLA VRKLRLEQDA SGSARGPILC
     FVGPPGVGKT SLGTSIARAL GRKFVRVALG GVRDEAEIRG HRRTYIGALP GRIIQGINRA
     GSNNPVFMLD EVDKLSVGFQ GDPAAALLEV LDPEQNVAFV DRYLDVPFDL SRALFICTAN
     RSDTIPPALL DRMELLELAG YTEMEKLEIC RRYLIQRQRN EQGLAERAPT ITEAALRRLI
     REYTHEAGVR DLERRIGAIY RKMATRAAEG QPLPDQVDAP DLDDLLGPPR FRSETLLGED
     EVGVVTGLAW TPTGGDVLFV EASVVPGNGQ LTLTGQLGDV MKESARAALT YARSRARALN
     IPTDFAQICD IHIHVPAGAV PKDGPSAGIT MASALISALT DRRAYKHVAM TGEITLRGKV
     LPIGGVKEKV LAAQRAGVRT VLLPKANAPD LRELPEETRQ QIDIVLVEHM DEVLPRVLHP
     KSESVTLAEP APPDGAGTVQ AT