ID   LON_RICBR               Reviewed;         775 AA.
AC   Q1RID6;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   16-JUN-2009, entry version 27.
DE   RecName: Full=ATP-dependent protease La;
DE            EC=3.4.21.53;
GN   Name=lon; OrderedLocusNames=RBE_0797;
OS   Rickettsia bellii (strain RML369-C).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia.
OX   NCBI_TaxID=336407;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16703114; DOI=10.1371/journal.pgen.0020076;
RA   Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C.,
RA   Fournier P.-E., Claverie J.-M., Raoult D.;
RT   "Genome sequence of Rickettsia bellii illuminates the role of amoebae
RT   in gene exchanges between intracellular pathogens.";
RL   PLoS Genet. 2:733-744(2006).
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.
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DR   EMBL; CP000087; ABE04878.1; -; Genomic_DNA.
DR   RefSeq; YP_537967.1; -.
DR   MEROPS; S16.001; -.
DR   GeneID; 3995620; -.
DR   GenomeReviews; CP000087_GR; RBE_0797.
DR   KEGG; rbe:RBE_0797; -.
DR   HOGENOM; Q1RID6; -.
DR   OMA; Q1RID6; VMKESIQ.
DR   BioCyc; RBEL336407:RBE_0797-MON; -.
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    775       ATP-dependent protease La.
FT                                /FTId=PRO_0000280891.
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   775 AA;  86722 MW;  5F0AB73EE9EA39A8 CRC64;
     MNKKSLPLMA LRDIVVFPGV IAPVFVGRQK SLHALSNTTL SEEDNSKYIL VTLQKKFDQE
     NPNRNELYDV GILAKVIQIV KLPNTTAKIL VEAIARVKIS NIKGDEAFEA NYEIIPDEEI
     FDANNMRSLV DNAVQLFAKY AGSDKKINAE IIETINKEIS ETSNFINIIN ILASHLITSL
     EEKQRLLEET SPFKRISTII NILTSNIVNS ETEQALQQRV KKQIEKTQRD YYLHEQMKAI
     QKELDEDKSD LAEFDKKIKA AKLSKEAREK AEAELKKLRT MNQMSAESGV TRNYLETLLS
     LPWGKYDNSK IDINQAEKIL NRDHFGLEKV KERIIEYLAV LQRSSKIRGP ILCLIGPPGV
     GKTSLIKSIA EGMGRKYTKF ALGGVRDEAE IRGHRKTYLG SMPGKILTQL KKVKTSNPVM
     LLDEIDKMGS DFRGDPASAL LEVLDPEQNS HFVDHYLEVE YDLSNVIFIA TANSYNLPRA
     LIDRMEIIDI SGYMEEEKIQ IAKNYLVPKQ LKMHKIKKDE ITISDDAILD LIRYYTKESG
     VRSLEREIGA LTRKALKQIL ADKKVKHISV DSNNLEEFLG ARKYNFGLAE KNDQIGSTTG
     LAYTEVGGEL LTIEALSFPG KGEIKTTGKL GDVMKESAMA AYSCFRSRAA DFGLKYEDYK
     DFDVHIHVPA GAIPKDGPSA GCALFTTIVS LMTKIPVRRT VAMTGEVTLR GNVLPIGGLK
     EKLLAASRGG IKTVLIPEEN VKDLKDIPPN IKSSLEIIPV SNIDQVLEHA LTKKT
//