ID   LON_BRUA2               Reviewed;         812 AA.
AC   Q2YPX3; O52605; Q57D31;
DT   07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 97.
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=BAB1_1130;
OS   Brucella abortus (strain 2308).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=359391;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INDUCTION.
RX   PubMed=10672180; DOI=10.1046/j.1365-2958.2000.01726.x;
RA   Robertson G.T., Kovach M.E., Allen C.A., Ficht T.A., Roop R.M. II;
RT   "The Brucella abortus Lon functions as a generalized stress response
RT   protease and is required for wild-type virulence in BALB/c mice.";
RL   Mol. Microbiol. 35:577-588(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2308;
RX   PubMed=16299333; DOI=10.1128/iai.73.12.8353-8361.2005;
RA   Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A.,
RA   Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.;
RT   "Whole-genome analyses of speciation events in pathogenic Brucellae.";
RL   Infect. Immun. 73:8353-8361(2005).
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). Required for wild-type virulence
CC       during the initial stages of infection in the mouse model, but not
CC       essential for the establishment and maintenance of chronic infection in
CC       this host. {ECO:0000255|HAMAP-Rule:MF_01973,
CC       ECO:0000269|PubMed:10672180}.
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 stress conditions (acid shock, heat shock, ethanol and
CC       puromycin). {ECO:0000269|PubMed:10672180}.
CC   -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000255|HAMAP-
CC       Rule:MF_01973}.
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DR   EMBL; AF042348; AAB97420.1; -; Genomic_DNA.
DR   EMBL; AM040264; CAJ11086.1; -; Genomic_DNA.
DR   RefSeq; WP_002966840.1; NZ_KN046823.1.
DR   AlphaFoldDB; Q2YPX3; -.
DR   SMR; Q2YPX3; -.
DR   STRING; 359391.BAB1_1130; -.
DR   MEROPS; S16.001; -.
DR   EnsemblBacteria; CAJ11086; CAJ11086; BAB1_1130.
DR   GeneID; 3787778; -.
DR   KEGG; bmf:BAB1_1130; -.
DR   PATRIC; fig|359391.11.peg.30; -.
DR   HOGENOM; CLU_004109_4_3_5; -.
DR   OMA; GAWQVVD; -.
DR   PhylomeDB; Q2YPX3; -.
DR   PHI-base; PHI:8922; -.
DR   Proteomes; UP000002719; Chromosome I.
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   2: Evidence at transcript level;
KW   ATP-binding; Cytoplasm; Hydrolase; Nucleotide-binding; Protease;
KW   Reference proteome; Serine protease; Stress response.
FT   CHAIN           1..812
FT                   /note="Lon protease"
FT                   /id="PRO_0000076122"
FT   DOMAIN          22..213
FT                   /note="Lon N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT   DOMAIN          602..783
FT                   /note="Lon proteolytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT   REGION          787..812
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        689
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT   ACT_SITE        732
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT   BINDING         367..374
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT   CONFLICT        227
FT                   /note="R -> P (in Ref. 1; AAB97420)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   812 AA;  89919 MW;  DB30B60818FF6AAE CRC64;
     MTGIEQKTPV GGSETGGADG LYAVLPLRDI VVFPHMIVPL FVGREKSIRA LEEVMGVDKQ
     ILLATQKNAA DDDPAPDAIY EIGTIANVLQ LLKLPDGTVK VLVEGTARAK ISKFTDREDY
     HEAYAAALQE PEEDAVEIEA LARSVVPDFE NYVKLNKKIS PEVVGAASQI DDYSKLADTV
     ASHLAIKIPE KQEMLSVLSV RERLEKALSF MEAEISVLQV EKRIRSRVKR QMEKTQREYY
     LNEQMKAIQK ELGDSEDGRD EVAEIEERIT KTKLSKEARE KALAELKKLR SMSPMSAEAT
     VVRNYLDWLL SIPWGKKSKV KQDLNFAQEV LDAEHFGLGK VKERIVEYLA VQARSTKIKG
     PILCLVGPPG VGKTSLARSI AKATGREYVR MSLGGVRDEA EIRGHRRTYI GSMPGKVIQS
     MKKAKKSNPL FLLDEIDKMG QDFRGDPSSA MLEVLDPEQN ATFMDHYLEV EYDLSNVMFV
     TTANTMNIPV PLLDRMEIIR IAGYTEDEKL EIAKRHLLPK AIKDHALQPK EFSVTEDALR
     NVIRHYTREA GVRSLEREVM TLARKAVTEI LKTKKKSVKI TDKNLSDYLG VEKFRFGQID
     GEDQVGVVTG LAWTEVGGEL LTIEGVMMPG KGRMTVTGNL RDVMKESISA AASYVRSRAI
     DFGIEPPLFD KRDIHVHVPE GATPKDGPSA GIAMVTAIVS VLTGIPVRKD IAMTGEVTLR
     GRVLPIGGLK EKLLATLRGG IKKVLIPEEN AKDLAEIPDN VKNNLEIVPV SRVGEVLKHA
     LVRQPEPIEW TEQENPTAVP PVEDEAGASL AH