LON_DESRM
ID LON_DESRM Reviewed; 810 AA.
AC A4J7L6;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 91.
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=Dred_2559;
OS Desulforamulus reducens (strain ATCC BAA-1160 / DSM 100696 / MI-1)
OS (Desulfotomaculum reducens).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptococcaceae;
OC Desulforamulus.
OX NCBI_TaxID=349161;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1160 / DSM 100696 / MI-1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Sims D., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Kim E., Tebo B.M., Richardson P.;
RT "Complete sequence of Desulfotomaculum reducens MI-1.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000612; ABO51069.1; -; Genomic_DNA.
DR RefSeq; WP_011878867.1; NC_009253.1.
DR AlphaFoldDB; A4J7L6; -.
DR SMR; A4J7L6; -.
DR STRING; 349161.Dred_2559; -.
DR MEROPS; S16.001; -.
DR PRIDE; A4J7L6; -.
DR EnsemblBacteria; ABO51069; ABO51069; Dred_2559.
DR KEGG; drm:Dred_2559; -.
DR eggNOG; COG0466; Bacteria.
DR HOGENOM; CLU_004109_4_3_9; -.
DR OMA; GAWQVVD; -.
DR OrthoDB; 128102at2; -.
DR Proteomes; UP000001556; 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 Reference proteome; Serine protease; Stress response.
FT CHAIN 1..810
FT /note="Lon protease"
FT /id="PRO_0000396557"
FT DOMAIN 8..199
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 589..770
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT ACT_SITE 676
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT ACT_SITE 719
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT BINDING 353..360
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
SQ SEQUENCE 810 AA; 91333 MW; 303024FC556AFADC CRC64;
MNSEIKSLPL LPLRGILVFP YMVIHLDVGR EKSIQAIEEA MVQDRMIFLA TQREAQTDEP
TVDDIYNIGT VAEVKQLLKL PGGTIRVLVE GIARAKIEKY EHQDPYFRVE VQQYSEEFEK
GAEVEALMRS LVYQFEQYVK LSKRIPPETV VSVVNLEEPG RLADIIASHL ALKIEDKQNV
LESVEIVDRL EKLCGIVAKE LEIVELERKI NIRVRKQMEK TQKEYYLREQ MKAIQKELGE
KDERVAECEE FREKISKAKF PKEAEEKALK EVERLEKMPP MAAEAAVVRN YLDWMLSLPW
SKSTKDRIDI NAAEEVLEAD HYGLKDPKER ITEYLAIRKL AKKMKGPILC LVGPPGVGKT
SLGRSVARAL DRKFVRISLG GVRDEAEIRG HRRTYVGAMP GRVIQGMRTA GSKNPVFLLD
EIDKMASDFR GDPSSALLEV LDPEQNSTFS DHYIETPFDL SNVMFITTAN NMYSIPRPLL
DRMEVIQISG YTEEEKLQIA KRHLMPKQIK DHGLTEEMIQ ISENTILKVI REYTRESGVR
NLERKIASIC RKTAKKIVAG QAEKVKVTTQ NLEQFLGIPR YRYGVAEQND EVGTVTGMAW
TEVGGDTLVI EVTTYKGTGR MTLTGKLGDV MKESAQAGYS FIRSRAQELG IDQEMFEKWD
LHIHIPEGAI PKDGPSAGIT MATAMASVLT GRKVRHDIAM TGEITLRGRV LPVGGIKEKV
MAAHRAGIKL IILPNDNKKD LEDIPVNIKK QLEFKLVDHI DQVLAIALLE KEVVDTTTVL
EPEAAVMDNP HFSAVDSQEV QQQGGTQLPS
