ID   LON_PORG3               Reviewed;         845 AA.
AC   B2RII6;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 84.
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=PGN_0662;
OS   Porphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / CIP 103683 / JCM
OS   12257 / NCTC 11834 / 2561).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC   Porphyromonas.
OX   NCBI_TaxID=431947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561;
RX   PubMed=18524787; DOI=10.1093/dnares/dsn013;
RA   Naito M., Hirakawa H., Yamashita A., Ohara N., Shoji M., Yukitake H.,
RA   Nakayama K., Toh H., Yoshimura F., Kuhara S., Hattori M., Hayashi T.,
RA   Nakayama K.;
RT   "Determination of the genome sequence of Porphyromonas gingivalis strain
RT   ATCC 33277 and genomic comparison with strain W83 revealed extensive genome
RT   rearrangements in P. gingivalis.";
RL   DNA Res. 15:215-225(2008).
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; AP009380; BAG33181.1; -; Genomic_DNA.
DR   RefSeq; WP_012457682.1; NZ_CP025930.1.
DR   AlphaFoldDB; B2RII6; -.
DR   SMR; B2RII6; -.
DR   STRING; 431947.PGN_0662; -.
DR   PRIDE; B2RII6; -.
DR   EnsemblBacteria; BAG33181; BAG33181; PGN_0662.
DR   GeneID; 29255885; -.
DR   KEGG; pgn:PGN_0662; -.
DR   eggNOG; COG0466; Bacteria.
DR   HOGENOM; CLU_004109_4_3_10; -.
DR   OMA; GAWQVVD; -.
DR   BioCyc; PGIN431947:G1G2V-727-MON; -.
DR   Proteomes; UP000008842; 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..845
FT                   /note="Lon protease"
FT                   /id="PRO_0000396593"
FT   DOMAIN          45..240
FT                   /note="Lon N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT   DOMAIN          629..811
FT                   /note="Lon proteolytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT   ACT_SITE        717
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT   ACT_SITE        760
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   845 AA;  95966 MW;  60CBB5FBFBD876C8 CRC64;
     MIDRKYIRLG EDDEDDGFPV FFPVLSVCEE DEDFKVKEDH MQEEMPILAL RNMILFPGVA
     MPIMVGREKS LKLIRYVEKK GVYFGAVSQR DMDVEEPDRA DLYDVGVVAE IIRVLEMPDG
     TTTAIVQGRQ RFALQEITAT EPFMKGRVKL LPDILPGKNK DHEFEALVST IQDMSLKMME
     LMVERPPREL ILSMRRNKNP MYQINFASAN ISTSIAVKQE LLEISKMKDR GYRLLYLLHK
     ELQVMELKAS IQMKTREEMD KQQKEYFLQQ QIKTIQEELG GNINDIEVQE LRTKATTMKW
     SSEVAETFEK ELRKLERLHP QSPDYSVQMQ YVQTIISLPW GVFSKDNFNL KRAQSVLDRD
     HFGLEKVKER IIEHLAVLKM KGDMKSPIIC LYGPPGVGKT SLGKSIAESL GRKYVRISLG
     GLHDEAEIRG HRRTYIGAMC GRIIQSLQRA GTSNPVFVLD EIDKIDSDYK GDPSSALLEV
     LDPEQNNAFH DNYLDIDFDL SHVLFIATAN SLSSISRPLL DRMELIDVSG YIIEEKVEIA
     ARHLIPKQLV EHGFRKNDIK FSKKTIEKLI DDYTRESGVR TLEKQIAAVI RKITKEAAMN
     VVHTTKVEPS DLVTFLGAPR YTRDRYQGNG DAGVVIGLAW TSVGGEILFI ETSLHRGREP
     KLTLTGNLGD VMKESAVIAL DYIRAHSDEL GISQEIFNNW QVHVHVPEGA IPKDGPSAGI
     TMVTSLVSAL TRRKVRAGIA MTGEITLRGK VLPVGGIKEK ILAAKRSGIT EIILCEENRK
     DIEEINDIYL KGLKFHYVSN INEVLKEALL EEKVIDTTDI YSFGKKTEEE KAEKVEKTEK
     KQRKK