ID Q1YIN8_AURMS Unreviewed; 819 AA. AC Q1YIN8; DT 02-MAY-2006, integrated into UniProtKB/TrEMBL. DT 02-MAY-2006, sequence version 1. DT 28-FEB-2018, entry version 80. DE RecName: Full=Lon protease {ECO:0000256|HAMAP-Rule:MF_01973}; DE EC=3.4.21.53 {ECO:0000256|HAMAP-Rule:MF_01973}; 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 / OS SI85-9A1). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; 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., RA Bernier-Latmani R., McCarthy J.K., Torpey J.W., Clement B.G., RA Gaasterland T., Tebo B.M.; RT "Genomic insights into Mn(II) oxidation by the marine RT alphaproteobacterium Aurantimonas sp. strain SI85-9A1."; RL Appl. Environ. Microbiol. 74:2646-2658(2008). CC -!- FUNCTION: ATP-dependent serine protease that mediates the CC selective degradation of mutant and abnormal proteins as well as CC certain short-lived regulatory proteins. Required for cellular CC homeostasis and for survival from DNA damage and developmental CC changes induced by stress. Degrades polypeptides processively to CC yield small peptide fragments that are 5 to 10 amino acids long. CC Binds to DNA in a double-stranded, site-specific manner. CC {ECO:0000256|HAMAP-Rule:MF_01973}. CC -!- CATALYTIC ACTIVITY: Hydrolysis of proteins in presence of ATP. CC {ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|SAAS:SAAS00338825}. CC -!- SUBUNIT: Homohexamer. Organized in a ring with a central cavity. CC {ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|SAAS:SAAS00536021}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01973, CC ECO:0000256|SAAS:SAAS00007367}. CC -!- INDUCTION: By heat shock. {ECO:0000256|HAMAP-Rule:MF_01973}. CC -!- SIMILARITY: Belongs to the peptidase S16 family. CC {ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|SAAS:SAAS00536024}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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 ProteinModelPortal; Q1YIN8; -. DR STRING; 287752.SI859A1_01435; -. DR MEROPS; S16.001; -. DR EnsemblBacteria; EAS50079; EAS50079; SI859A1_01435. DR eggNOG; ENOG4105C6P; Bacteria. DR eggNOG; COG0466; LUCA. DR OrthoDB; POG091H00WA; -. 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: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:0033554; P:cellular response to stress; IEA:UniProtKB-UniRule. DR GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IEA:UniProtKB-UniRule. DR Gene3D; 3.30.230.10; -; 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_substr-bd. DR InterPro; IPR027417; P-loop_NTPase. 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. PE 2: Evidence at transcript level; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01973, KW ECO:0000256|PIRSR:PIRSR001174-2, ECO:0000256|SAAS:SAAS00004265}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000000321}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01973, KW ECO:0000256|SAAS:SAAS00004285}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01973, KW ECO:0000256|SAAS:SAAS00004308}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01973, KW ECO:0000256|PIRSR:PIRSR001174-2, ECO:0000256|SAAS:SAAS00417296}; KW Protease {ECO:0000256|HAMAP-Rule:MF_01973, KW ECO:0000256|SAAS:SAAS00417289, ECO:0000313|EMBL:EAS50079.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000321}; KW Serine protease {ECO:0000256|HAMAP-Rule:MF_01973, KW ECO:0000256|SAAS:SAAS00004356}; KW Stress response {ECO:0000256|HAMAP-Rule:MF_01973, KW ECO:0000256|SAAS:SAAS00004281}. FT DOMAIN 29 220 Lon N-terminal. {ECO:0000259|PROSITE: FT PS51787}. FT DOMAIN 609 790 Lon proteolytic. {ECO:0000259|PROSITE: FT PS51786}. FT NP_BIND 374 381 ATP. {ECO:0000256|HAMAP-Rule:MF_01973, FT ECO:0000256|PIRSR:PIRSR001174-2}. FT COILED 208 245 {ECO:0000256|SAM:Coils}. FT ACT_SITE 696 696 {ECO:0000256|HAMAP-Rule:MF_01973, FT ECO:0000256|PIRSR:PIRSR001174-1}. FT ACT_SITE 739 739 {ECO:0000256|HAMAP-Rule:MF_01973, FT ECO:0000256|PIRSR:PIRSR001174-1}. 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 //