ID Q6HD56_BACHK Unreviewed; 776 AA. AC Q6HD56; DT 19-JUL-2004, integrated into UniProtKB/TrEMBL. DT 19-JUL-2004, sequence version 1. DT 29-OCT-2014, entry version 98. 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=lonA {ECO:0000313|EMBL:AAT60850.1}; GN Synonyms=lon {ECO:0000256|HAMAP-Rule:MF_01973}; GN OrderedLocusNames=BT9727_4203 {ECO:0000313|EMBL:AAT60850.1}; OS Bacillus thuringiensis subsp. konkukian (strain 97-27). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=281309 {ECO:0000313|EMBL:AAT60850.1, ECO:0000313|Proteomes:UP000001301}; RN [1] {ECO:0000313|Proteomes:UP000001301} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=97-27 {ECO:0000313|Proteomes:UP000001301}; 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 -!- 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|PIRNR:PIRNR001174, CC ECO:0000256|SAAS:SAAS00004348}. 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|HAMAP-Rule:MF_01973, CC ECO:0000256|PIRNR:PIRNR001174, ECO:0000256|SAAS:SAAS00004358}. 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|PIRNR:PIRNR001174, CC ECO:0000256|RuleBase:RU000591}. CC -!- SIMILARITY: Contains 1 Lon domain. {ECO:0000256|HAMAP- CC Rule:MF_01973}. CC -!- SIMILARITY: Contains Lon domain. {ECO:0000256|SAAS:SAAS00004345}. 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; WP_000097310.1; NC_005957.1. DR RefSeq; YP_038520.1; NC_005957.1. DR ProteinModelPortal; Q6HD56; -. DR SMR; Q6HD56; 492-586, 594-773. DR STRING; 281309.BT9727_4203; -. DR MEROPS; S16.004; -. DR EnsemblBacteria; AAT60850; AAT60850; BT9727_4203. DR GeneID; 2855702; -. DR KEGG; btk:BT9727_4203; -. DR PATRIC; 18989513; VBIBacThu119411_4481. DR HOGENOM; HOG000261408; -. DR KO; K01338; -. DR OMA; KVCRKAA; -. DR OrthoDB; EOG6XHC23; -. DR BioCyc; BTHU281309:GJID-4275-MONOMER; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0033554; P:cellular response to stress; IEA:UniProtKB-HAMAP. DR GO; GO:0006515; P:misfolded or incompletely synthesized protein catabolic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.230.10; -; 1. DR Gene3D; 3.40.50.300; -; 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; IPR027065; Lon_Prtase. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR008269; Pept_S16_C. 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 InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr. DR PANTHER; PTHR10046; PTHR10046; 1. 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; SSF52540; SSF52540; 1. DR SUPFAM; SSF54211; SSF54211; 1. DR SUPFAM; SSF88697; SSF88697; 1. DR TIGRFAMs; TIGR00763; lon; 1. DR PROSITE; PS01046; LON_SER; 1. PE 2: Evidence at transcript level; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01973, KW ECO:0000256|PIRNR:PIRNR001174}; KW Complete proteome {ECO:0000313|Proteomes:UP000001301}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01973, KW ECO:0000256|PIRNR:PIRNR001174}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01973, KW ECO:0000256|PIRNR:PIRNR001174}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01973, KW ECO:0000256|PIRNR:PIRNR001174}; KW Protease {ECO:0000256|HAMAP-Rule:MF_01973, KW ECO:0000256|PIRNR:PIRNR001174}; KW Serine protease {ECO:0000256|HAMAP-Rule:MF_01973, KW ECO:0000256|PIRNR:PIRNR001174}; KW Stress response {ECO:0000256|HAMAP-Rule:MF_01973, KW ECO:0000256|SAAS:SAAS00004281}. FT DOMAIN 11 201 Lon. {ECO:0000256|HAMAP-Rule:MF_01973}. FT NP_BIND 356 363 ATP. {ECO:0000256|HAMAP-Rule:MF_01973, FT ECO:0000256|PIRSR:PIRSR001174-2}. FT ACT_SITE 679 679 {ECO:0000256|HAMAP-Rule:MF_01973, FT ECO:0000256|PIRSR:PIRSR001174-1}. FT ACT_SITE 722 722 {ECO:0000256|HAMAP-Rule:MF_01973, FT ECO:0000256|PIRSR:PIRSR001174-1}. 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 //