ID A0A6M4A2H5_9BURK Unreviewed; 802 AA. AC A0A6M4A2H5; DT 07-OCT-2020, integrated into UniProtKB/TrEMBL. DT 07-OCT-2020, sequence version 1. DT 24-JAN-2024, entry version 15. 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:QJQ05374.1}; GN ORFNames=EJG51_005390 {ECO:0000313|EMBL:QJQ05374.1}; OS Undibacterium piscinae. OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Oxalobacteraceae; Undibacterium. OX NCBI_TaxID=2495591 {ECO:0000313|EMBL:QJQ05374.1, ECO:0000313|Proteomes:UP000274350}; RN [1] {ECO:0000313|EMBL:QJQ05374.1, ECO:0000313|Proteomes:UP000274350} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S11R28 {ECO:0000313|EMBL:QJQ05374.1, RC ECO:0000313|Proteomes:UP000274350}; RX PubMed=31385778; RA Lee S.Y., Kang W., Kim P.S., Kim H.S., Sung H., Shin N.R., Whon T.W., RA Yun J.H., Lee J.Y., Lee J.Y., Jung M.J., Jeong Y.S., Tak E.J., Han J.E., RA Hyun D.W., Kang M.S., Lee K.E., Lee B.H., Bae J.W.; RT "Undibacterium piscinae sp. nov., isolated from Korean shiner intestine."; RL Int. J. Syst. Evol. Microbiol. 69:3148-3154(2019). 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 --------------------------------------------------------------------------- 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; CP051152; QJQ05374.1; -; Genomic_DNA. DR AlphaFoldDB; A0A6M4A2H5; -. DR KEGG; upi:EJG51_005390; -. DR OrthoDB; 9803599at2; -. DR Proteomes; UP000274350; 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 CDD; cd19500; RecA-like_Lon; 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; 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_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; 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. DR PROSITE; PS01046; LON_SER; 1. PE 2: Evidence at transcript level; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_01973}; 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 Reference proteome {ECO:0000313|Proteomes:UP000274350}; KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|HAMAP- KW Rule:MF_01973}; Stress response {ECO:0000256|HAMAP-Rule:MF_01973}. FT DOMAIN 12..203 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 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" FT BINDING 356..363 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 802 AA; 88875 MW; E86B2A6DDBCF1FFC CRC64; MTTSMITERI ELPLLPLRDV VVFPHMVIPL FVGRPKSIKA LEAAMEMGKS IMLAAQKAAA KDEPSADDIY EIGCIANILQ MLKLPDGTVK VLVEGVQRAR IHKITETESH FSADLTPVAL EEGDDTEIEG MRRAIVQQFD QYVKLNKKIP PEILASLSGI DDAGRLGDTI AAHLPLKLEQ KQVILEIFSV AKRLEHLLGQ LEGELDILQV EKRIRGRVKR QMEKSQREYY LNEQVKAIQK ELGEGEEGAD IDELEKKIVA AKMPKEARDK AMNELKKLKM MSPMSAEATV VRNYIDTVVN LPWKKKSKVN NDLSNAEKVL EDDHYGLDKV KERILEYLAV QQRVDKLKAP ILCFVGPPGV GKTSLGQSIA RATNRKFVRM ALGGVRDEAE IRGHRRTYIG SMPGKILQSL AKVGVRNPLF LLDEVDKMGA DFRGDPSSAL LEVLDPEQNH TFSDHYIEVD FDLSDVMFVA TSNSYNIPAA LLDRMEVIRL SGYTEDEKTS IAQRYLLPKQ IKSNGLKEEE ITIAETAIRD IIRYYTREAG VRSLEREISK ICRKVVKMLL LKKTEKKATI NSKNIDKYLG VRRYDFGMAV KDNQVGQVVG LAWTEVGGDL LTIEAVAMPG KGGVIRTGTL GDVMKESIEA ARTVVRSRAK RLGIKADVFE KSDIHIHVPE GATPKDGPSA GIAMTTALVS IFTGIPVRAD VAMTGEITLR GEVLPIGGLK EKLLAAHRGG IKTVLIPEEN AKDLTDIPDN VKNKLEIIPV RWIDKVLEIA LERQPVALSE EDVAVATATK TDVAVESPAI KH //