ID   LON_CLOD6               Reviewed;         787 AA.
AC   Q180E4;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   21-SEP-2011, sequence version 2.
DT   03-AUG-2022, entry version 103.
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=CD630_33010;
OS   Clostridioides difficile (strain 630) (Peptoclostridium difficile).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC   Clostridioides.
OX   NCBI_TaxID=272563;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=630;
RX   PubMed=16804543; DOI=10.1038/ng1830;
RA   Sebaihia M., Wren B.W., Mullany P., Fairweather N.F., Minton N.,
RA   Stabler R., Thomson N.R., Roberts A.P., Cerdeno-Tarraga A.M., Wang H.,
RA   Holden M.T.G., Wright A., Churcher C., Quail M.A., Baker S., Bason N.,
RA   Brooks K., Chillingworth T., Cronin A., Davis P., Dowd L., Fraser A.,
RA   Feltwell T., Hance Z., Holroyd S., Jagels K., Moule S., Mungall K.,
RA   Price C., Rabbinowitsch E., Sharp S., Simmonds M., Stevens K., Unwin L.,
RA   Whithead S., Dupuy B., Dougan G., Barrell B., Parkhill J.;
RT   "The multidrug-resistant human pathogen Clostridium difficile has a highly
RT   mobile, mosaic genome.";
RL   Nat. Genet. 38:779-786(2006).
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; AM180355; CAJ70198.2; -; Genomic_DNA.
DR   RefSeq; WP_003435613.1; NZ_CP010905.2.
DR   RefSeq; YP_001089817.2; NC_009089.1.
DR   AlphaFoldDB; Q180E4; -.
DR   SMR; Q180E4; -.
DR   STRING; 272563.CD630_33010; -.
DR   MEROPS; S16.001; -.
DR   EnsemblBacteria; CAJ70198; CAJ70198; CD630_33010.
DR   KEGG; cdf:CD630_33010; -.
DR   KEGG; pdc:CDIF630_03602; -.
DR   PATRIC; fig|272563.120.peg.3486; -.
DR   eggNOG; COG0466; Bacteria.
DR   OMA; GAWQVVD; -.
DR   PhylomeDB; Q180E4; -.
DR   BioCyc; PDIF272563:G12WB-3468-MON; -.
DR   Proteomes; UP000001978; 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   Reference proteome; Serine protease; Stress response.
FT   CHAIN           1..787
FT                   /note="Lon protease"
FT                   /id="PRO_0000396548"
FT   DOMAIN          12..208
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         362..369
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
SQ   SEQUENCE   787 AA;  89254 MW;  E7CCA55AA9D7773F CRC64;
     MEQNYTKIDH ELPLIPLRGL AIFPYMILNF DIGREISLKA LDQAMMDEEL IFLTSQKEAE
     VDEPGEEDFY HVGTICKVKQ MIKLPGDTVR VLVEGVSRGR VKKIEQEDGY FRAVIEEIVF
     DSDNLDSETE VEIEAFVRNV FDAFEEYINI GNRVSPEILI SLADIEDVDR FIDTIAANIY
     LKSSQKQEIL EEFDIRKRLE LIYSILLEEI DILKIEKKIT LRVKKQMNKV QKEYYLREQL
     KAIQKELGEE EDINSEADEY REKLKKIKAP KTTKEKIEKE IDKFSKISSM SPDVSVSRNY
     LDTIFSLPWN KETKDKLDIT KAKDILDEDH YGLEKVKERI LEYLAIRTLA KSLKGPIICL
     VGPPGTGKTS IVKSIARALN RKFVRISLGG VRDEAEIRGH RRTYVGSIPG RIINGVKEAQ
     TKNPVFLFDE IDKMAADYKG DPASAMLEVL DPEQNKDFVD HYLEIPFDLS KILFVTTANS
     LGNIPRPLLD RMEVIEVSGY IEEEKLNIAK KYLLPKQIKE HALKENFIKI DDETLRSIIN
     HYTREAGVRT LERTIGKICR KVAKKYVEDP TLEEVVINKS DLETYLGKDM FKYQLAEVNP
     QIGLVNGLAW TEVGGVTLEV EVNVLKGKGE IVLTGKLGDV MKESAKTGIS YIRSIVDKFD
     IDPEFYKTND IHIHIPEGAV PKDGPSAGIT MALAVISALT KRPVPGNIAM TGEITLRGRV
     LAVGGVKEKL LAAHRAGITK VLIPKECEAD LDEIPENVKE KMEFVLVEHM DEVLEQALLK
     SGENNEN