LON_TRIL1
ID LON_TRIL1 Reviewed; 816 AA.
AC B3E7K2;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 82.
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=Glov_2806;
OS Trichlorobacter lovleyi (strain ATCC BAA-1151 / DSM 17278 / SZ) (Geobacter
OS lovleyi).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC Geobacteraceae; Trichlorobacter.
OX NCBI_TaxID=398767;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1151 / DSM 17278 / SZ;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Meincke L., Brettin T.,
RA Detter J.C., Han C., Tapia R., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Sung Y., Fletcher K.E.,
RA Ritalahti K.M., Loeffler F.E., Richardson P.;
RT "Complete sequence of chromosome of Geobacter lovleyi SZ.";
RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001089; ACD96519.1; -; Genomic_DNA.
DR AlphaFoldDB; B3E7K2; -.
DR SMR; B3E7K2; -.
DR STRING; 398767.Glov_2806; -.
DR MEROPS; S16.001; -.
DR PRIDE; B3E7K2; -.
DR EnsemblBacteria; ACD96519; ACD96519; Glov_2806.
DR KEGG; glo:Glov_2806; -.
DR eggNOG; COG0466; Bacteria.
DR HOGENOM; CLU_004109_4_3_7; -.
DR OMA; KKMNPVM; -.
DR Proteomes; UP000002420; 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..816
FT /note="Lon protease"
FT /id="PRO_0000396570"
FT DOMAIN 27..219
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 608..789
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT REGION 795..816
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 695
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT ACT_SITE 738
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT BINDING 372..379
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
SQ SEQUENCE 816 AA; 90910 MW; AC439FBB7BBC0EF0 CRC64;
MSKSDQEHTT TEPTIVAEEE LRIPELLPLL PIRDVVVYPF MIIPLFVGRE MSIKAVDQAL
AGDRMIMLAT QHDIGDEDPT PDKIYNVGTV AMIMRMLKLP DGRVKILVQG LVKARIAEFV
EFKPFHTVRI ERLVEPVAVD NLETEALMRT VREQLAKIAE LGKQISPEVM VILENITDPG
SMADLIASNL GLKLSEAQML LEIEDPVRRL TKVNDLLARE HEMLSVQAQI QNAAREEMGK
NQKEYYLREQ MKAIQQELGD HDGKEELEEL RKAIETARMP ENVEKEALKQ LGRLERMHGD
SGEAGVIRTY LDWLIEIPWS KTTRDSLDII RAKKILDEDH SYLDKVKERI LEFLAVRKLN
KQMKGPILCF VGPPGVGKTS LGKSIARALN RKFVRISLGG VRDEAEIRGH RRTYLGALPG
RIIQGMKQAG TRNPVFMLDE LDKLGYDYKG DPSAALLEVL DPQQNNAFSD HYVNLPYDLS
NVLFVATANH SDPIPSALFD RMEVINIPGY TEEEKLEIAI RYLVPRQMKD NGLKAKHIVF
EEEALKEIIA KYTREAGLRN LEREIGNVCR KVARKIAEGH KRQIRVTPAA VATFLGAAKF
LRDDEMDKNE VGVVNGLAWT SVGGEVLHIE ATTMAGKGGM ALTGQLGDVM KESVQAALAY
IRSHGSEFHI NPDWFQENEI HVHVPAGAVP KDGPSAGCAM ATALISVLTK VPVKKDVAMT
GEISLRGKVL PIGGLKEKIL AAVRAGMKMV IIPEQNRKDL EDIPKAMQKK VKIVPVKEID
EVLKLALEKF PIPAPKGKAK PATPKVVVRP SKEISA
