LON_ORITI
ID LON_ORITI Reviewed; 790 AA.
AC B3CUN9;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 77.
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=OTT_1628;
OS Orientia tsutsugamushi (strain Ikeda) (Rickettsia tsutsugamushi).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Orientia.
OX NCBI_TaxID=334380;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ikeda;
RX PubMed=18508905; DOI=10.1093/dnares/dsn011;
RA Nakayama K., Yamashita A., Kurokawa K., Morimoto T., Ogawa M., Fukuhara M.,
RA Urakami H., Ohnishi M., Uchiyama I., Ogura Y., Ooka T., Oshima K.,
RA Tamura A., Hattori M., Hayashi T.;
RT "The whole-genome sequencing of the obligate intracellular bacterium
RT Orientia tsutsugamushi revealed massive gene amplification during reductive
RT genome evolution.";
RL DNA Res. 15:185-199(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; AP008981; BAG41086.1; -; Genomic_DNA.
DR AlphaFoldDB; B3CUN9; -.
DR SMR; B3CUN9; -.
DR MEROPS; S16.001; -.
DR EnsemblBacteria; BAG41086; BAG41086; OTT_1628.
DR KEGG; ott:OTT_1628; -.
DR HOGENOM; CLU_004109_4_3_5; -.
DR OMA; GAWQVVD; -.
DR Proteomes; UP000001033; 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; 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 Serine protease; Stress response.
FT CHAIN 1..790
FT /note="Lon protease"
FT /id="PRO_0000396588"
FT DOMAIN 13..207
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 598..779
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT ACT_SITE 685
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT ACT_SITE 728
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT BINDING 362..369
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
SQ SEQUENCE 790 AA; 88221 MW; DCF447BCB7D85EB9 CRC64;
MAQVLNDISN RVLPLFPIRN TVLFPGLVLP ILIGRDDSVK NLLRLGNDSE NQHTILLTTQ
KNADDIKPSI NSLYKIGVLA KITELVQLPN DNYKILIKVL DRVKLTIRRS HDLLVAEYVI
VPDDEINNAD EIKDKLANAI VLFNKYIRLS KKINPDLLVH VLSYTNQSYV VNALAANLIC
NVANKQSLLE ITDVKQRIER LTDHVAKEII IMETDELITS KAQKNLEKMQ RDCFLNEKMK
IIKNVLGVDD EKSDIAELQK KIDTLHLSKE AKAKAESELK KLKMMNPISA EAALTRNYLD
ILLGLPWKKE KESKININID KALQDLNADH HGLEKVKERI TEYLAVLQRT KKSIGTILCF
IGPPGVGKTS LVKSIAEATK CKYAKFALGG VRDEAEIRGH RKTYIGAMPG KIISLIKREN
SNNLVILLDE IDKISRDSRG DPAFALLEVL DPEQNSRFQD NYLEVEYDLS KVLFIATANS
FNFPIPLRDR MEIIQIPGYV EGEKLEIAKH HLIPKQIKNN GLKNTEISFS DEAILELIRY
YTREAGVRGL ERKIGGICRK VLKKILSSKD IKSESVSKEN IKDYLGSRKY KYGLAEDDNQ
VGITIGLAYT ETGGDLIWVE AVMIPGKGKV KATGKLGDVM KESSQTAFSY FCSRAQKYNV
KYEQYHKYDI HIHFPEGAIP KDGPSAGIAI FTTIVSLMTG IPVKLSVAMT GEITLRGRIL
PIGGLKEKLM AAKRGGIKTV IIPEGNTSDL EDIPNSIKND LDIIPLSEAD QVLDIALATT
VTNSPAETAC
