LON_CHLTR
ID LON_CHLTR Reviewed; 819 AA.
AC O84348;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 128.
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=CT_344;
OS Chlamydia trachomatis (strain D/UW-3/Cx).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=272561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D/UW-3/Cx;
RX PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT trachomatis.";
RL Science 282:754-759(1998).
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; AE001273; AAC67939.1; -; Genomic_DNA.
DR PIR; C71527; C71527.
DR RefSeq; NP_219851.1; NC_000117.1.
DR RefSeq; WP_009871695.1; NC_000117.1.
DR AlphaFoldDB; O84348; -.
DR SMR; O84348; -.
DR STRING; 813.O172_01875; -.
DR EnsemblBacteria; AAC67939; AAC67939; CT_344.
DR GeneID; 884768; -.
DR KEGG; ctr:CT_344; -.
DR PATRIC; fig|272561.5.peg.372; -.
DR HOGENOM; CLU_004109_1_0_0; -.
DR InParanoid; O84348; -.
DR OMA; GAWQVVD; -.
DR Proteomes; UP000000431; 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; IBA:GO_Central.
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; IBA:GO_Central.
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 Reference proteome; Serine protease; Stress response.
FT CHAIN 1..819
FT /note="Lon protease"
FT /id="PRO_0000076132"
FT DOMAIN 42..237
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 634..818
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 724
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT ACT_SITE 767
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT BINDING 392..399
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
SQ SEQUENCE 819 AA; 91965 MW; FEA7802A5441557C CRC64;
MNSTNNTDSQ NLDPNASEVE KLLDESAEAE EKVDDHTPPS ELFILPLNKR PFFPGMAAPL
LIEAGPHYEV LTLLAKSSQK HIGLVLTKKE DANTLKVGFN QLHRVGVSAR ILRIMPIEGG
SAQVLLSIED RIRIVKPIQD KYLKAKVSYH KENKELTEEL KAYSISIVSI IKDLLKLNPL
FKEELQIFLG HSDFTEPGKL ADFSVALTTA TREELQEILE TTDMHDRIDK ALVLLKKELD
LSRLQSSINQ KIEATITKSQ KEFFLKEQLK TIKKELGLEK DDHAVDLEKF MERFNKRDVP
QYAMDVIQDE MDKLQTLETS SAEYAVCRNY LDWLTIVPWG IQTKEYHDLK KAESILNKDH
YGLEDIKQRI LELISVGKLA NGMKGSIICL VGPPGVGKTS IGRSIAKVLH RKFFRFSVGG
MRDEAEIKGH RRTYIGAMPG KLVQALKQSQ IMNPVIMIDE VDKIGSSYHG DPASALLEVL
DPEQNKDFLD HYLDVRVDLS NVLFILTANV LDSIPDPLLD RMEVLRLSGY ILEEKLQIAT
KYLVPRARKE MGLSAQNVTF QPEALKHMIN NYAREAGVRT LNENIKKVLR KVALKIVQNQ
EKNLSKKSRF TITPKNLQDY LGKPVFSSDR FYEKTPVGVA TGLAWTSLGG ATLYIESVQV
PSSSGKADMH LTGQAGDVMK ESSQIAWTYL HSALERYAPG QPFFEKSQVH IHIPEGATPK
DGPSAGITMV TSLLSLLLDV PVLNNLGMTG ELTLTGRVLG IGGIREKLIA ARRSKLNILI
FPEDNRRDYD ELPAYLKKGL KVHFVTHYDD VFKIAFPGV
