LON_CHLAD
ID LON_CHLAD Reviewed; 824 AA.
AC B8G736;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, 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=Cagg_1079;
OS Chloroflexus aggregans (strain MD-66 / DSM 9485).
OC Bacteria; Chloroflexi; Chloroflexia; Chloroflexales; Chloroflexineae;
OC Chloroflexaceae; Chloroflexus.
OX NCBI_TaxID=326427;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD-66 / DSM 9485;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Pitluck S., Foster B., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Bryant D.A., Richardson P.;
RT "Complete sequence of Chloroflexus aggregans DSM 9485.";
RL Submitted (DEC-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; CP001337; ACL23993.1; -; Genomic_DNA.
DR RefSeq; WP_012616357.1; NC_011831.1.
DR AlphaFoldDB; B8G736; -.
DR SMR; B8G736; -.
DR STRING; 326427.Cagg_1079; -.
DR MEROPS; S16.001; -.
DR PRIDE; B8G736; -.
DR EnsemblBacteria; ACL23993; ACL23993; Cagg_1079.
DR KEGG; cag:Cagg_1079; -.
DR eggNOG; COG0466; Bacteria.
DR HOGENOM; CLU_004109_4_3_0; -.
DR OMA; DVMKMID; -.
DR OrthoDB; 128102at2; -.
DR Proteomes; UP000002508; 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; 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.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Hydrolase; Nucleotide-binding; Protease;
KW Serine protease; Stress response.
FT CHAIN 1..824
FT /note="Lon protease"
FT /id="PRO_0000396543"
FT DOMAIN 26..220
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 617..798
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 800..824
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 704
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT ACT_SITE 747
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT BINDING 375..382
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
SQ SEQUENCE 824 AA; 92561 MW; EA5591C738B94337 CRC64;
MNEPMSLFDD LPEEHDEPQE APERRLPMVV LGEMVIMPHM TIPLQVPQGK SYRAMERAWE
EDRDVLLIFV REHQLEGYKS NQPQNLPPIG VIAQLQEFAK LNDGTARVIL EGQSRAQIIE
AIQITPFYRV RCRPYTDPPV SGLEVEALME TVKQQVDEFV EHLGEVPQEA VQFVHRIDRP
GHLADIVTWG PAFDFKDRLE VLNTLDPVER LRKVYLVLAR QLELLKLRVK IQQDTKEVLD
QSQREYFLRE QLRIIRRELG EDEEGDDPID ELRRKIHELD APEYVKNQAL HELKRLAQQG
MNNPESGVIR TYLDWILSLP WADEELPEIS ITEAQKVLDA DHYGLEKVKE RILEYLAVRK
LAGDKMRSPI LCFVGPPGVG KTSLGRSIAR ALGRKFVRTS LGGVRDEAEI RGHRRTYIGA
MPGRIIQAMK NAKSKSPVYI LDEVDKIGLD FRGDPTSALL EVLDPEQNNA FSDHYLEIPF
DLSKVIFIAT ANQLDPIPLP LRDRMEIIEI GGYTEDEKLE IARGFLIPKQ REFHGLTEDQ
IEFTEGAILK LIREYTREAG VRGLEREIAS LCRKVARQVA EQTEANGELP PKFVIDEAAV
VKYLGPERYT YGIAEEQDEV GVATGVAWTS AGGDILSIEV LPFKGKGQLQ LTGQLGEVMK
ESAQTAVSYV RSRAADFGID PNTFEETNIH IHIPEGAVPK DDPSAGITLT TALISALTGT
PVRRDVAMTG EVTLRGKVLP IGGLKEKTLA AHRAGIRTFI LPKENAKDIS ELPEKVRREL
NLIPVSSMDE VLRIALSRMP TPANNQNGSH TNNRGQPSPA PAGT
