LON_DICT6
ID LON_DICT6 Reviewed; 792 AA.
AC B5YFG2;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 73.
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=DICTH_1451;
OS Dictyoglomus thermophilum (strain ATCC 35947 / DSM 3960 / H-6-12).
OC Bacteria; Dictyoglomi; Dictyoglomales; Dictyoglomaceae; Dictyoglomus.
OX NCBI_TaxID=309799;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35947 / DSM 3960 / H-6-12;
RX PubMed=24558247; DOI=10.1128/genomea.00109-14;
RA Coil D.A., Badger J.H., Forberger H.C., Riggs F., Madupu R., Fedorova N.,
RA Ward N., Robb F.T., Eisen J.A.;
RT "Complete Genome Sequence of the Extreme Thermophile Dictyoglomus
RT thermophilum H-6-12.";
RL Genome Announc. 2:0-0(2014).
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; CP001146; ACI18312.1; -; Genomic_DNA.
DR AlphaFoldDB; B5YFG2; -.
DR SMR; B5YFG2; -.
DR STRING; 309799.DICTH_1451; -.
DR MEROPS; S16.001; -.
DR EnsemblBacteria; ACI18312; ACI18312; DICTH_1451.
DR KEGG; dth:DICTH_1451; -.
DR eggNOG; COG0466; Bacteria.
DR HOGENOM; CLU_004109_4_3_0; -.
DR OMA; GAWQVVD; -.
DR Proteomes; UP000001733; 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..792
FT /note="Lon protease"
FT /id="PRO_0000396561"
FT DOMAIN 16..206
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 597..778
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT ACT_SITE 684
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT ACT_SITE 727
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 792 AA; 89422 MW; 4AD88AB9FC340033 CRC64;
MEERELNQTQ DIPEVLPILP LRETVVYPQM LIPLIVGREK SIRLVEDALS GNKLIGMCMQ
KTPVEDPTPD DIYRIGTVGI IVRSLRFPDN TLRLFVQGLQ RIRVIEFLET EPYFKAKVEV
IEEKVEKTVE IEGMMRNLLN LFQKMASLIP QFPEELLINA MNIQEPGRLA DFIAFNTNLN
INEKQEILET IDVKERLQKV TYYLTRELEI LEIANKIQNE VKNEIEKSQK EYFLRQQMKA
IQKELGEIDP REMEINELRQ KLQEAKLPPE AMKEAERELE RLSLMPPGSA EYTVTRTYLD
WLISLPWAIS TEDNLDIKRA EEILNEDHYD LEKVKERILE YLAVRKLKSD MKGPILCFVG
PPGVGKTSLG KSIARALGRK FVRISLGGIR DEAEIRGHRR TYVGALPGRI IQGIRKAESN
NPVFMLDEID KLGSDFRGDP AAALLEVLDP EQNNAFVDNY LGVPFDLSKV MFIATANVLY
TIPPALLDRM EVIELPGYTE YQKMGIAKGF LIPRQLKEHG LEKEQIEFSD DAIRKIIREY
TREAGVRNLE REIASIIRKV AKGIAEGSIT EKVIVKVEDV PKYLGPEKYT YGMKGEKDEV
GVATGLAWTE AGGDILFVEA LVVEGKGNLI LTGKLGEVMQ ESAKTALSYV RSKLKDLNVS
YELLEKADIH VHVPSGAIPK DGPSAGVTIA TAIASALTRR PVKKDIGMTG EITLRGKVLP
VGGIREKVLA AHRAGLTAVI MPKENKKDLE EIPEEVKKEI TFYFVEHADE VLNLALLEVK
ESAEQRNPER IG
