ID   LON2_BDEBA              Reviewed;         801 AA.
AC   Q6MGP8;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=Lon protease 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_01973};
GN   Name=lon2 {ECO:0000255|HAMAP-Rule:MF_01973}; OrderedLocusNames=Bd3876;
OS   Bdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIMB 9529 /
OS   HD100).
OC   Bacteria; Proteobacteria; Oligoflexia; Bdellovibrionales;
OC   Bdellovibrionaceae; Bdellovibrio.
OX   NCBI_TaxID=264462;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15356 / DSM 50701 / NCIMB 9529 / HD100;
RX   PubMed=14752164; DOI=10.1126/science.1093027;
RA   Rendulic S., Jagtap P., Rosinus A., Eppinger M., Baar C., Lanz C.,
RA   Keller H., Lambert C., Evans K.J., Goesmann A., Meyer F., Sockett R.E.,
RA   Schuster S.C.;
RT   "A predator unmasked: life cycle of Bdellovibrio bacteriovorus from a
RT   genomic perspective.";
RL   Science 303:689-692(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; BX842656; CAE81231.1; -; Genomic_DNA.
DR   RefSeq; WP_011166174.1; NC_005363.1.
DR   AlphaFoldDB; Q6MGP8; -.
DR   SMR; Q6MGP8; -.
DR   STRING; 264462.Bd3876; -.
DR   MEROPS; S16.001; -.
DR   PRIDE; Q6MGP8; -.
DR   EnsemblBacteria; CAE81231; CAE81231; Bd3876.
DR   KEGG; bba:Bd3876; -.
DR   eggNOG; COG0466; Bacteria.
DR   HOGENOM; CLU_004109_4_3_7; -.
DR   OMA; KKMNPVM; -.
DR   OrthoDB; 128102at2; -.
DR   Proteomes; UP000008080; 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..801
FT                   /note="Lon protease 2"
FT                   /id="PRO_0000396537"
FT   DOMAIN          14..207
FT                   /note="Lon N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT   DOMAIN          597..778
FT                   /note="Lon proteolytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT   REGION          780..801
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        684
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT   ACT_SITE        727
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT   BINDING         361..368
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
SQ   SEQUENCE   801 AA;  88761 MW;  DA4C9AAC6BA791B1 CRC64;
     MSFDDKVLEI PQTLPMLPVR DIVVFPYMII PLFVGRDASI RSVEEALAKN RLIFLASQKD
     ITEENPSPDN IYTVGTVAMI MRMRKLSDGR VKILIQGVAK GRVKNFTKTS PSFEVAVEKI
     EETPVQKTVV ENEALIRTAK EHIERIIALG RPLSPDILLV LDDVSDPGRI ADLIASNLGI
     KVQDAQKVLE TSDATERLKL VNEILAAELE VMQTQSKNRT GAKDDMSKSQ REYFLREQMK
     AIKNELGEGD SKSEEMDELR EKLVNAGMPT HVEAEALKQL GRLERMHPDA SEATMVRTYL
     DWMADLPWSK KSEDHIDLKR SKEILDEDHY ELEKAKDRIM EFLAVRKLKP NLKGPILCFG
     GPPGVGKTSL GKSIARAMGR EYFRIALGGV KDEAEIRGHR RTYVGAMPGK IIQALRQAKT
     SNPVIVLDEI DKLGSDFRGD PSAAMLEVLD PEQNATFRDN YLNVDFDLSN VLFIATANVL
     ENIPPALRDR MEILNIPGYT ENDKLLITKK HLIKRQIEAN GITEENIKFT DEGIKYLIAG
     YTREAGLRNL EREVGSVCRK VAKMVVMEET NFVEVNATTV PELLGPPRFQ RDDKIADSQV
     GVVQGLAWTQ AGGEVLTIEA LKMKGKGHLA LTGQLGDVMK ESAHAAMSYA RAHQEELGIP
     EDFFEKYDVH VHLPAGAIPK DGPSAGITLT TALVSLMTGT PVRHDIAMTG EVTLQGRVLP
     VGGIREKCLA ALNLGITNII IPMACQKDLA DIPKVFKDKI NFILAENLDE VFAVAFDKSA
     KGQEKKPAAK KDPKKTKSLA A