ID LON_BRUA2 STANDARD; PRT; 812 AA. AC Q2YPX3; O52605; Q57D31; DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot. DT 20-DEC-2005, sequence version 1. DT 07-MAR-2006, entry version 6. DE ATP-dependent protease La (EC 3.4.21.53). GN Name=lon; OrderedLocusNames=BAB1_1130; OS Brucella abortus (strain 2308). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Brucellaceae; Brucella. OX NCBI_TaxID=359391; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INDUCTION. RX PubMed=10672180; RA Robertson G.T., Kovach M.E., Allen C.A., Ficht T.A., Roop R.M. II; RT "The Brucella abortus Lon functions as a generalized stress response RT protease and is required for wild-type virulence in BALB/c mice."; RL Mol. Microbiol. 35:577-588(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16299333; DOI=10.1128/IAI.73.12.8353-8361.2005; RA Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A., RA Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.; RT "Whole-genome analyses of speciation events in pathogenic Brucellae."; RL Infect. Immun. 73:8353-8361(2005). CC -!- FUNCTION: Degrades short-lived regulatory and abnormal proteins in CC presence of ATP. Hydrolyzes two ATPs for each peptide bond cleaved CC in the protein substrate. Required for wild-type virulence during CC the initial stages of infection in the mouse model, but not CC essential for the establishment and maintenance of chronic CC infection in this host. CC -!- CATALYTIC ACTIVITY: Hydrolysis of proteins in presence of ATP. CC -!- SUBUNIT: Homotetramer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- INDUCTION: By stress conditions (acid shock, heat shock, ethanol CC and puromycin). CC -!- SIMILARITY: Belongs to the peptidase S16 family. CC -!- SIMILARITY: Contains 1 Lon domain. 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; AF042348; AAB97420.1; -; Genomic_DNA. DR EMBL; AM040264; CAJ11086.1; -; Genomic_DNA. DR MEROPS; S16.001; -. DR GenomeReviews; AM040264_GR; BAB1_1130. DR PROSITE; PS01046; LON_SER; 1. KW ATP-binding; Complete proteome; Heat shock; Hydrolase; KW Nucleotide-binding; Protease; Serine protease. FT CHAIN 1 812 ATP-dependent protease La. FT /FTId=PRO_0000076122. FT DOMAIN 23 213 Lon. FT NP_BIND 367 374 ATP (Potential). FT ACT_SITE 689 689 By similarity. FT ACT_SITE 732 732 By similarity. FT CONFLICT 227 227 R -> P (in Ref. 1). SQ SEQUENCE 812 AA; 89919 MW; DB30B60818FF6AAE CRC64; MTGIEQKTPV GGSETGGADG LYAVLPLRDI VVFPHMIVPL FVGREKSIRA LEEVMGVDKQ ILLATQKNAA DDDPAPDAIY EIGTIANVLQ LLKLPDGTVK VLVEGTARAK ISKFTDREDY HEAYAAALQE PEEDAVEIEA LARSVVPDFE NYVKLNKKIS PEVVGAASQI DDYSKLADTV ASHLAIKIPE KQEMLSVLSV RERLEKALSF MEAEISVLQV EKRIRSRVKR QMEKTQREYY LNEQMKAIQK ELGDSEDGRD EVAEIEERIT KTKLSKEARE KALAELKKLR SMSPMSAEAT VVRNYLDWLL SIPWGKKSKV KQDLNFAQEV LDAEHFGLGK VKERIVEYLA VQARSTKIKG PILCLVGPPG VGKTSLARSI AKATGREYVR MSLGGVRDEA EIRGHRRTYI GSMPGKVIQS MKKAKKSNPL FLLDEIDKMG QDFRGDPSSA MLEVLDPEQN ATFMDHYLEV EYDLSNVMFV TTANTMNIPV PLLDRMEIIR IAGYTEDEKL EIAKRHLLPK AIKDHALQPK EFSVTEDALR NVIRHYTREA GVRSLEREVM TLARKAVTEI LKTKKKSVKI TDKNLSDYLG VEKFRFGQID GEDQVGVVTG LAWTEVGGEL LTIEGVMMPG KGRMTVTGNL RDVMKESISA AASYVRSRAI DFGIEPPLFD KRDIHVHVPE GATPKDGPSA GIAMVTAIVS VLTGIPVRKD IAMTGEVTLR GRVLPIGGLK EKLLATLRGG IKKVLIPEEN AKDLAEIPDN VKNNLEIVPV SRVGEVLKHA LVRQPEPIEW TEQENPTAVP PVEDEAGASL AH //