LON2_DESPS
ID LON2_DESPS Reviewed; 774 AA.
AC Q6AK61;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Lon protease 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_01973};
GN Name=lon2 {ECO:0000255|HAMAP-Rule:MF_01973}; OrderedLocusNames=DP2536;
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; CAG37265.1; -; Genomic_DNA.
DR RefSeq; WP_011189777.1; NC_006138.1.
DR AlphaFoldDB; Q6AK61; -.
DR SMR; Q6AK61; -.
DR STRING; 177439.DP2536; -.
DR MEROPS; S16.001; -.
DR PRIDE; Q6AK61; -.
DR EnsemblBacteria; CAG37265; CAG37265; DP2536.
DR KEGG; dps:DP2536; -.
DR eggNOG; COG0466; Bacteria.
DR HOGENOM; CLU_004109_4_3_7; -.
DR OMA; KKMNPVM; -.
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; 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..774
FT /note="Lon protease 2"
FT /id="PRO_0000396555"
FT DOMAIN 5..196
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 588..769
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT ACT_SITE 675
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT ACT_SITE 718
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT BINDING 350..357
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
SQ SEQUENCE 774 AA; 86416 MW; C4743261204F9C23 CRC64;
MTKIYPLMPL RDIVIFPHMV APLVVGREKS IRALEDAMEK KTEIFLVTQL EPTCEDPNEG
EIYQCGTLST VMQLLRLPDG TIKALVEGQR RARIVSRVPH EEFMQVEVEE CTEVLPGQDE
LIAYERELRK AFQQFAHLGK KIGEEVVVSC SSIEDPVKLA NVICSHLPLS SKEKQEVLEV
ETLGGRIELL LEILFRELQL AEVERKINIK VKQKLSRAQR DYYLGEKIRE MQKEIGQGED
GVDEMTELEN IIKAKKMPAY ARARVQKELK KLRGMPAMSA ETTVVRSYID TILGLPWKKR
SKGQLNVLKA EGILNKDHYG LEKPKERILE FLAVQSQVAK LKGPILCFVG PPGVGKTSIC
QSIAKSMGRE FARLSLGGLR DEAEIRGHRR TYVGAMAGKV LRAMQKVGVA NPVFCLDEID
KMSTDFRGDP AAALLEVLDP EQNSSFNDHY LDLDYDLSQV FFITTANSLE GIPIPLQDRM
EIIQLSGYTE EDKQVIAEKY LLPKQLKANG FQKDDIFLSP GAMLTVVRHY TREAGVRGLE
RVLASLCRKV ARDRLQKGKK SKKYRIGEKS VPTYLGTPKY RYGLAEERDE VGLATGLAWT
QVGGVLLQIE VILMPGKGKL TLTGQLGDVM QESAQAAYSY IRSRAKELKL EPDFYEKVDI
HVHVPEGAIP KDGPSAGITI ATTLASALTG RPIRHELAMT GEITLRGRVL PIGGLTEKLL
AAKRGNITKV LLPEENGRDL KDVPAKIKNA LDIKLVSHMD QVLEQALLSK GKNK
