LON1_DESPS
ID LON1_DESPS Reviewed; 808 AA.
AC Q6AS16;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 117.
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=DP0130;
OS Desulfotalea psychrophila (strain LSv54 / DSM 12343).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales;
OC Desulfocapsaceae; Desulfotalea.
OX NCBI_TaxID=177439;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12343 / LSv54;
RX PubMed=15305914; DOI=10.1111/j.1462-2920.2004.00665.x;
RA Rabus R., Ruepp A., Frickey T., Rattei T., Fartmann B., Stark M., Bauer M.,
RA Zibat A., Lombardot T., Becker I., Amann J., Gellner K., Teeling H.,
RA Leuschner W.D., Gloeckner F.-O., Lupas A.N., Amann R., Klenk H.-P.;
RT "The genome of Desulfotalea psychrophila, a sulfate-reducing bacterium from
RT permanently cold Arctic sediments.";
RL Environ. Microbiol. 6:887-902(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; CR522870; CAG34859.1; -; Genomic_DNA.
DR RefSeq; WP_011187375.1; NC_006138.1.
DR AlphaFoldDB; Q6AS16; -.
DR SMR; Q6AS16; -.
DR STRING; 177439.DP0130; -.
DR EnsemblBacteria; CAG34859; CAG34859; DP0130.
DR KEGG; dps:DP0130; -.
DR eggNOG; COG0466; Bacteria.
DR HOGENOM; CLU_004109_1_0_7; -.
DR OMA; VLDCVPM; -.
DR OrthoDB; 128102at2; -.
DR Proteomes; UP000000602; 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 Reference proteome; Serine protease; Stress response.
FT CHAIN 1..808
FT /note="Lon protease 1"
FT /id="PRO_0000396556"
FT DOMAIN 35..236
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 627..808
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT ACT_SITE 715
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT ACT_SITE 758
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT BINDING 391..398
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
SQ SEQUENCE 808 AA; 90775 MW; AB7084B6019A42DD CRC64;
MAEEPTILTP DGVENPDHDD LQFPARMEDI LPEMLMVIPL YERPMFPKMM GPIIIEDMRL
QKFILSQKDK KVPLFFALLL TRQDPDGQVK APESADDFYD VGVVAKVIQI SPLTIGEPLQ
FIVEIKARFD VVKLIKKEPL FQVEVKYWQE EKIKVTDELK AYSTAIIDSI KELVHLNPIF
REGLSLLIER INLHEPGSLA DFSAAMTTSS GPEIQKVLAT RSVRKRIELA LVLIKKELEI
SKLKVKISSR IEEQLSKQQR EFFLKQQLQE IKKELGLTKD DTQTEMEKYE NRIKDLHLPE
EAQERIDEEL EKIRLLGPSS PEFNVSRTYL DWLTMMPWGV YTKDNYSVKK ARKILDDDHH
GLDDVKDRII ELISVGSIKG ELTGTILLLT GPPGVGKTSV GQSIARSLGR KFFRFSLGGM
RDEAEIKGHR RTYIGAMPGK VIQAIKSCKS ANPLIMLDEI DKIGASFRGD PASALLEVLD
PEQNSDFLDH YLDVRFDLSK VLFICTANLL DTIPPALLDR MERIELPGYI LAEKIAIARK
HLIPRQMKHH GLRPSQIIIS NPVLTAIVEG YAREAGVRGL ETCIRKILRK TITSHLAGGL
EKVRIRKRDL RGLLGRRLFA EEQVYSTPRV GVITGLAYTN MGGTTLYIES LAVPTGDSGF
KQTGQLGKVM IESSEIAYSY IRFLLGDDSA AVKFFNKNFI HLHVPAGATP KDGPSAGITM
ACSLYSMATG KTIVPGVAMT GELTLTGLVM PIGGVKEKMI AARRAHVKQV ILPKENEEDF
DMLPDYIKED LSAKFVETFE DVLKICFK
