ID Q6HD56_BACHK Unreviewed; 776 AA. AC Q6HD56; DT 19-JUL-2004, integrated into UniProtKB/TrEMBL. DT 19-JUL-2004, sequence version 1. DT 13-JUN-2012, entry version 79. DE RecName: Full=Lon protease; DE EC=3.4.21.53; GN Name=lonA; OrderedLocusNames=BT9727_4203; OS Bacillus thuringiensis subsp. konkukian (strain 97-27). OC Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=281309; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=97-27; RX PubMed=16621833; DOI=10.1128/JB.188.9.3382-3390.2006; RA Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., RA Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O., RA Cleland C., Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., RA Goodwin L.A., Hill K.K., Hitchcock P., Jackson P.J., Keim P., RA Kewalramani A.R., Longmire J., Lucas S., Malfatti S., McMurry K., RA Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C., RA Okinaka R.T., Parson-Quintana B., Reilly L.P., Richardson P., RA Robinson D.L., Rubin E., Saunders E., Tapia R., Tesmer J.G., RA Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L., RA Brettin T.S., Gilna P.; RT "Pathogenomic sequence analysis of Bacillus cereus and Bacillus RT thuringiensis isolates closely related to Bacillus anthracis."; RL J. Bacteriol. 188:3382-3390(2006). 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 --------------------------------------------------------------------------- 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; AE017355; AAT60850.1; -; Genomic_DNA. DR RefSeq; YP_038520.1; NC_005957.1. DR ProteinModelPortal; Q6HD56; -. DR SMR; Q6HD56; 492-586, 594-773. DR MEROPS; S16.001; -. DR EnsemblBacteria; EBBACT00000073562; EBBACP00000071648; EBBACG00000073553. DR GeneID; 2855702; -. DR GenomeReviews; AE017355_GR; BT9727_4203. DR KEGG; btk:BT9727_4203; -. DR PATRIC; 18989513; VBIBacThu119411_4481. DR HOGENOM; HOG000261408; -. DR KO; K01338; -. DR OMA; KVCRKAA; -. DR ProtClustDB; CLSK873491; -. 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:0004252; F:serine-type endopeptidase activity; IEA:InterPro. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR GO; GO:0006950; P:response to stress; 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; IPR008268; Peptidase_S16_AS. 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. DR PROSITE; PS01046; LON_SER; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Cytoplasm; Hydrolase; KW Nucleotide-binding; Protease; Serine protease; Stress response. SQ SEQUENCE 776 AA; 86448 MW; EF7263D524E4E8AF CRC64; MSSMNTNERI VPLLPLRGVL VYPTMVLHLD VGRDKSIQAL EQAAMDENII FLAMQKEMNI DDPKEDDIYS VGTVAKVKQM LKLPNGTLRV LVEGLHRAEV VEFIEEENVV QVSIKTVTEE VEADVEEKAL MRTLLEHFEQ YIKVSKKVSN ETFATVADVE EPGRLADLIA SHLPIKTKQK QEILEIISVK ERLHTLISII QDEQELLSLE KKIGQKVKRS MERTQKEYFL REQMKAIQTE LGDKEGKGGE VEELREKIEQ SGMPEETMKA ALKELDRYEK LPASSAESGV IRNYMDWLLA LPWTDATEDM IDLAHSEEIL NKDHYGLEKV KERVLEYLAV QKLTNSLKGP ILCLVGPPGV GKTSLARSIA TSLNRNFVRV SLGGVRDESE IRGHRRTYVG AMPGRIIQGM KKAKSVNPVF LLDEIDKMSN DFRGDPSAAL LEVLDPEQNH NFSDHYIEEP YDLSKVMFVA TANTLSSIPG PLLDRMEIIS IAGYTELEKV HIAREHLLPK QLQEHGLRKG NLQVRDEALL EIIRYYTREA GVRTLERQIA KVCRKAAKII VTAERKRIVV TEKNVVDLLG KHIFRYGQAE KTDQVGMATG LAYTAAGGDT LAIEVSVAPG KGKLILTGKL GDVMKESAQA AFSYIRSRAE ELQIDPNFHE KNDIHIHVPE GAVPKDGPSA GITMATALIS ALTGIPVSKE VGMTGEITLR GRVLPIGGLK EKTLSAHRAG LTKIILPAEN EKDLDDIPES VKENLTFVLA SHLDEVLEHA LVGVKQ //