LON2_BORBU
ID LON2_BORBU Reviewed; 796 AA.
AC O51558;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2012, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Lon protease 2;
DE EC=3.4.21.53;
DE AltName: Full=ATP-dependent protease La 2;
GN Name=lon2; OrderedLocusNames=BB_0613;
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 [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 (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 -!- 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; AE000783; AAC66962.2; -; Genomic_DNA.
DR PIR; D70176; D70176.
DR RefSeq; NP_212747.2; NC_001318.1.
DR RefSeq; WP_002658127.1; NC_001318.1.
DR AlphaFoldDB; O51558; -.
DR SMR; O51558; -.
DR STRING; 224326.BB_0613; -.
DR MEROPS; S16.009; -.
DR PRIDE; O51558; -.
DR EnsemblBacteria; AAC66962; AAC66962; BB_0613.
DR GeneID; 56568049; -.
DR KEGG; bbu:BB_0613; -.
DR PATRIC; fig|224326.49.peg.1003; -.
DR HOGENOM; CLU_004109_4_3_12; -.
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-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; 2.30.130.40; -; 1.
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; 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..796
FT /note="Lon protease 2"
FT /id="PRO_0000076119"
FT DOMAIN 9..204
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 617..796
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT ACT_SITE 702
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10087"
FT ACT_SITE 745
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10087"
FT BINDING 352..359
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 796 AA; 90334 MW; C840B8988691A93F CRC64;
MIKNRKEDLP IVILKENVLF PNITLWVTFD NEYVINSIAQ SMLEERLILF AYSNEPNCDE
SDRGVVKNLC SVGTYSKLIQ VIKISKDVIK VLVECQSRVL IDSVSKKNDY LRAKVTFVPD
SSGLNRELFT YSKFLKETYE AYRNSLSLKS YDADNEPINY FENPSKLVDI IASNSNLENS
IKLELLQELN VKTRIEKLIV NLSIEIDLLD LKKDINSKVR AKLDKGQRDY FLSEQVKEIQ
KRLGKDENDY IDRLNSKDIP EDVKSKIEKE ISRLSKMQMN SPDANIIRSY IELILDLPWN
ENTVMKNHLS EIEFILRNSH YGMDEAKEKI INFLAVYQIN SKVKAPILCL VGPPGIGKTS
LVESIARSLS REFVKISLGG LRDEAEIRGH RRTYVGSLPG VFISAMKRSG KSNPVILLDE
IDKINSSYKG NPESALLEVL DPEQNYKFID HYLEIPYDLS NVLFVTTANS LNGMSKPLLD
RMEIIKVEGY SYIEKLEIAK IFLIPSIIKE SFLDKVYIRI EDDVIFNLIR NYTMESGVRG
LKRVLTNLIR RLVRELLYEY SKDQIIKGNF YSPSSLIHGN NSLFTHDPDI PGIYKIININ
NYYNYVDTED NLDLIKIDSS GFVYGLAWTN YGGTVLPVEA TKFEKKGDII LTGSLGAIMK
ESAQLAYSIV KTYSSKLNFD VKESPEIHLH FPEGATPKDG PSAGITIATA IASILSDKKV
PLDLAMTGEV TLKGFVLPVG GIKEKVLAAY RNGISKVILP KDNKKDYSKL PEEVKDNIDV
KFVSSLEEVF DYLNII
