LON_ENDTX
ID LON_ENDTX Reviewed; 802 AA.
AC B1GZQ6;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 84.
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=TGRD_255;
OS Endomicrobium trichonymphae.
OC Bacteria; Elusimicrobia; Endomicrobia; Endomicrobiales; Endomicrobiaceae;
OC Endomicrobium.
OX NCBI_TaxID=1408204;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=18391199; DOI=10.1073/pnas.0801389105;
RA Hongoh Y., Sharma V.K., Prakash T., Noda S., Taylor T.D., Kudo T.,
RA Sakaki Y., Toyoda A., Hattori M., Ohkuma M.;
RT "Complete genome of the uncultured termite group 1 bacteria in a single
RT host protist cell.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:5555-5560(2008).
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; AP009510; BAG13738.1; -; Genomic_DNA.
DR RefSeq; WP_015423265.1; NC_020419.1.
DR RefSeq; YP_001956199.1; NC_020419.1.
DR AlphaFoldDB; B1GZQ6; -.
DR SMR; B1GZQ6; -.
DR STRING; 471821.TGRD_255; -.
DR MEROPS; S16.001; -.
DR PRIDE; B1GZQ6; -.
DR EnsemblBacteria; BAG13738; BAG13738; TGRD_255.
DR KEGG; rsd:TGRD_255; -.
DR PATRIC; fig|471821.5.peg.381; -.
DR HOGENOM; CLU_004109_4_3_0; -.
DR OMA; GAWQVVD; -.
DR OrthoDB; 128102at2; -.
DR Proteomes; UP000001691; 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 Serine protease; Stress response.
FT CHAIN 1..802
FT /note="Lon protease"
FT /id="PRO_0000396614"
FT DOMAIN 21..213
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 603..784
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT ACT_SITE 690
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT ACT_SITE 733
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT BINDING 367..374
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
SQ SEQUENCE 802 AA; 90373 MW; 2B2DB7074FF58A25 CRC64;
MSELDRFSND KNEMPKIPDV LPLLPVRDII LYPAMVLPLA VGREKSIKAL EESMSTNRLV
FIVTQKNIQI EDPTPKDVYN IGTICEVLQM LKMPDGTLKA LVEGISRAQW TDFKLSDKGY
IEVGLKVFDE NTLKMPEVEA IMRQTIALFE QYVKLNPRIP IDISVSVSNI ADPARLADTI
ASHLVIKNND KQTILELVDP VKRLEKIIQI LNAEIEILNI ERRIQNRVRN QIEKTQKEYY
LTEQMKAIQK ELKQKDEAQK DLDDLKGKLK KTKMPQAAKS AADKEMSRLE KMMPMSPEAT
VIRTYLEWIL DLPWEKSTID NLDLNRAKEV LDQDHYGLEK VKDRVLEYLA VLSRVQKIKG
PILCFIGPPG VGKTSIAKSV ARSLGRNFVR ISMGGVKDEA EIRGHRRTYI GSMPGKIIQS
IKKAGSNNPV FILDEIDKIG SDWRGDPSSA LLEVLDPEQN YTFNDHYLDV DFDLSNVMFI
TTANTLNNIP VTLFDRLELI RFSSYTDVEK RHIAEDFIVP KQLKEHGLKP EEFIFDDGAL
DIVIKNYTHE AGVRNLTREI ANLCRKVVKG LEFNKELKSI TIKPENLNKY LGIAYYERER
IAENDVGVAT GLAWTEVGGE TLTIEVNKMG GKNSLVLTGK LGDVMKESAQ AALTYVRSSS
QKLKIDENMF SNTDFHVHVP EGAVPKDGPS AGIALATALA SVCMNKPIKK KIAMTGEVTL
RGRVLSIGGL KEKVLAAYRE GITMILFPES NKKDLVDIPE DVIKKLQMIP VSHMDEVISL
TIERLPENKN IKMDKRNGEN GI
