LON1_BORBU
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 03-AUG-2022, entry version 139.
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}; OrderedLocusNames=BB_0253;
OS Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)
OS (Borrelia burgdorferi).
OC Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; 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 PRIDE; Q59185; -.
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 OMA; MVNIEDK; -.
DR BRENDA; 3.4.21.53; 902.
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 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; PTHR43718; PTHR43718; 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..806
FT /note="Lon protease 1"
FT /id="PRO_0000076118"
FT DOMAIN 31..233
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
