ID   LON_RICTY               Reviewed;         784 AA.
AC   Q68WS8;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   27-MAR-2024, entry version 117.
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=RT0437;
OS   Rickettsia typhi (strain ATCC VR-144 / Wilmington).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=257363;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-144 / Wilmington;
RX   PubMed=15317790; DOI=10.1128/jb.186.17.5842-5855.2004;
RA   McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E.,
RA   McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E.,
RA   Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C.,
RA   Yu X.-J., Walker D.H., Weinstock G.M.;
RT   "Complete genome sequence of Rickettsia typhi and comparison with sequences
RT   of other Rickettsiae.";
RL   J. Bacteriol. 186:5842-5855(2004).
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}.
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DR   EMBL; AE017197; AAU03914.1; -; Genomic_DNA.
DR   RefSeq; WP_011190898.1; NC_006142.1.
DR   AlphaFoldDB; Q68WS8; -.
DR   SMR; Q68WS8; -.
DR   MEROPS; S16.001; -.
DR   KEGG; rty:RT0437; -.
DR   eggNOG; COG0466; Bacteria.
DR   HOGENOM; CLU_004109_4_3_5; -.
DR   OrthoDB; 9803599at2; -.
DR   Proteomes; UP000000604; 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   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   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Hydrolase; Nucleotide-binding; Protease;
KW   Serine protease; Stress response.
FT   CHAIN           1..784
FT                   /note="Lon protease"
FT                   /id="PRO_0000280894"
FT   DOMAIN          6..207
FT                   /note="Lon N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT   DOMAIN          592..773
FT                   /note="Lon proteolytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT   ACT_SITE        679
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT   ACT_SITE        722
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT   BINDING         356..363
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
SQ   SEQUENCE   784 AA;  88102 MW;  1475B928B9428BC7 CRC64;
     MNKKSLPLMA LRDMVLFPGV IAPIFVGRKK SLQALSRTTI SEENNTKYIL VTLQKKFDQE
     NPSKHELYNT AILAKIIQIV KLPNNTAKIL IEAVARVKLS DIKDEESFEA NYEIIPDEEI
     LDMHNMRSLV DNAVQLFNKY AMNDKKVNTE IIETINKEIS NKTNFINIIN ILASHLITSL
     ETKQQLLEET SPVKRITTVI TTLTSNIVNS ETEHALQQRV RKQIEKTQRD YYLHEQMKAI
     QKELDEDKSE LADIEKKIKS LKLSKEAKEK AESEFKKLRA MNQMSAESGV TRNYLETLLS
     LPWGKYDNSK IDINQAEKIL NRDHFGLEKV KERIIEYLAV LQRSNKIRGP ILCLIGPPGV
     GKTSLVKSIA EGMGRKYAKF SLGGVRDEAE IRGHRKTYLG SMPGKILGQL KKVKTSNPVM
     LLDEIDKMSS DFRGDPASAL LEVLDPEQNS HFVDHYLEVE YDLSNVVFIA TANSHDLPRA
     LSDRMEKIYI SGYVEEEKLQ IAKNYLVPKQ FKVHKIKKDE ITISEDAILD LIRYYTKESG
     VRALEREICA LTRKALKQIL ADNTVKNISI DSNNLEEFLG AKKYNFGLVE KEDQIGSTTG
     LAYTEVGGEL LTIEALAFSG KGEIKTTGKL GDVMKESAMA AYSCFRSRAP NFGLKYDNYK
     DFDIHIHVPA GAIPKDGPSA GCALFTTIVS LMTKIPVHRT VAMTGEITLR GNVLPIGGLK
     EKLLAASRGG IKTVLIPEEN VKDLKDIPPN IKENLEIISV SNIDQVLKHA LVEMPINKGL
     SYDL
//