ID LON_CHLPN Reviewed; 819 AA. AC Q9Z9F4; Q9JQ69; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 16-JUN-2009, entry version 68. DE RecName: Full=ATP-dependent protease La; DE EC=3.4.21.53; GN Name=lon; OrderedLocusNames=CPn_0027, CP_0749, CpB0031; OS Chlamydia pneumoniae (Chlamydophila pneumoniae). OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae; Chlamydophila. OX NCBI_TaxID=83558; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CWL029; RX MEDLINE=99206606; PubMed=10192388; DOI=10.1038/7716; RA Kalman S., Mitchell W.P., Marathe R., Lammel C.J., Fan J., Hyman R.W., RA Olinger L., Grimwood J., Davis R.W., Stephens R.S.; RT "Comparative genomes of Chlamydia pneumoniae and C. trachomatis."; RL Nat. Genet. 21:385-389(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AR39; RX MEDLINE=20150255; PubMed=10684935; DOI=10.1093/nar/28.6.1397; RA Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., RA White O., Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., RA Bass S., Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., RA Dodson R.J., Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., RA McClarty G., Salzberg S.L., Eisen J.A., Fraser C.M.; RT "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia RT pneumoniae AR39."; RL Nucleic Acids Res. 28:1397-1406(2000). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=J138; RX MEDLINE=20330349; PubMed=10871362; DOI=10.1093/nar/28.12.2311; RA Shirai M., Hirakawa H., Kimoto M., Tabuchi M., Kishi F., Ouchi K., RA Shiba T., Ishii K., Hattori M., Kuhara S., Nakazawa T.; RT "Comparison of whole genome sequences of Chlamydia pneumoniae J138 RT from Japan and CWL029 from USA."; RL Nucleic Acids Res. 28:2311-2314(2000). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TW-183; RA Geng M.M., Schuhmacher A., Muehldorfer I., Bensch K.W., Schaefer K.P., RA Schneider S., Pohl T., Essig A., Marre R., Melchers K.; RT "The genome sequence of Chlamydia pneumoniae TW183 and comparison with RT other Chlamydia strains based on whole genome sequence analysis."; RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases. 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; AE001363; AAD18180.1; -; Genomic_DNA. DR EMBL; AE002161; AAF38554.1; -; Genomic_DNA. DR EMBL; BA000008; BAA98239.1; -; Genomic_DNA. DR EMBL; AE017157; AAP97964.1; -; Genomic_DNA. DR PIR; B72128; B72128. DR PIR; E86494; E86494. DR RefSeq; NP_224235.1; -. DR RefSeq; NP_300088.1; -. DR RefSeq; NP_445291.1; -. DR RefSeq; NP_876307.1; -. DR MEROPS; S16.002; -. DR GeneID; 1466714; -. DR GeneID; 894928; -. DR GeneID; 918819; -. DR GeneID; 963156; -. DR GenomeReviews; AE001363_GR; CPn_0027. DR GenomeReviews; AE002161_GR; CP_0749. DR GenomeReviews; AE009440_GR; CpB0031. DR GenomeReviews; BA000008_GR; lon. DR KEGG; cpa:CP0749; -. DR KEGG; cpn:CPn0027; -. DR KEGG; cpt:CpB0031; -. DR TIGR; CP_0749; -. DR HOGENOM; Q9Z9F4; -. DR OMA; Q9Z9F4; WGNYSDE. DR BioCyc; CPNE115711:CP_0749-MON; -. DR BioCyc; CPNE115713:CPN0027-MON; -. DR BioCyc; CPNE138677:CPJ0027-MON; -. DR BioCyc; CPNE182082:CPB0031-MON; -. DR BRENDA; 3.4.21.53; 264832. 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 1 819 ATP-dependent protease La. FT /FTId=PRO_0000076131. FT DOMAIN 42 238 Lon. FT NP_BIND 393 400 ATP (Potential). FT ACT_SITE 723 723 By similarity. FT ACT_SITE 766 766 By similarity. SQ SEQUENCE 819 AA; 92276 MW; 788BCB2A0D294E6A CRC64; MDSTTNSDSP ILDPNPEDVE KLLDESEEES EDQSTERLLP SELFILPLNK RPFFPGMAAP ILIESGPYYE VLKVLAKSSQ KYIGLVLTKK ENADILKVSF NQLHKTGVAA RILRIMPIEG GSAQVLLSIE ERIRIIEPIK DKYLKARVSY HADNKELTEE LKAYSISIVS VIKDLLKLNP LFKEELQIFL GHSDFTEPGK LADFSVALTT ATREELQEVL ETTNMHDRID KALILLKKEL DLSRLQSSIN QKIEATITKS QKEFFLKEQL KTIKKELGLE KEDRAIDIEK FSERLRKRHV PDYAMEVIQD EIEKLQTLET SSAEYTVCRN YLDWLTIIPW GIQSKEYHDL KKAEIVLNKD HYGLDEIKQR ILELISVGKL SKGLKGSIIC LVGPPGVGKT SIGRSIAKVL HRKFFRFSVG GMRDEAEIKG HRRTYIGAMP GKMVQALKQS QAMNPVIMID EVDKIGASYH GDPASALLEV LDPEQNKDFL DHYLDVRVDL SNVLFILTAN VLDTIPDPLL DRMEILRLSG YILEEKLQIA KKYLVPKARK EIGLTASEVN FQPEALKYMI NNYAREAGVR TLNGNIKKVL RKVALKIVQN QEKPKSKKIT FKISSKNLQT YLGKPIFSSD RFYESTPVGV ATGLAWTSLG GATLYIESVQ VSSLKTDMHL TGQAGEVMKE SSQIAWTYLH SALHRYAPGY TFFPKSQVHI HIPEGATPKD GPSAGITMVT SLLSLLLETP VVNNLGMTGE ITLTGRVLGV GGIREKLIAA RRSRLNILIF PEDNRRDYEE LPAYLKTGLK IHFVSHYDDV LKVAFPKLK //