ID   LON2_BACSU              Reviewed;         552 AA.
AC   P42425;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   03-AUG-2022, entry version 143.
DE   RecName: Full=Lon protease 2;
DE            EC=3.4.21.53;
DE   AltName: Full=ATP-dependent protease La 2;
GN   Name=lon2; Synonyms=lonB, ysxF; OrderedLocusNames=BSU28210;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RA   Ye R., Wong S.L.;
RL   Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=8969504; DOI=10.1099/13500872-142-11-3067;
RA   Wipat A., Carter N., Brignell C.S., Guy J.B., Piper K., Sanders J.,
RA   Emmerson P.T., Harwood C.R.;
RT   "The dnaB-pheA (256 degrees-240 degrees) region of the Bacillus subtilis
RT   chromosome containing genes responsible for stress responses, the
RT   utilization of plant cell walls and primary metabolism.";
RL   Microbiology 142:3067-3078(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 499-552.
RC   STRAIN=168 / IS58;
RX   PubMed=7961402; DOI=10.1128/jb.176.21.6518-6527.1994;
RA   Riethdorf S., Voelker U., Gerth U., Winkler A., Engelmann S., Hecker M.;
RT   "Cloning, nucleotide sequence, and expression of the Bacillus subtilis lon
RT   gene.";
RL   J. Bacteriol. 176:6518-6527(1994).
RN   [5]
RP   DEVELOPMENTAL STAGE.
RX   PubMed=11325926; DOI=10.1128/jb.183.10.2995-3003.2001;
RA   Serrano M., Hoevel S., Moran C.P. Jr., Henriques A.O., Voelker U.;
RT   "Forespore-specific transcription of the lonB gene during sporulation in
RT   Bacillus subtilis.";
RL   J. Bacteriol. 183:2995-3003(2001).
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 (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of proteins in presence of ATP.; EC=3.4.21.53;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10087};
CC   -!- SUBUNIT: Homohexamer. Organized in a ring with a central cavity (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- DEVELOPMENTAL STAGE: Restricted to the prespore compartment of
CC       sporulating cells. {ECO:0000269|PubMed:11325926}.
CC   -!- INDUCTION: By heat shock. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01122}.
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DR   EMBL; U18229; AAA84744.1; -; Genomic_DNA.
DR   EMBL; Z75208; CAA99539.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14781.1; -; Genomic_DNA.
DR   EMBL; X76424; CAA53987.1; -; Genomic_DNA.
DR   PIR; G69652; G69652.
DR   RefSeq; NP_390699.1; NC_000964.3.
DR   RefSeq; WP_004398923.1; NZ_JNCM01000036.1.
DR   AlphaFoldDB; P42425; -.
DR   SMR; P42425; -.
DR   STRING; 224308.BSU28210; -.
DR   MEROPS; S16.005; -.
DR   PaxDb; P42425; -.
DR   PRIDE; P42425; -.
DR   EnsemblBacteria; CAB14781; CAB14781; BSU_28210.
DR   GeneID; 937484; -.
DR   KEGG; bsu:BSU28210; -.
DR   PATRIC; fig|224308.179.peg.3064; -.
DR   eggNOG; COG0470; Bacteria.
DR   eggNOG; COG1067; Bacteria.
DR   InParanoid; P42425; -.
DR   OMA; GLYFWNL; -.
DR   PhylomeDB; P42425; -.
DR   BioCyc; BSUB:BSU28210-MON; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:InterPro.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030163; P:protein catabolic process; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR008269; Lon_proteolytic.
DR   InterPro; IPR027065; Lon_Prtase.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR008268; Peptidase_S16_AS.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR   InterPro; IPR014251; Spore_LonB.
DR   PANTHER; PTHR10046; PTHR10046; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF05362; Lon_C; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   TIGRFAMs; TIGR02902; spore_lonB; 1.
DR   PROSITE; PS51786; LON_PROTEOLYTIC; 1.
DR   PROSITE; PS01046; LON_SER; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Cytoplasm; Hydrolase; Nucleotide-binding; Protease;
KW   Reference proteome; Serine protease; Stress response.
FT   CHAIN           1..552
FT                   /note="Lon protease 2"
FT                   /id="PRO_0000076117"
FT   DOMAIN          349..535
FT                   /note="Lon proteolytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT   ACT_SITE        445
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10087"
FT   ACT_SITE        488
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10087"
FT   BINDING         97..104
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        500
FT                   /note="V -> G (in Ref. 4; CAA53987)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   552 AA;  60429 MW;  313AAF539662A0B5 CRC64;
     MSWTGIALFI QLFFGIIIGL YFWNLLKNQR TQKVTIDKES KKEMEQLRKM RAISLSEPLS
     EKVRPKSFKD IVGQEDGIKA LKAALCGPNP QHVIVYGPPG VGKTAAARLV LEEAKKHKQS
     PFKEQAVFVE LDATTARFDE RGIADPLIGS VHDPIYQGAG AMGQAGIPQP KQGAVTHAHG
     GVLFIDEIGE LHPIQMNKML KVLEDRKVFL DSAYYSEENT QIPNHIHDIF QNGLPADFRL
     IGATTRMPNE IPPAIRSRCL EVFFRELEKD ELKTVAKTAA DKIEKNISEE GLDLLTSYTR
     NGREAVNMIQ IAAGMAVTEN RKDITIEDIE WVIHSSQLTP KHEQKIGVEP QVGIVNGLAV
     YGPNSGSLLE IEVSVTAAQD KGSINITGIA EEESIGSQSK SIRRKSMAKG SVENVLTVLR
     TMGMKPSDYD IHINFPGGIP IDGPSAGIAM AAGIFSAIHK IPIDNTVAMT GEISLNGLVK
     PIGGVIPKIK AAKQSGAKKV IIPYENQQAI LKQIDGIEII AVKTFQEVLD EILVNPPTEQ
     KPFHIEINKE SV