ID Q6HD56_BACHK Unreviewed; 776 AA. AC Q6HD56; DT 19-JUL-2004, integrated into UniProtKB/TrEMBL. DT 19-JUL-2004, sequence version 1. DT 19-JAN-2022, entry version 144. 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 ORFNames=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|EMBL:AAT60850.1, ECO:0000313|Proteomes:UP000001301} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=97-27 {ECO:0000313|EMBL:AAT60850.1, RC 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., Brown N., RA Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C., RA Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A., RA Green L.D., 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., Okinaka R.T., RA Parson-Quintana B., Reilly L.P., Richardson P., Robinson D.L., Rubin E., RA Saunders E., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., RA Ticknor L.O., Wills P.L., 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 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, ECO:0000256|RuleBase:RU000591}. 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 MEROPS; S16.001; -. DR EnsemblBacteria; AAT60850; AAT60850; BT9727_4203. DR KEGG; btk:BT9727_4203; -. DR PATRIC; fig|281309.8.peg.4481; -. DR HOGENOM; CLU_004109_4_3_9; -. DR OMA; GAWQVVD; -. DR BioCyc; BTHU281309:G1G14-4275-MONOMER; -. DR Proteomes; UP000001301; Chromosome. 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 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; IPR008269; Lon_proteolytic. DR InterPro; IPR027065; Lon_Prtase. DR InterPro; IPR003111; Lon_substr-bd. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR008268; Peptidase_S16_AS. 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. DR PROSITE; PS01046; LON_SER; 1. PE 2: Evidence at transcript level; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_01973}; 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|HAMAP-Rule:MF_01973, KW ECO:0000256|PIRNR:PIRNR001174}; KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|HAMAP-Rule:MF_01973}; 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 11..202 FT /note="Lon N-terminal" FT /evidence="ECO:0000259|PROSITE:PS51787" FT DOMAIN 592..773 FT /note="Lon proteolytic" FT /evidence="ECO:0000259|PROSITE:PS51786" FT NP_BIND 356..363 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01973, FT ECO:0000256|PIRSR:PIRSR001174-2" FT ACT_SITE 679 FT /evidence="ECO:0000256|HAMAP-Rule:MF_01973, FT ECO:0000256|PIRSR:PIRSR001174-1" FT ACT_SITE 722 FT /evidence="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 //