ID Q6HD56_BACHK PRELIMINARY; PRT; 776 AA. AC Q6HD56; DT 25-OCT-2004 (TrEMBLrel. 28, Created) DT 25-OCT-2004 (TrEMBLrel. 28, Last sequence update) DT 25-OCT-2004 (TrEMBLrel. 28, Last annotation update) DE Endopeptidase La (ATP-dependent protease La 1) (EC DE 3.4.21.53). GN Name=lonA; OrderedLocusNames=BT9727_4203; OS Bacillus thuringiensis (subsp. konkukian). OC Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=180856; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=97-27; RA Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., RA Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., RA Richardson P., Rubin E., Tice H.; RT "Complete genome sequence of Bacillus thuringiensis 97-27."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: Hydrolysis of large proteins such as globin, CC casein and denaturated serum albumin, in presence of ATP. CC -!- SUBCELLULAR LOCATION: Cytoplasmic (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; -. DR GO; GO:0005524; F:ATP binding; IEA. DR GO; GO:0004176; F:ATP-dependent peptidase activity; IEA. DR GO; GO:0017111; F:nucleoside-triphosphatase activity; IEA. DR GO; GO:0000166; F:nucleotide binding; IEA. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA. DR GO; GO:0006510; P:ATP-dependent proteolysis; IEA. DR InterPro; IPR003593; AAA_ATPase. DR InterPro; IPR003959; AAA_ATPase_centr. DR InterPro; IPR001984; Peptidase_S16. DR InterPro; IPR008268; Peptid_S16_AS. DR InterPro; IPR008269; Pept_S16_C. DR InterPro; IPR004815; Pept_S16_lon. DR InterPro; IPR003111; Pept_S16_N. DR Pfam; PF00004; AAA; 1. DR Pfam; PF02190; LON; 1. DR Pfam; PF05362; Lon_C; 1. DR PRINTS; PR00830; ENDOLAPTASE. DR SMART; SM00382; AAA; 1. DR SMART; SM00464; LON; 1. DR TIGRFAMs; TIGR00763; lon; 1. DR PROSITE; PS01046; LON_SER; 1. KW ATP-binding; Complete proteome; Hydrolase; Protease; Serine protease. SQ SEQUENCE 776 AA; 86447 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 //