LON_CALS8
ID LON_CALS8 Reviewed; 774 AA.
AC A4XJL4;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 85.
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=Csac_1506;
OS Caldicellulosiruptor saccharolyticus (strain ATCC 43494 / DSM 8903 / Tp8T
OS 6331).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacterales Family III. Incertae Sedis; Caldicellulosiruptor.
OX NCBI_TaxID=351627;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43494 / DSM 8903 / Tp8T 6331;
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 Kiss H., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Lykidis A., van de Werken H.J.G., Verhaart M.R.A.,
RA VanFossen A.L., Lewis D.L., Nichols J.D., Goorissen H.P., van Niel E.W.J.,
RA Stams F.J.M., Willquist K.U., Ward D.E., van der Oost J., Kelly R.M.,
RA Kengen S.M.W., Richardson P.;
RT "Genome sequence of the thermophilic hydrogen-producing bacterium
RT Caldicellulosiruptor saccharolyticus DSM 8903.";
RL Submitted (APR-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; CP000679; ABP67099.1; -; Genomic_DNA.
DR AlphaFoldDB; A4XJL4; -.
DR SMR; A4XJL4; -.
DR STRING; 351627.Csac_1506; -.
DR MEROPS; S16.001; -.
DR PRIDE; A4XJL4; -.
DR EnsemblBacteria; ABP67099; ABP67099; Csac_1506.
DR KEGG; csc:Csac_1506; -.
DR eggNOG; COG0466; Bacteria.
DR HOGENOM; CLU_004109_4_3_9; -.
DR OMA; GAWQVVD; -.
DR Proteomes; UP000000256; 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..774
FT /note="Lon protease"
FT /id="PRO_0000396541"
FT DOMAIN 10..203
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 593..774
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT ACT_SITE 680
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT ACT_SITE 723
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT BINDING 357..364
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
SQ SEQUENCE 774 AA; 88114 MW; 7306A6C1E3E74C55 CRC64;
MMIAVTKRTI PVIPLRGLVV FPYMMLHFDV GRQISLKALE EAMNSDQQVL LLAQKDPKQE
EPSPEDLYQY GTVAKIKQML KLPSETSRIL VEGLSRAKVI GYVSVDPYFL VEVEEYKEKG
GNLDDPELEA LIRNVVSAFE EYARLTSRIP PDAILSVTTI QNPGQLADVI AANVIVKLED
KQLLLEQVDL KERLTKLYEL ILREKEIIEI ERKITIKVKK QIDKMQKEYY LREQLKAIQS
ELGEKDSLFS EAQEYREQVQ KLGLSNENLQ KVYKEIDRLE KLPPNSPEIG VIRTYLEWII
DLPWNVKSEE KIDINVVKNV LDEDHYGLTK VKERILEYIA VRKLKNNLKG PILCLVGPPG
VGKTSIAKSI ARALNRNYVR ISLGGLRDEA EIRGHRKTYV GAMPGRIIYA LRQAKTKNPL
ILLDEIDKMS QDFRGDPASA LLEVLDSEQN YAFRDHYVEI PFDLSEVMFI ATANTLETIP
RPLLDRLEVI EITGYTEEEK VEIAKRYLFP KQIEQNGLKK SQIRYDEAVI RDIISFYTRE
SGVRNLEREI ARLCRRVAKE ILEENKKMVR ITTRNLEKYL GVRKYRRDEL IEEDRIGIVT
GLAWTPFGGE TLSVEALVMP GSGKLELTGQ LGDVMKESAK AAVSIIRARA KELGIDENFY
KEYDIHIHVP EGAIPKDGPS AGVTMATAMV SALSKKPVRH DVAMTGEITL SGRVLPIGGV
KEKILAAKRV GIKNVILPYE NKKDVDELED YVKKDMNFVF VKAIDEVFKI AIKE
