ID   LON_BUCAP               Reviewed;         777 AA.
AC   Q8K988;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   16-JUN-2009, entry version 53.
DE   RecName: Full=ATP-dependent protease La;
DE            EC=3.4.21.53;
GN   Name=lon; OrderedLocusNames=BUsg_461;
OS   Buchnera aphidicola subsp. Schizaphis graminum.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Buchnera.
OX   NCBI_TaxID=98794;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=22084549; PubMed=12089438; DOI=10.1126/science.1071278;
RA   Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA   Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT   "50 million years of genomic stasis in endosymbiotic bacteria.";
RL   Science 296:2376-2379(2002).
CC   -!- FUNCTION: Degrades short-lived regulatory and abnormal proteins in
CC       presence of ATP. Degrades the regulatory proteins rcsA and sulA.
CC       Hydrolyzes two ATPs for each peptide bond cleaved in the protein
CC       substrate (By similarity).
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of proteins in presence of ATP.
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the peptidase S16 family.
CC   -!- SIMILARITY: Contains 1 Lon domain.
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DR   EMBL; AE013218; AAM68004.1; -; Genomic_DNA.
DR   RefSeq; NP_660793.1; -.
DR   SMR; Q8K988; 8-117, 491-584, 594-775.
DR   MEROPS; S16.001; -.
DR   GeneID; 1005704; -.
DR   GenomeReviews; AE013218_GR; BUsg_461.
DR   KEGG; bas:BUsg461; -.
DR   HOGENOM; Q8K988; -.
DR   OMA; Q8K988; VMKESIQ.
DR   BioCyc; BAPH198804:BUSG461-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    777       ATP-dependent protease La.
FT                                /FTId=PRO_0000076126.
FT   DOMAIN       10    202       Lon.
FT   NP_BIND     356    363       ATP (Potential).
FT   ACT_SITE    679    679       By similarity.
FT   ACT_SITE    722    722       By similarity.
SQ   SEQUENCE   777 AA;  87755 MW;  768ACD8B06713DD2 CRC64;
     MNSERSERIK IPVLPLRDVV VYPHMVIPLF VGRKKSIHCI ETSMNNDKKI MLIAQKEASK
     DEPSTNDLFN IGTISSILQM LKLPDGTVKV LVEGLQRACI KNIESNGEHL VAEVELIISP
     TVIDKEQEVL IRTTVNQFES YIKLNKKIPS EILNTLSQTK NAEKLADTIA AHMPLKLADK
     QSVLEIYNVN ERLEFLMAIM ETEIDLLKVE KRIRNRVKKQ MEKSQREYYL NEQIKAIQKE
     LGDMDEIPDE NKILKRKIKS LKMPKEAKEK TESELQKLKM MSPMSAEATV VRSYIDWMIQ
     VPWNIKTKIK KDIQEAKKIL DIDHFGLEKV KERILEYLAV QSRTNKVKGP ILCLIGPPGV
     GKTSLGKSIA KSTGRKYVRM ALGGIRDEAE IRGHRRTYIG SMPGKLMQKM VKAKVKNPLF
     LLDEIDKMSC DIRVDPASAL LEVLDPEQNI NFNDHYLEVD YDLSDVMFVA TSNSMNIPAP
     LLDRMEIIRL SGYTENEKLN IAKCYLYPKQ MERNALKRNE LIITDCAIIS IIQYYTREAG
     VRSLEREISK ICRKVVKLLI LNKSLKKIEI NSKNLKKFLG IKRFDYGKTN NLNQIGQVVG
     LAWTEVGGEL LTIETACVSG KGKLTYTGSL GEVMQESIQA ALTVVRSQAK KLGIKKDFHE
     KHDIHVHVPE GATPKDGPSA GIAMCTAIVS SLTKNPVKSN IAMTGEITLQ GRVLTIGGLK
     EKLLAAHRGG VKTVLIPYEN KRNLEEIPKN IIEGLTIYPV KNIEEVLKIA LENTPYV
//