ID Q1YIN8_AURMS Unreviewed; 819 AA. AC Q1YIN8; DT 02-MAY-2006, integrated into UniProtKB/TrEMBL. DT 02-MAY-2006, sequence version 1. DT 02-OCT-2024, entry version 110. 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 ORFNames=SI859A1_01435 {ECO:0000313|EMBL:EAS50079.1}; OS Aurantimonas manganoxydans (strain ATCC BAA-1229 / DSM 21871 / SI85-9A1). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Aurantimonadaceae; Aurantimonas. OX NCBI_TaxID=287752 {ECO:0000313|EMBL:EAS50079.1, ECO:0000313|Proteomes:UP000000321}; RN [1] {ECO:0000313|EMBL:EAS50079.1, ECO:0000313|Proteomes:UP000000321} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SI85-9A1 {ECO:0000313|EMBL:EAS50079.1, RC ECO:0000313|Proteomes:UP000000321}; RX PubMed=18344346; DOI=10.1128/AEM.01656-07; RA Dick G.J., Podell S., Johnson H.A., Rivera-Espinoza Y., Bernier-Latmani R., RA McCarthy J.K., Torpey J.W., Clement B.G., Gaasterland T., Tebo B.M.; RT "Genomic insights into Mn(II) oxidation by the marine alphaproteobacterium RT Aurantimonas sp. strain SI85-9A1."; RL Appl. Environ. Microbiol. 74:2646-2658(2008). 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:EAS50079.1}. 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; AAPJ01000003; EAS50079.1; -; Genomic_DNA. DR AlphaFoldDB; Q1YIN8; -. DR MEROPS; S16.001; -. DR HOGENOM; CLU_004109_4_3_5; -. DR BioCyc; AURANTIMONAS:SI859A1_01435-MONOMER; -. DR Proteomes; UP000000321; 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 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; 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|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_01973}; KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|HAMAP-Rule:MF_01973}; KW Reference proteome {ECO:0000313|Proteomes:UP000000321}; 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 29..222 FT /note="Lon N-terminal" FT /evidence="ECO:0000259|PROSITE:PS51787" FT DOMAIN 609..790 FT /note="Lon proteolytic" FT /evidence="ECO:0000259|PROSITE:PS51786" FT REGION 1..20 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 798..819 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 208..245 FT /evidence="ECO:0000256|SAM:Coils" FT ACT_SITE 696 FT /evidence="ECO:0000256|HAMAP-Rule:MF_01973, FT ECO:0000256|PIRSR:PIRSR001174-1" FT ACT_SITE 739 FT /evidence="ECO:0000256|HAMAP-Rule:MF_01973, FT ECO:0000256|PIRSR:PIRSR001174-1" FT BINDING 374..381 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 819 AA; 90552 MW; E0322396DEA85C95 CRC64; MAEHGEDAVE RNTMSDTQER QGAAEAALYP VLPLRDIVVF PHMIVPLFVG REKSIKALEE VMGADKQILL ATQKNASDED PTADAIYEIG TVANVLQLLK LPDGTVKVLV EGMGRAKIES FSPRTEWHEA SASLIEETEE DPVEIEALAR SVVSEFENYV KLNKKISPEV VGAAGQIEDY SKLADTVASH LAIKIPEKQD MLAMISVRER LEKALGFMES EISVLQVEKR IRSRVKRQME KTQREYYLNE QMKAIQKELG DGEDGRDEMA ELEDRIKKTK LSKEAREKVA AEMKKLKQMS PMSAESTVVR NYLDWILGLP WGVKSRVKVD LKKAEDVLEA DHFGLEKVKE RIVEYLAVQS RQSKLKGPIL CLVGPPGVGK TSLAKSIAKA TGREYVRMAL GGVRDEAEIR GHRRTYIGSM PGKVIQSMKK AKKTNPLFLL DEIDKMGQDF RGDPSSALLE VLDPEQNASF VDHYLEVEYD LSSTMFVTTA NTLNIPAPLM DRMEIIRIAG YTEDEKVEIA SRHLLPKAIR DHALKPEEFS VSADALQEIA RRYTREAGVR NFERELMTLA RKAVTKILKG EETKIEVTAA NLADYLGVPR YRYGEAETED QVGVVTGLAW TEVGGELLTI EGVMMPGKGK MTVTGNLKEV MKESISAAAS YVRSRALDYG IKPPLFEKRD IHVHVPEGAT PKDGPSAGVG MATAIVSVLT GIPVRRDIAM TGEITLRGRV LPIGGLKEKL LAALRGGIKK VLIPQENAKD LADIPDNVKN GLEIVPVSRM GEVLRHALIE MPTPVEWSEV DEPMSGQPLV ENGATAVAH //