ID LON_BRUA2 Reviewed; 812 AA. AC Q2YPX3; O52605; Q57D31; DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot. DT 20-DEC-2005, sequence version 1. DT 16-NOV-2011, entry version 44. DE RecName: Full=Lon protease; DE EC=3.4.21.53; DE AltName: Full=ATP-dependent protease La; 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; DOI=10.1046/j.1365-2958.2000.01726.x; 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]. RC STRAIN=2308; 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: 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 (By CC similarity). Required for wild-type virulence during the initial CC stages of infection in the mouse model, but not essential for the CC establishment and maintenance of chronic infection in this host. 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 -!- 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 RefSeq; YP_414523.1; NC_007618.1. DR ProteinModelPortal; Q2YPX3; -. DR SMR; Q2YPX3; 502-596, 604-789. DR STRING; Q2YPX3; -. DR GeneID; 3787778; -. DR GenomeReviews; AM040264_GR; BAB1_1130. DR KEGG; bmf:BAB1_1130; -. DR eggNOG; COG0466; -. DR HOGENOM; HBG566281; -. DR OMA; FMEGEIS; -. DR ProtClustDB; CLSK864999; -. DR BioCyc; BMEL359391:BAB1_1130-MONOMER; -. 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; ATPase_AAA+_core. 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 KO; K01338; -. DR Pfam; PF00004; AAA; 1. DR Pfam; PF02190; LON; 1. DR Pfam; PF05362; Lon_C; 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 2: Evidence at transcript level; KW ATP-binding; Complete proteome; Cytoplasm; Hydrolase; KW Nucleotide-binding; Protease; Serine protease; Stress response. FT CHAIN 1 812 Lon protease. FT /FTId=PRO_0000076122. FT DOMAIN 24 212 Lon. FT NP_BIND 367 374 ATP (By similarity). FT ACT_SITE 689 689 By similarity. FT ACT_SITE 732 732 By similarity. FT CONFLICT 227 227 R -> P (in Ref. 1; AAB97420). 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 //