ID   LON_CHLPN               Reviewed;         819 AA.
AC   Q9Z9F4; Q9JQ69;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 145.
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};
GN   OrderedLocusNames=CPn_0027, CP_0749, CpB0031;
OS   Chlamydia pneumoniae (Chlamydophila pneumoniae).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=83558;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CWL029;
RX   PubMed=10192388; DOI=10.1038/7716;
RA   Kalman S., Mitchell W.P., Marathe R., Lammel C.J., Fan J., Hyman R.W.,
RA   Olinger L., Grimwood J., Davis R.W., Stephens R.S.;
RT   "Comparative genomes of Chlamydia pneumoniae and C. trachomatis.";
RL   Nat. Genet. 21:385-389(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AR39;
RX   PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA   Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA   Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA   Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA   Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA   Salzberg S.L., Eisen J.A., Fraser C.M.;
RT   "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT   AR39.";
RL   Nucleic Acids Res. 28:1397-1406(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J138;
RX   PubMed=10871362; DOI=10.1093/nar/28.12.2311;
RA   Shirai M., Hirakawa H., Kimoto M., Tabuchi M., Kishi F., Ouchi K.,
RA   Shiba T., Ishii K., Hattori M., Kuhara S., Nakazawa T.;
RT   "Comparison of whole genome sequences of Chlamydia pneumoniae J138 from
RT   Japan and CWL029 from USA.";
RL   Nucleic Acids Res. 28:2311-2314(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TW-183;
RA   Geng M.M., Schuhmacher A., Muehldorfer I., Bensch K.W., Schaefer K.P.,
RA   Schneider S., Pohl T., Essig A., Marre R., Melchers K.;
RT   "The genome sequence of Chlamydia pneumoniae TW183 and comparison with
RT   other Chlamydia strains based on whole genome sequence analysis.";
RL   Submitted (MAY-2002) 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}.
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DR   EMBL; AE001363; AAD18180.1; -; Genomic_DNA.
DR   EMBL; AE002161; AAF38554.1; -; Genomic_DNA.
DR   EMBL; BA000008; BAA98239.1; -; Genomic_DNA.
DR   EMBL; AE009440; AAP97964.1; -; Genomic_DNA.
DR   PIR; B72128; B72128.
DR   PIR; E86494; E86494.
DR   RefSeq; NP_224235.1; NC_000922.1.
DR   RefSeq; WP_010882677.1; NZ_LN847257.1.
DR   AlphaFoldDB; Q9Z9F4; -.
DR   SMR; Q9Z9F4; -.
DR   STRING; 115711.CP_0749; -.
DR   EnsemblBacteria; AAD18180; AAD18180; CPn_0027.
DR   EnsemblBacteria; AAF38554; AAF38554; CP_0749.
DR   GeneID; 45050074; -.
DR   KEGG; cpa:CP_0749; -.
DR   KEGG; cpj:lon; -.
DR   KEGG; cpn:CPn_0027; -.
DR   KEGG; cpt:CpB0031; -.
DR   PATRIC; fig|115713.3.peg.34; -.
DR   eggNOG; COG0466; Bacteria.
DR   HOGENOM; CLU_004109_2_0_0; -.
DR   OMA; GAWQVVD; -.
DR   OrthoDB; 128102at2; -.
DR   Proteomes; UP000000583; Chromosome.
DR   Proteomes; UP000000801; 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; PTHR43718; PTHR43718; 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..819
FT                   /note="Lon protease"
FT                   /id="PRO_0000076131"
FT   DOMAIN          43..238
FT                   /note="Lon N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT   DOMAIN          635..817
FT                   /note="Lon proteolytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT   REGION          1..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        723
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT   ACT_SITE        766
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT   BINDING         393..400
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
SQ   SEQUENCE   819 AA;  92276 MW;  788BCB2A0D294E6A CRC64;
     MDSTTNSDSP ILDPNPEDVE KLLDESEEES EDQSTERLLP SELFILPLNK RPFFPGMAAP
     ILIESGPYYE VLKVLAKSSQ KYIGLVLTKK ENADILKVSF NQLHKTGVAA RILRIMPIEG
     GSAQVLLSIE ERIRIIEPIK DKYLKARVSY HADNKELTEE LKAYSISIVS VIKDLLKLNP
     LFKEELQIFL GHSDFTEPGK LADFSVALTT ATREELQEVL ETTNMHDRID KALILLKKEL
     DLSRLQSSIN QKIEATITKS QKEFFLKEQL KTIKKELGLE KEDRAIDIEK FSERLRKRHV
     PDYAMEVIQD EIEKLQTLET SSAEYTVCRN YLDWLTIIPW GIQSKEYHDL KKAEIVLNKD
     HYGLDEIKQR ILELISVGKL SKGLKGSIIC LVGPPGVGKT SIGRSIAKVL HRKFFRFSVG
     GMRDEAEIKG HRRTYIGAMP GKMVQALKQS QAMNPVIMID EVDKIGASYH GDPASALLEV
     LDPEQNKDFL DHYLDVRVDL SNVLFILTAN VLDTIPDPLL DRMEILRLSG YILEEKLQIA
     KKYLVPKARK EIGLTASEVN FQPEALKYMI NNYAREAGVR TLNGNIKKVL RKVALKIVQN
     QEKPKSKKIT FKISSKNLQT YLGKPIFSSD RFYESTPVGV ATGLAWTSLG GATLYIESVQ
     VSSLKTDMHL TGQAGEVMKE SSQIAWTYLH SALHRYAPGY TFFPKSQVHI HIPEGATPKD
     GPSAGITMVT SLLSLLLETP VVNNLGMTGE ITLTGRVLGV GGIREKLIAA RRSRLNILIF
     PEDNRRDYEE LPAYLKTGLK IHFVSHYDDV LKVAFPKLK