LON_COPPD
ID LON_COPPD Reviewed; 768 AA.
AC B5Y8Q8;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 79.
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};
GN OrderedLocusNames=COPRO5265_0816;
OS Coprothermobacter proteolyticus (strain ATCC 35245 / DSM 5265 / OCM 4 /
OS BT).
OC Bacteria; Coprothermobacterota; Coprothermobacteria; Coprothermobacterales;
OC Coprothermobacteraceae; Coprothermobacter.
OX NCBI_TaxID=309798;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35245 / DSM 5265 / OCM 4 / BT;
RA Dodson R.J., Durkin A.S., Wu M., Eisen J., Sutton G.;
RT "The complete genome sequence of Coprothermobacter proteolyticus strain
RT ATCC 5245 / DSM 5265 / BT.";
RL Submitted (AUG-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; CP001145; ACI16990.1; -; Genomic_DNA.
DR RefSeq; WP_012543642.1; NC_011295.1.
DR AlphaFoldDB; B5Y8Q8; -.
DR SMR; B5Y8Q8; -.
DR STRING; 309798.COPRO5265_0816; -.
DR MEROPS; S16.001; -.
DR PRIDE; B5Y8Q8; -.
DR EnsemblBacteria; ACI16990; ACI16990; COPRO5265_0816.
DR KEGG; cpo:COPRO5265_0816; -.
DR eggNOG; COG0466; Bacteria.
DR HOGENOM; CLU_004109_4_3_9; -.
DR OMA; KKMNPVM; -.
DR OrthoDB; 128102at2; -.
DR Proteomes; UP000001732; 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..768
FT /note="Lon protease"
FT /id="PRO_0000396550"
FT DOMAIN 5..195
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 585..766
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT ACT_SITE 672
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT ACT_SITE 715
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT BINDING 349..356
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
SQ SEQUENCE 768 AA; 85999 MW; CE552E3FA159C3C2 CRC64;
MSEKLPVIPL KNVVMFPGIV LPLLIGRPKS IKALEEAMKG TKQVILLAQK DENIDEPAPS
DLYDVGVIGE VIQIFRAPDG TVRMVVEAKT RVKASVSDSG EFLEGNYEVL EEVEGDATRT
EALVKATIAR FEEYARLSGR IPIEVVAGIG GLDNPGKIAD MVAANMFISY YEKQKVLELL
SIPERLEHVL QLLLREIEVL KLSQEIEETV RERMEKNQRE YILREQLKAI QEELGEKDER
TIEIEQYKKR IEESGMPEEA RKKAEEELDR LQRMPPYSAE LAVIRTYLDW LVSLPWNART
EDEDDLKTVK QKLDKSHYGL DDAKERIVEF IATKKLSSNP KAPILCLVGP PGVGKTSLAK
AIATALNRKL VRISLGGIRD EAEIRGHRRT YVGAMPGRII QGIRSAGTKN PVFVLDEIDK
LSSDFLGDPS AALLEALDPE QNYAFQDHYL EVPFDLSEVF FITTANNLYT IPPALLDRME
VIRVPGYTEE EKLHIAKDFI LPKLYEQSGL NPEEVSFSDQ AIIRIIREYT REAGVRNLER
NLLSILRKLA VEKLEKGFSR VRITVKNVED YLGVPKFRYG KALEKPEIGV VAGLAWTEFG
GETMLIECQV VKGKGQLILT GSLGQTLKES AMAALTYVRS RAKQLGIDEE FYKKYDIHVH
APEGAIPKDG PSAGITIATA MISALKKEPV PNDLAMTGEI TITGKVLPIG GVKEKVLAAH
RIGLDRVILP KDNKINMEEI GDEVKKKLRF YFVDTMDQVV EIVFGKTS
