ID Q1YIN8_MOBAS Unreviewed; 819 AA. AC Q1YIN8; DT 02-MAY-2006, integrated into UniProtKB/TrEMBL. DT 02-MAY-2006, sequence version 1. DT 16-MAY-2012, entry version 38. DE RecName: Full=Lon protease; DE EC=3.4.21.53; GN ORFNames=SI859A1_01435; OS Manganese-oxidizing bacterium (strain SI85-9A1). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Aurantimonadaceae; Aurantimonas. OX NCBI_TaxID=287752; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=SI85-9A1; 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 -!- CATALYTIC ACTIVITY: Hydrolysis of proteins in presence of ATP. CC -!- SUBUNIT: Homohexamer. Organized in a ring with a central cavity CC (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the peptidase S16 family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. 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 SMR; Q1YIN8; 610-788. DR MEROPS; S16.001; -. DR PATRIC; 24560085; VBIAurMan112117_2208. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:InterPro. DR GO; GO:0008846; F:endopeptidase La activity; IEA:EC. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003959; ATPase_AAA_core. DR InterPro; IPR008269; Pept_S16_C. DR InterPro; IPR004815; Pept_S16_lon. DR InterPro; IPR003111; Pept_S16_N. DR InterPro; IPR015947; PUA-like_domain. DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold. DR Pfam; PF00004; AAA; 1. DR Pfam; PF02190; LON; 1. DR Pfam; PF05362; Lon_C; 1. DR PIRSF; PIRSF001174; Lon_proteas; 1. DR SMART; SM00382; AAA; 1. DR SMART; SM00464; LON; 1. DR SUPFAM; SSF88697; PUA-like; 1. DR SUPFAM; SSF54211; Ribosomal_S5_D2-typ_fold; 1. DR TIGRFAMs; TIGR00763; Lon; 1. PE 3: Inferred from homology; KW ATP-binding; Cytoplasm; Hydrolase; Nucleotide-binding; Protease; KW Serine protease. 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 //