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 03-MAY-2023, entry version 100. DE RecName: Full=Lon protease {ECO:0000255|HAMAP-Rule:MF_01973}; DE EC=3.4.21.53 {ECO:0000255|HAMAP-Rule:MF_01973}; DE AltName: Full=ATP-dependent protease La {ECO:0000255|HAMAP-Rule:MF_01973}; GN Name=lon {ECO:0000255|HAMAP-Rule:MF_01973}; OrderedLocusNames=BAB1_1130; OS Brucella abortus (strain 2308). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Brucellaceae; Brucella/Ochrobactrum group; 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 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 (By similarity). Required for wild-type virulence CC during the initial stages of infection in the mouse model, but not CC essential for the establishment and maintenance of chronic infection in CC this host. {ECO:0000255|HAMAP-Rule:MF_01973, CC ECO:0000269|PubMed:10672180}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Hydrolysis of proteins in presence of ATP.; EC=3.4.21.53; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01973}; CC -!- SUBUNIT: Homohexamer. Organized in a ring with a central cavity. CC {ECO:0000255|HAMAP-Rule:MF_01973}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01973}. CC -!- INDUCTION: By stress conditions (acid shock, heat shock, ethanol and CC puromycin). {ECO:0000269|PubMed:10672180}. CC -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000255|HAMAP- CC Rule:MF_01973}. 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; WP_002966840.1; NZ_KN046823.1. DR AlphaFoldDB; Q2YPX3; -. DR SMR; Q2YPX3; -. DR STRING; 359391.BAB1_1130; -. DR MEROPS; S16.001; -. DR EnsemblBacteria; CAJ11086; CAJ11086; BAB1_1130. DR GeneID; 3787778; -. DR KEGG; bmf:BAB1_1130; -. DR PATRIC; fig|359391.11.peg.30; -. DR HOGENOM; CLU_004109_4_3_5; -. DR OMA; GAWQVVD; -. DR PhylomeDB; Q2YPX3; -. DR PHI-base; PHI:8922; -. DR Proteomes; UP000002719; Chromosome I. 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 CDD; cd19500; RecA-like_Lon; 1. DR Gene3D; 1.10.8.60; -; 1. DR Gene3D; 1.20.5.5270; -; 1. DR Gene3D; 1.20.58.1480; -; 1. DR Gene3D; 3.30.230.10; -; 1. DR Gene3D; 2.30.130.40; LON domain-like; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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_prtase_N. DR InterPro; IPR046336; Lon_prtase_N_sf. 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; ATP DEPENDENT LON PROTEASE FAMILY MEMBER; 1. DR PANTHER; PTHR10046:SF56; LON PROTEASE; 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 PRINTS; PR00830; ENDOLAPTASE. DR SMART; SM00382; AAA; 1. DR SMART; SM00464; LON; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR SUPFAM; SSF88697; PUA domain-like; 1. DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 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; Cytoplasm; Hydrolase; Nucleotide-binding; Protease; KW Reference proteome; Serine protease; Stress response. FT CHAIN 1..812 FT /note="Lon protease" FT /id="PRO_0000076122" FT DOMAIN 22..213 FT /note="Lon N-terminal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123" FT DOMAIN 602..783 FT /note="Lon proteolytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122" FT REGION 787..812 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 689 FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973" FT ACT_SITE 732 FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973" FT BINDING 367..374 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973" FT CONFLICT 227 FT /note="R -> P (in Ref. 1; AAB97420)" FT /evidence="ECO:0000305" 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 //