LON1_THET2
ID LON1_THET2 Reviewed; 795 AA.
AC Q72KS4;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 115.
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=TT_C0418;
OS Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=262724;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-163 / DSM 7039 / HB27;
RX PubMed=15064768; DOI=10.1038/nbt956;
RA Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H.,
RA Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C.,
RA Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P.,
RA Kramer W., Merkl R., Gottschalk G., Fritz H.-J.;
RT "The genome sequence of the extreme thermophile Thermus thermophilus.";
RL Nat. Biotechnol. 22:547-553(2004).
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; AE017221; AAS80766.1; -; Genomic_DNA.
DR RefSeq; WP_011172865.1; NC_005835.1.
DR AlphaFoldDB; Q72KS4; -.
DR SMR; Q72KS4; -.
DR STRING; 262724.TT_C0418; -.
DR MEROPS; S16.001; -.
DR PRIDE; Q72KS4; -.
DR EnsemblBacteria; AAS80766; AAS80766; TT_C0418.
DR GeneID; 3168778; -.
DR KEGG; tth:TT_C0418; -.
DR eggNOG; COG0466; Bacteria.
DR HOGENOM; CLU_004109_4_3_0; -.
DR OMA; KKMNPVM; -.
DR OrthoDB; 128102at2; -.
DR Proteomes; UP000000592; 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..795
FT /note="Lon protease 1"
FT /id="PRO_0000396611"
FT DOMAIN 9..202
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 596..777
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT ACT_SITE 683
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT ACT_SITE 726
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT BINDING 360..367
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
SQ SEQUENCE 795 AA; 89312 MW; 063878B00EC09741 CRC64;
MKDFLRLELP VLPLRNTVVL PHTTTGVDVG RLKSKRAVEE ALSADRLLFL VTQKDPEVDD
PAPEDLYAVG TLAVVKQAMR LPDGTLQVMV EARSRARLLS YVAAPYLRAV GEAIPEPPLK
DPELARVLVN EVQEAFERYL QNHKTLRLDR YQQEAVKSTR DPAILADLVA HHATWTLEEK
QTILETPEVE ERLKRVLALL LRDLERFELD KKIAARVKEQ MDQNQREYYL REQMKAIQKE
LGGGEDFLTE IEELRERIEK KGMPEPVKEK ALKELKRLER MQPGSPEATV SRTYLDWLLE
VPWTEADPEV LDISVTKRVL DEDHYGLKEV KERILEYLAV RQLTQGKEVK GHAPILCFVG
PPGVGKTSLG KSIARSMNRR FHRISLGGVR DEAEIRGHRR TYIGALPGKI IQGMKQVGVV
NPVFLLDEID KLSSDWRGDP AAALLEVLDP EQNHTFTDHY LDVPYDLSKV FFITTANTLS
TIPRPLLDRM EVIEIPGYTL HEKRAIARYF RWPFQVKEAG LEGRLEITDR AIERIVQEYT
REAGVRNLDR ELSKVARKAA KDYLEKPWEG VRVVDAEDLE AYLGVPKYRP DRAEKEPQVG
AAQGLAWTPY GGTLLTIEAV AVPGTGKVNL TGNLGEVMKE SAHAALTYLR AHREEWGLPE
GFHKDYDLHI HVPEGATPKD GPSAGITIAT ALASALTGRP VRMDIAMTGE ITLRGRVLPI
GGVKEKLLAA HQAGIHRVIL PKENAAELKE VPEEILKDLE IHFVEEVGEV LKLLLLPPPP
PPAVQPDRPQ PGVGA
