LON_PARD8
ID LON_PARD8 Reviewed; 823 AA.
AC A6LD45;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 90.
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}; OrderedLocusNames=BDI_1874;
OS Parabacteroides distasonis (strain ATCC 8503 / DSM 20701 / CIP 104284 / JCM
OS 5825 / NCTC 11152).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Tannerellaceae;
OC Parabacteroides.
OX NCBI_TaxID=435591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8503 / DSM 20701 / CIP 104284 / JCM 5825 / NCTC 11152;
RX PubMed=17579514; DOI=10.1371/journal.pbio.0050156;
RA Xu J., Mahowald M.A., Ley R.E., Lozupone C.A., Hamady M., Martens E.C.,
RA Henrissat B., Coutinho P.M., Minx P., Latreille P., Cordum H.,
RA Van Brunt A., Kim K., Fulton R.S., Fulton L.A., Clifton S.W., Wilson R.K.,
RA Knight R.D., Gordon J.I.;
RT "Evolution of symbiotic bacteria in the distal human intestine.";
RL PLoS Biol. 5:1574-1586(2007).
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. {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 {ECO:0000255|HAMAP-Rule:MF_01973}.
CC -!- INDUCTION: By heat shock. {ECO:0000255|HAMAP-Rule:MF_01973}.
CC -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000255|HAMAP-
CC Rule:MF_01973}.
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DR EMBL; CP000140; ABR43609.1; -; Genomic_DNA.
DR RefSeq; WP_005854849.1; NZ_LR215978.1.
DR AlphaFoldDB; A6LD45; -.
DR SMR; A6LD45; -.
DR STRING; 435591.BDI_1874; -.
DR PRIDE; A6LD45; -.
DR EnsemblBacteria; ABR43609; ABR43609; BDI_1874.
DR KEGG; pdi:BDI_1874; -.
DR eggNOG; COG0466; Bacteria.
DR HOGENOM; CLU_004109_4_3_10; -.
DR OMA; GAWQVVD; -.
DR OrthoDB; 128102at2; -.
DR BioCyc; PDIS435591:G1G5A-1927-MON; -.
DR Proteomes; UP000000566; Chromosome.
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 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Hydrolase; Nucleotide-binding; Protease;
KW Reference proteome; Serine protease; Stress response.
FT CHAIN 1..823
FT /note="Lon protease"
FT /id="PRO_0000396589"
FT DOMAIN 51..244
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 633..815
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT ACT_SITE 721
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT ACT_SITE 764
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT BINDING 397..404
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
SQ SEQUENCE 823 AA; 92725 MW; 32BCF1F1CB8E2FBA CRC64;
MNVYMKEKTR VFCQNSFDDL DDNIGIVMPI LTECDVDEDF TEGIEKVGDT IPILPLRNMV
LFPGVALPVI IGRPKSMRLI KEAVHKKSLI GVVCQKEMGT EDPILEDLYT TGVIADIVRV
LEMPDGSTTV ILQGKKRFEL NELTETDPYL SGKITVLEDT KPDKTDREFE ALISTIKDLT
IKMLGAVAEP PRDLIFSIKN NKNVLYVVNF SCSNIPSGSA EKQQLLLIGD LKERAYRLLF
ILNREYQLVE LKASIQMKTH EDINQQQKEY FLQQQIKTIQ EELGGNINEL EIKELREKAS
RKKWPAEVAQ VFEKELRKLE RLHPQSPDYS VQTQYVQNIV NLPWNEYSKD NFNLSHAQKV
LDRDHYGLEK VKERIIEHLA VLKLKGDMKS PIICLYGPPG VGKTSLGRSI AEALRRKYVR
VSLGGLHDEA EIRGHRRTYI GAMCGRIIQN IQKAGTSNPV FILDEIDKIT NDFKGDPASA
LLEVLDPEQN NAFHDNYLDI DYDLSKVMFI ATANNLNTIS QPLLDRMELI EVSGYIMEEK
VEIAAKHLVP KQMDVHGLKK GSVKFPKKTL QVIVEAYTRE SGVRELDKKI AKIMRKLARK
VASDEPIPTS IKPEDLYEYL GAVEYSRDKY QGNDYAGVVT GLAWTAVGGE ILFVESSLSK
GKGSKLTLTG NLGDVMKESA MLALEYIHAH AAQFNINEEL FENWNVHVHV PEGAIPKDGP
SAGITMVTSL VSAFTQRKVK KNLAMTGEIT LRGKVLPVGG IKEKILAAKR AGIKELILCK
ENEKDINEIK PEYLKGLVFH YVSDIQQVVD LALLREKVDN PLF
