ID LON_RICFE Reviewed; 778 AA. AC Q4ULN0; DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2005, sequence version 1. DT 16-JUN-2009, entry version 33. DE RecName: Full=ATP-dependent protease La; DE EC=3.4.21.53; GN Name=lon; OrderedLocusNames=RF_0692; OS Rickettsia felis (Rickettsia azadi). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales; OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group. OX NCBI_TaxID=42862; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC VR-1525 / URRWXCal2; RX PubMed=15984913; DOI=10.1371/journal.pbio.0030248; RA Ogata H., Renesto P., Audic S., Robert C., Blanc G., Fournier P.-E., RA Parinello H., Claverie J.-M., Raoult D.; RT "The genome sequence of Rickettsia felis identifies the first putative RT conjugative plasmid in an obligate intracellular parasite."; RL PLoS Biol. 3:1-12(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 (By similarity). CC -!- CATALYTIC ACTIVITY: Hydrolysis of proteins in presence of ATP. CC -!- SUBUNIT: Homotetramer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the peptidase S16 family. CC -!- SIMILARITY: Contains 1 Lon domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000053; AAY61543.1; -; Genomic_DNA. DR RefSeq; YP_246708.1; -. DR MEROPS; S16.001; -. DR GeneID; 3400757; -. DR GenomeReviews; CP000053_GR; RF_0692. DR KEGG; rfe:RF_0692; -. DR NMPDR; fig|315456.3.peg.692; -. DR HOGENOM; Q4ULN0; -. DR OMA; Q4ULN0; VMKESIQ. DR BioCyc; RFEL315456:RF_0692-MON; -. DR BRENDA; 3.4.21.53; 297363. 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:InterPro. 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; IPR001984; Peptidase_S16_C. 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. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Cytoplasm; Hydrolase; KW Nucleotide-binding; Protease; Serine protease. FT CHAIN 1 778 ATP-dependent protease La. FT /FTId=PRO_0000280893. FT DOMAIN 5 205 Lon. FT NP_BIND 356 363 ATP (Potential). FT ACT_SITE 679 679 By similarity. FT ACT_SITE 722 722 By similarity. SQ SEQUENCE 778 AA; 87027 MW; E0855BF70147205A CRC64; MNKKSLPLMA LRDMVVFPGV IAPIFVGRQK SLQALSHTTV SEEDNSKYIL VTLQKKFDQE NPSKHELNNT AILAKIIQIV KLPNNTAKIL IEAVARVKLS NIKGNDAFEA NYEIIPDEEI FDVNNMRSLV DNAVQLFSKY AINDKKVNAE IIETINKEIS NSTNFINIIN ILASHLITSL EAKQHLLEET SPFKRITTVI STLTSNIVNS ETEQALQQRV RKQIEKTQRD YYLHEQMKAI QKELDEDKSE LADIEKKIKS LKLSKEAKEK AESELKKLRS MNQMSAESGV TRNYLETLLS LPWGKYDNSK IDINQAEKIL NRDHFGLEKV KERIIEYLAV LQRSSKIRGP ILCLIGPPGV GKTSLVKSIA EGMGRKYTKF ALGGVRDEAE IRGHRKTYLG STPGKILGQL KKVKTSNPVM LLDEIDKMSS DFRGDPASAL LEVLDPEQNS HFVDHYLEVE YDLSNVIFIA TANSHDLPRA LSDRMEKIYI SGYVEEEKLQ IAKNYLVPKQ FKMHKIKKDE ITISETAILD LIRYYTKESG VRALEREIGA LTRKALKQIL ADKTVKHIAI DSSNLEEFLE AKKYNFGLAE KEDQIGSTTG LAYTEVGGEL LTIEALAFPG KGEIKTTGKL GDVMKESAMA AYSCFRSRAT NFGLKYDNYK DFDIHIHVPA GAIPKDGPSA GCALFTTIVS LMTKIPVHRT VAMTGEITLR GNVLPIGGLK EKLLAASRGG IKTVLIPEEN VKDLKDIPPN IKESLEIISV SNIDQVLKHA LVETPINK //