ID   LON_AZOBR      STANDARD;      PRT;   810 AA.
AC   P77810;
DT   15-DEC-1998 (Rel. 37, Created)
DT   15-DEC-1998 (Rel. 37, Last sequence update)
DT   01-FEB-2005 (Rel. 46, Last annotation update)
DE   ATP-dependent protease La (EC 3.4.21.53).
GN   Name=lon;
OS   Azospirillum brasilense.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Azospirillum.
OX   NCBI_TaxID=192;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=SpF94;
RX   MEDLINE=96256595; PubMed=8655539;
RA   Mori E., Fulchieri M., Indorato C., Fani R., Bazzicalupo M.;
RT   "Cloning, nucleotide sequencing, and expression of the Azospirillum
RT   brasilense lon gene: involvement in iron uptake.";
RL   J. Bacteriol. 178:3440-3446(1996).
CC   -!- FUNCTION: Degrades short-lived regulatory and abnormal proteins in
CC       the presence of ATP. Hydrolyzes two ATP for each peptide bond
CC       cleaved in the protein substrate (By similarity). Involved in iron
CC       uptake.
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of proteins in presence of ATP.
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic.
CC   -!- SIMILARITY: Belongs to the peptidase S16 family.
CC   --------------------------------------------------------------------------
CC   This Swiss-Prot entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use as long as its content is in no way modified and this statement is not
CC   removed.
CC   --------------------------------------------------------------------------
DR   EMBL; U35611; AAB16819.1; -.
DR   PIR; JC6045; JC6045.
DR   MEROPS; S16.001; -.
DR   InterPro; IPR003593; AAA_ATPase.
DR   InterPro; IPR003959; AAA_ATPase_centr.
DR   InterPro; IPR008269; Pept_S16_C.
DR   InterPro; IPR004815; Pept_S16_lon.
DR   InterPro; IPR003111; Pept_S16_N.
DR   InterPro; IPR008268; Peptid_S16_AS.
DR   InterPro; IPR001984; Peptidase_S16.
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.
KW   ATP-binding; Hydrolase; Serine protease.
FT   NP_BIND     361    368       ATP (Potential).
FT   ACT_SITE    685    685       By similarity.
SQ   SEQUENCE   810 AA;  90143 MW;  2833882C69886C4B CRC64;
     MKEAQSMFEI PRGALYPVPP LRDIVVFPHM IVPLFVGREK SVRALEDVMK DDKQILLVTQ
     KNAAQDDPTP ADIYSVGTVG TVLQLLKLPD GTVKVLVEGG QRASITKFAE NEDFFQAHAD
     LVEEKVGESQ ELEALGRAVV SQFEQYIKLN KKIPPEVLVS INQIEEPGKL ADTVASHLAL
     KIPEKQQLLE CATVSERLER VYAFMEGEIG VLQVEKRIRN RVKRQMEKTQ REYYLNEQLK
     AIQKELGETE DGRDESAELE EKINKTRFSK EARDKALAEL KKLRSMSPMS AEATVVRNYL
     DWMLSIPWKK RTKVKKDLKL AQKILDADHY GLEKVKERIL EYLRVQNRMN KVKGPIQSLV
     GPPGVGKTSL GKSIAKSTGR NFVRMSLGGV RDEAEVRGHR RTYIGSMPGK VIQGMKKAKS
     SNPLFLLDEI DKLGADWRGD PSSALLEVLD PEQNGTFNDH YLEVDYDLSD VMFVCTANTM
     RMPQPLLDRM EIIRVAGYTE DEKVEISKRH LIEKQVEANG LKKGEFAISD DALRDLIRYY
     TREAGVRSLE REIANLCRKA VKEILMKGSA GAKVSVTRRN LDKYAGVRRF HFGEAELEDL
     VGVTTGLAWT EVGGELLSIE AVSLPGKGRV TTTGKLGDVM KESVQAAESY VKSRATAFGI
     KPTLFEKRDI HVHVPEGATP KDGPSAGVAM ITSIVSVLTG IAVRKDVAMT GEITLRGRVL
     PIGGLKEKLL AALRGGLKHV LIPKDNEKDL AEIPDNVKRG LEIIPVSTVD DVLKHALVRE
     VEPIEWKEPE AVEPAVAKPQ TDGGGEVLRH
//