LON_BORDL
ID LON_BORDL Reviewed; 816 AA.
AC B5RL78;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 04-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 84.
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=BDU_255;
OS Borrelia duttonii (strain Ly).
OC Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borrelia.
OX NCBI_TaxID=412419;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ly;
RX PubMed=18787695; DOI=10.1371/journal.pgen.1000185;
RA Lescot M., Audic S., Robert C., Nguyen T.T., Blanc G., Cutler S.J.,
RA Wincker P., Couloux A., Claverie J.-M., Raoult D., Drancourt M.;
RT "The genome of Borrelia recurrentis, the agent of deadly louse-borne
RT relapsing fever, is a degraded subset of tick-borne Borrelia duttonii.";
RL PLoS Genet. 4:E1000185-E1000185(2008).
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 {ECO:0000255|HAMAP-Rule:MF_01973}.
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; CP000976; ACH93207.1; -; Genomic_DNA.
DR AlphaFoldDB; B5RL78; -.
DR SMR; B5RL78; -.
DR STRING; 412419.BDU_255; -.
DR EnsemblBacteria; ACH93207; ACH93207; BDU_255.
DR KEGG; bdu:BDU_255; -.
DR eggNOG; COG0466; Bacteria.
DR HOGENOM; CLU_004109_4_3_12; -.
DR OMA; MVNIEDK; -.
DR Proteomes; UP000000611; 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 Serine protease; Stress response.
FT CHAIN 1..816
FT /note="Lon protease"
FT /id="PRO_0000396539"
FT DOMAIN 40..242
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 636..816
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT ACT_SITE 724
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT ACT_SITE 767
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT BINDING 398..405
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
SQ SEQUENCE 816 AA; 92252 MW; 75185EE380A6C506 CRC64;
MKSREIEYFM EEIKDTVSKE KKRSKNSGGI LPHFDKPVRV PLIAVPSHPV FPSMFIPIVI
VSDIDMKAVD YVIKGNGIIS LFVLRDKFLE KSGNNKDGKL TINYQKDIYS VGVTAKIVKK
INLPDGGYNI FVSTIDRVKF VKVVLNEDFP IIEVDYLKQI PIKKYDVNLK AIYSSILLKT
KEIFSHRKMP EFQLNMVNIE DKGRLCDVVA GMIASSKESH QEVLETLSVK DRLKKVLELL
YEELNLIEIQ NKIAKGIQEK LEKQQKEFFL KEQLKAIKTE LGVGDEKNSE FLKMKSKIDA
LALKGEALDA VGRELEKFSF LERHSSEYIV VRNYLELITN LPWEDTKVDF DKFNLQRAEK
ILDKTHYGMR EVKDRILEYI SVLKLRKSQK GAIMLLVGPP GVGKTSIGAA IAEVLNTKFF
RFSVGGIRDE SEIKGHRRTY VGALPGKIIQ GLRITKTNSP VFLIDEIDKV SSSHYGDPFS
VLLEVLDPEQ NVNFRDHYLD LPFDISNVFF ILTANSLETI PTPLLNRMEV IQLSGYVDDE
KIEIARKYLI PKVLKENGVD KDSLKFQSSS LVQIAREYAR DNGLRNFEKY LKQIVRKIAR
KLVEDQSVKA YQISKENLEE YIGIPVFRKE KFLDKAMSPG MVMGLAWTNY GGSTLIIETV
KTESKSPGIK LTGRLGDVMK ESANIAFTYV NSISNELKVH KSFFEKYMIH LHIPEGATPK
DGPSAGITIA SAFISLALNK TVRPNLAMTG ELSLTGNVMA IGGLKAKIIA AKRNGVEHII
IPKANKVDLD DIPINIKNGI NFHLVDSMKE VIKLLF
