ID   LON1_BORBU              Reviewed;         806 AA.
AC   Q59185;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   27-MAR-2024, entry version 147.
DE   RecName: Full=Lon protease 1 {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 1 {ECO:0000255|HAMAP-Rule:MF_01973};
GN   Name=lon1 {ECO:0000255|HAMAP-Rule:MF_01973};
GN   OrderedLocusNames=BB_0253;
OS   Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)
OS   (Borrelia burgdorferi).
OC   Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Borreliaceae;
OC   Borreliella.
OX   NCBI_TaxID=224326;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX   PubMed=9266683; DOI=10.1016/s0378-1119(97)00196-0;
RA   Cloud J.L., Marconi R.T., Eggers C.H., Garon C.F., Tilly K., Samuels D.S.;
RT   "Cloning and expression of the Borrelia burgdorferi lon gene.";
RL   Gene 194:137-141(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX   PubMed=9403685; DOI=10.1038/37551;
RA   Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA   Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L.,
RA   Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L.,
RA   Peterson J.D., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M.,
RA   van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F.,
RA   Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C.,
RA   Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B.,
RA   Smith H.O., Venter J.C.;
RT   "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi.";
RL   Nature 390:580-586(1997).
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.
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; L77216; AAB72011.1; -; Genomic_DNA.
DR   EMBL; AE000783; AAB91493.1; -; Genomic_DNA.
DR   PIR; E70131; E70131.
DR   RefSeq; NP_212387.1; NC_001318.1.
DR   RefSeq; WP_002656104.1; NC_001318.1.
DR   AlphaFoldDB; Q59185; -.
DR   SMR; Q59185; -.
DR   STRING; 224326.BB_0253; -.
DR   PaxDb; 224326-BB_0253; -.
DR   EnsemblBacteria; AAB91493; AAB91493; BB_0253.
DR   KEGG; bbu:BB_0253; -.
DR   PATRIC; fig|224326.49.peg.652; -.
DR   HOGENOM; CLU_004109_4_3_12; -.
DR   OrthoDB; 9803599at2; -.
DR   BRENDA; 3.4.21.53; 902.
DR   PHI-base; PHI:11477; -.
DR   Proteomes; UP000001807; 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   CDD; cd19500; RecA-like_Lon; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 1.20.5.5270; -; 1.
DR   Gene3D; 1.20.58.1480; -; 1.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 2.30.130.40; LON domain-like; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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_Su5_D2-typ_SF.
DR   InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR   NCBIfam; TIGR00763; lon; 1.
DR   PANTHER; PTHR43718; LON PROTEASE; 1.
DR   PANTHER; PTHR43718:SF2; LON PROTEASE HOMOLOG, MITOCHONDRIAL; 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   PRINTS; PR00830; ENDOLAPTASE.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00464; LON; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF88697; PUA domain-like; 1.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 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..806
FT                   /note="Lon protease 1"
FT                   /id="PRO_0000076118"
FT   DOMAIN          31..235
FT                   /note="Lon N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT   DOMAIN          626..806
FT                   /note="Lon proteolytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT   ACT_SITE        714
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT   ACT_SITE        757
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT   BINDING         389..396
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
SQ   SEQUENCE   806 AA;  90710 MW;  71F488D719B1424E CRC64;
     MDESKKARSG DKKKEKAVAG ILPHSNKPAR VPLIAVPSHP VFPGMFIPIV LISDSDMKAI
     DYAMKGNGII ALFVLNDKFL EKNNNNAQQK LIIDYSKDIY SVGVTGKIIK KINLPDGGYN
     IFVSTFDRIK FVKVVLNDKF PIIEIDYLKQ IPVRKDDIQS KAVYGSILLR TKEIFAHRKM
     PEVQLNMVNI EDKGKLCDIV ASTISSSKND HQIVLETLNV KDRLKKVLEL IYEELNLIEI
     QNKIAKGIQE RLEKQQKEFF LKEQLKAIKA ELGIGDKKSS DLEKLKTKLK ALELKGEPLE
     VVEKELEKFS LLETSSAEYI VVRNYLELIT ELPWRDFKIN FDKLDLQKSK KILDKTHYGM
     NEVKDRIIEY ISVLKLRKTQ KGAIILLVGP PGVGKTSIGA AIAKVLRTKF FRFSVGGMRD
     ESEIKGHRRT YVGALPGKII QGLRITKTNS PVFLIDEVDK ISASSYGDPF SVLLEVLDPE
     QNVRFRDHYL DLPFDISNVF FILTANSVET IPRPLLNRME IIEISGYIDN EKIEIARKYL
     IPKVLSENGV DKDSLKFQSS SLVQIAQEYA RDNGVRNFEK YLNKIVRKVA RKLIENTEVK
     SYQISNDNLE EYVGVPVFRK ESMPNAMYSG MVMGLAWTNY GGSTLMIETV KTESKVGGIK
     LTGRLGDVMK ESANIAYTYV NSIKGDLSIS KSFFEKNIIH LHIPEGATPK DGPSAGITIA
     SAFISLALNK VVRPHLAMTG ELSLTGNVMM IGGLKEKIIA AKRSGVEHII VPKANRVDLE
     EIPTNIKSGI NFYLVDNMRE VIKLLF
//