ID A0A7C6LCW7_9FIRM Unreviewed; 776 AA. AC A0A7C6LCW7; DT 02-DEC-2020, integrated into UniProtKB/TrEMBL. DT 02-DEC-2020, sequence version 1. DT 25-MAY-2022, entry version 7. DE RecName: Full=Lon protease {ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|PIRNR:PIRNR001174}; DE EC=3.4.21.53 {ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|PIRNR:PIRNR001174}; DE AltName: Full=ATP-dependent protease La {ECO:0000256|HAMAP-Rule:MF_01973}; GN Name=lon {ECO:0000256|HAMAP-Rule:MF_01973, GN ECO:0000313|EMBL:HHW07516.1}; GN ORFNames=GXX34_08345 {ECO:0000313|EMBL:HHW07516.1}; OS Clostridia bacterium. OC Bacteria; Firmicutes; Clostridia. OX NCBI_TaxID=2044939 {ECO:0000313|EMBL:HHW07516.1, ECO:0000313|Proteomes:UP000525921}; RN [1] {ECO:0000313|EMBL:HHW07516.1, ECO:0000313|Proteomes:UP000525921} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AS04akNAM_29 {ECO:0000313|EMBL:HHW07516.1}; RX PubMed=32123542; RA Campanaro S., Treu L., Rodriguez-R L.M., Kovalovszki A., Ziels R.M., RA Maus I., Zhu X., Kougias P.G., Basile A., Luo G., Schluter A., RA Konstantinidis K.T., Angelidaki I.; RT "New insights from the biogas microbiome by comprehensive genome-resolved RT metagenomics of nearly 1600 species originating from multiple anaerobic RT digesters."; RL Biotechnol. Biofuels 13:25-20(2020). 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:0000256|HAMAP-Rule:MF_01973}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Hydrolysis of proteins in presence of ATP.; EC=3.4.21.53; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01973, CC ECO:0000256|PIRNR:PIRNR001174, ECO:0000256|PROSITE-ProRule:PRU01122}; CC -!- SUBUNIT: Homohexamer. Organized in a ring with a central cavity. CC {ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|PIRNR:PIRNR001174}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, CC ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|PIRNR:PIRNR001174}. CC -!- INDUCTION: By heat shock. {ECO:0000256|HAMAP-Rule:MF_01973}. CC -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000256|HAMAP- CC Rule:MF_01973, ECO:0000256|PIRNR:PIRNR001174, ECO:0000256|PROSITE- CC ProRule:PRU01122, ECO:0000256|RuleBase:RU000591}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:HHW07516.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; DULZ01000069; HHW07516.1; -; Genomic_DNA. DR Proteomes; UP000525921; Unassembled WGS sequence. 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 2: Evidence at transcript level; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01973, KW ECO:0000256|PIRNR:PIRNR001174}; Coiled coil {ECO:0000256|SAM:Coils}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|PIRNR:PIRNR001174}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|PIRNR:PIRNR001174}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01973, KW ECO:0000256|PIRNR:PIRNR001174}; KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|HAMAP-Rule:MF_01973}; KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|HAMAP- KW Rule:MF_01973}; KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP- KW Rule:MF_01973}. FT DOMAIN 11..202 FT /note="Lon N-terminal" FT /evidence="ECO:0000259|PROSITE:PS51787" FT DOMAIN 592..773 FT /note="Lon proteolytic" FT /evidence="ECO:0000259|PROSITE:PS51786" FT NP_BIND 356..363 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01973, FT ECO:0000256|PIRSR:PIRSR001174-2" FT COILED 127..147 FT /evidence="ECO:0000256|SAM:Coils" FT COILED 183..210 FT /evidence="ECO:0000256|SAM:Coils" FT COILED 237..257 FT /evidence="ECO:0000256|SAM:Coils" FT ACT_SITE 679 FT /evidence="ECO:0000256|HAMAP-Rule:MF_01973, FT ECO:0000256|PIRSR:PIRSR001174-1" FT ACT_SITE 722 FT /evidence="ECO:0000256|HAMAP-Rule:MF_01973, FT ECO:0000256|PIRSR:PIRSR001174-1" SQ SEQUENCE 776 AA; 87624 MW; C543F6E63DBBD51E CRC64; MARNAAEVRE LPLLPLRGLL VFPNMVIHLD VGRDRSVNAI DEAMNSDREI LLVMQKDAQV DVPDLDDVYQ IGTVAEIKQL LKLPGGTIRV LVEGLTRARI TRLLETDPVM RVEVEIPGET YEKTLEIEAL VRNLRELFEQ YVKVSKKIPP ETVMAVVAIE EPGRLADVIA SHLILKLSDK QEILEAIDIK ERLEKLLQIL TNEMEILELE RRISARVRRQ MEKTQKEYYL REQLKAIQKE LGEKDEKAAE VDELREKIEK AKLPKAVEEK ALKELERLEK MPPMVAEATV VRNYLDWLLS VPWSKETRDR LDIHAAEKIL DEDHYGLQDV KDRILEYLAI RQLAPKIRGP ILCFVGPPGV GKTSLGKSIA RCLGRKFVRM SLGGVRDEAE IRGHRRTYVG AMPGRIIQGL KNAGTRNPVF LLDEIDKLGS DFRGDPSSAL LEVLDPEQNN SFSDHYLEVP YDLSKVLFIT TANVTHTIPR PLLDRMEVIQ ISGYTEEEKL EIAKRHLLKK QMQEHGLKDD MLTVSDNALR KIIREYTREA GVRNLERQIA TVCRKTARDI VAKKVTAGKI TSKNLDTYLG MPRYRKRQAE KHNEVGVATG LAVTEFGGDV LAVEATLLNG KGKVTLTGQL GDVMKESAYA GLSYLRSRSE ELNIPEDFHE TMDIHIHVPE GAIPKDGPSA GITMATALAS ALTNRPVRKD VAMTGEITLR GRVLAIGGVK EKVLAAHRVG IQHIILPREN EKDLEEIPAE IRRKLKFHLV EHLDEVLEQA LVREEQ //