LON_AZOBR
ID LON_AZOBR Reviewed; 810 AA.
AC P77810;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Lon protease {ECO:0000255|HAMAP-Rule:MF_01973};
DE EC=3.4.21.53 {ECO:0000255|HAMAP-Rule:MF_01973};
DE AltName: Full=ATP-dependent protease La {ECO:0000255|HAMAP-Rule:MF_01973};
GN Name=lon {ECO:0000255|HAMAP-Rule:MF_01973};
OS Azospirillum brasilense.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Azospirillum.
OX NCBI_TaxID=192;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC STRAIN=SpF94;
RX PubMed=8655539; DOI=10.1128/jb.178.12.3440-3446.1996;
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: ATP-dependent serine protease that mediates the selective
CC degradation of mutant and abnormal proteins as well as certain short-
CC lived regulatory proteins. Required for cellular homeostasis and for
CC survival from DNA damage and developmental changes induced by stress.
CC Degrades polypeptides processively to yield small peptide fragments
CC that are 5 to 10 amino acids long. Binds to DNA in a double-stranded,
CC site-specific manner (By similarity). Involved in iron uptake.
CC {ECO:0000255|HAMAP-Rule:MF_01973}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins in presence of ATP.; EC=3.4.21.53;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01973};
CC -!- SUBUNIT: Homohexamer. Organized in a ring with a central cavity.
CC {ECO:0000255|HAMAP-Rule:MF_01973}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- INDUCTION: By heat shock. {ECO:0000255|HAMAP-Rule:MF_01973,
CC ECO:0000269|PubMed:8655539}.
CC -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000255|HAMAP-
CC Rule:MF_01973}.
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DR EMBL; U35611; AAB16819.1; -; Genomic_DNA.
DR PIR; JC6045; JC6045.
DR AlphaFoldDB; P77810; -.
DR SMR; P77810; -.
DR MEROPS; S16.001; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0034605; P:cellular response to heat; IEA:UniProtKB-UniRule.
DR GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IEA:UniProtKB-UniRule.
DR Gene3D; 2.30.130.40; -; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_01973; lon_bact; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR027543; Lon_bac.
DR InterPro; IPR004815; Lon_bac/euk-typ.
DR InterPro; IPR008269; Lon_proteolytic.
DR InterPro; IPR027065; Lon_Prtase.
DR InterPro; IPR003111; Lon_prtase_N.
DR InterPro; IPR046336; Lon_prtase_N_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR008268; Peptidase_S16_AS.
DR InterPro; IPR015947; PUA-like_sf.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR PANTHER; PTHR10046; PTHR10046; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF05362; Lon_C; 1.
DR Pfam; PF02190; LON_substr_bdg; 1.
DR PIRSF; PIRSF001174; Lon_proteas; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00464; LON; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF88697; SSF88697; 1.
DR TIGRFAMs; TIGR00763; lon; 1.
DR PROSITE; PS51787; LON_N; 1.
DR PROSITE; PS51786; LON_PROTEOLYTIC; 1.
DR PROSITE; PS01046; LON_SER; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cytoplasm; Hydrolase; Nucleotide-binding; Protease;
KW Serine protease; Stress response.
FT CHAIN 1..810
FT /note="Lon protease"
FT /id="PRO_0000076115"
FT DOMAIN 16..207
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 598..779
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT ACT_SITE 685
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT ACT_SITE 728
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT BINDING 361..368
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
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
