ID A0A8T7D5F4_9GAMM Unreviewed; 810 AA. AC A0A8T7D5F4; DT 12-OCT-2022, integrated into UniProtKB/TrEMBL. DT 12-OCT-2022, sequence version 1. DT 27-NOV-2024, entry version 13. 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:NNJ85435.1}; GN ORFNames=HKP13_10980 {ECO:0000313|EMBL:NNJ85435.1}, KJO08_00720 GN {ECO:0000313|EMBL:MBT8419363.1}; OS Gammaproteobacteria bacterium. OC Bacteria; Pseudomonadota; Gammaproteobacteria. OX NCBI_TaxID=1913989 {ECO:0000313|EMBL:NNJ85435.1, ECO:0000313|Proteomes:UP000569833}; RN [1] {ECO:0000313|EMBL:NNJ85435.1, ECO:0000313|Proteomes:UP000569833} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Site_C14 {ECO:0000313|EMBL:NNJ85435.1}; RA Chen Y.-J., Leung P.M., Cook P.L.M., Wong W.W., Kessler A.J., Greening C.; RT "Hydrodynamic disturbance controls microbial community assembly and RT biogeochemical processes in coastal sediments."; RL Submitted (APR-2020) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:MBT8419363.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=LDS-7 {ECO:0000313|EMBL:MBT8419363.1}; RA Chen Y.J., Leung P.M., Cook P.L.M., Wong W.W., Kessler A.J., Greening C.; RT "Hydrodynamic disturbance controls microbial community assembly and RT biogeochemical processes in coastal sediments."; RL Submitted (MAY-2021) 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: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}. 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:NNJ85435.1}. 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; JAHHNN010000032; MBT8419363.1; -; Genomic_DNA. DR EMBL; JABDQX010000448; NNJ85435.1; -; Genomic_DNA. DR Proteomes; UP000569833; Unassembled WGS sequence. DR Proteomes; UP000764094; 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 CDD; cd19500; RecA-like_Lon; 1. DR FunFam; 3.30.230.10:FF:000010; Lon protease; 1. DR FunFam; 1.20.5.5270:FF:000002; Lon protease homolog; 1. DR FunFam; 3.40.50.300:FF:000021; Lon protease homolog; 1. DR Gene3D; 1.10.8.60; -; 1. DR Gene3D; 1.20.5.5270; -; 1. DR Gene3D; 1.20.58.1480; -; 1. DR Gene3D; 3.30.230.10; -; 1. DR Gene3D; 2.30.130.40; LON domain-like; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; IPR054594; Lon_lid. 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; IPR015947; PUA-like_sf. DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF. DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr. DR NCBIfam; TIGR00763; lon; 1. DR PANTHER; PTHR10046; ATP DEPENDENT LON PROTEASE FAMILY MEMBER; 1. DR PANTHER; PTHR10046:SF56; LON PROTEASE; 1. DR Pfam; PF00004; AAA; 1. DR Pfam; PF05362; Lon_C; 1. DR Pfam; PF22667; Lon_lid; 1. DR Pfam; PF02190; LON_substr_bdg; 1. DR PIRSF; PIRSF001174; Lon_proteas; 1. DR PRINTS; PR00830; ENDOLAPTASE. DR SMART; SM00382; AAA; 1. DR SMART; SM00464; LON; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR SUPFAM; SSF88697; PUA domain-like; 1. DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1. DR PROSITE; PS51787; LON_N; 1. DR PROSITE; PS51786; LON_PROTEOLYTIC; 1. PE 2: Evidence at transcript level; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_01973}; 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 19..212 FT /note="Lon N-terminal" FT /evidence="ECO:0000259|PROSITE:PS51787" FT DOMAIN 600..781 FT /note="Lon proteolytic" FT /evidence="ECO:0000259|PROSITE:PS51786" FT REGION 786..810 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 191..218 FT /evidence="ECO:0000256|SAM:Coils" FT COMPBIAS 787..810 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 687 FT /evidence="ECO:0000256|HAMAP-Rule:MF_01973, FT ECO:0000256|PIRSR:PIRSR001174-1" FT ACT_SITE 730 FT /evidence="ECO:0000256|HAMAP-Rule:MF_01973, FT ECO:0000256|PIRSR:PIRSR001174-1" FT BINDING 364..371 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01973, FT ECO:0000256|PIRSR:PIRSR001174-2" SQ SEQUENCE 810 AA; 91016 MW; FD8149CA62DF7620 CRC64; MSNNDRQSSP ESNPTIVSLP VLPLRDVVVY PYMVVPLFVG RAKSIVALER AMVEERKILL TAQRDASQNE PTTEDIYHTG TVSTILQLLK LPDGTVKVLV EGLYRASIER FIETDNYLFA EITKYEEQPV ETKNVEALIR STMTQFEKYV KLNRKISPEI IASLTDINDS GRLADVVAAH LFIKIDQKQE LLETKDVKSR LEQLAHHLER EIDLLQVERK IHGRVKKQME KNQREYYLNE QMKAIQKELG DMEDGTNEIE RLAKKIEEAG MSKEAKEKAT AEIKKLKMMS PMSSEATVVR NYVDWLLDVP WKKRTRIRHD LPKAEGVLEE DHYGLEKVKE RITEYLAVQQ RVKKLKGPIL CLVGPPGVGK TSLGKSIARA TGREFIRMSL GGVRDEAEIR GHRRTYIGAL PGRIIQKLAK GGVRNPLFLL DEVDKMSMDF RGDPSSALLE VLDPEQNHTF NDHYLEVDYD LSEIMFVATA NSMNIPGPLL DRMEVIRIPG YTEIEKLNIA KRYLIPKQTK DNGLKDGEIN ITQNAIQDII RYYTREAGVR NVEREIAKIS RKVVKQKIIS GSDKQTLITP KSLEKYLGVQ RFHYGRAEEE DRIGHVTGLA WTEVGGDLLT IEAAIMPGKG NLSHTGSLGD VMQESIQAAM TVVRSRSKQL GLEPEFYQKH DVHIHVPEGA TPKDGPSAGV GMCTALVSTL TKIPVLSNVA MTGEITLRGE VLPIGGLKEK LLAALRGGIT KVLIPRENQR DLSEIPANIK QGLDIQTVKW IDEVLELALQ YTPTPTELKA DREKPASVGK EGAHDALRTH //