LON_CHLAA
ID LON_CHLAA Reviewed; 827 AA.
AC A9WGB5;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, 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=Caur_0798;
OS Chloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl).
OC Bacteria; Chloroflexi; Chloroflexia; Chloroflexales; Chloroflexineae;
OC Chloroflexaceae; Chloroflexus.
OX NCBI_TaxID=324602;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29366 / DSM 635 / J-10-fl;
RX PubMed=21714912; DOI=10.1186/1471-2164-12-334;
RA Tang K.H., Barry K., Chertkov O., Dalin E., Han C.S., Hauser L.J.,
RA Honchak B.M., Karbach L.E., Land M.L., Lapidus A., Larimer F.W.,
RA Mikhailova N., Pitluck S., Pierson B.K., Blankenship R.E.;
RT "Complete genome sequence of the filamentous anoxygenic phototrophic
RT bacterium Chloroflexus aurantiacus.";
RL BMC Genomics 12:334-334(2011).
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; CP000909; ABY34036.1; -; Genomic_DNA.
DR RefSeq; WP_012256692.1; NC_010175.1.
DR RefSeq; YP_001634425.1; NC_010175.1.
DR AlphaFoldDB; A9WGB5; -.
DR SMR; A9WGB5; -.
DR STRING; 324602.Caur_0798; -.
DR EnsemblBacteria; ABY34036; ABY34036; Caur_0798.
DR KEGG; cau:Caur_0798; -.
DR PATRIC; fig|324602.8.peg.909; -.
DR eggNOG; COG0466; Bacteria.
DR HOGENOM; CLU_004109_4_3_0; -.
DR InParanoid; A9WGB5; -.
DR OMA; MVNIEDK; -.
DR Proteomes; UP000002008; 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..827
FT /note="Lon protease"
FT /id="PRO_0000396544"
FT DOMAIN 32..223
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 625..806
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 712
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT ACT_SITE 755
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT BINDING 385..392
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
SQ SEQUENCE 827 AA; 91352 MW; F45ADBB74B3E5AEA CRC64;
MNDETLREQT TAESEETSPT TPSPEPEVVE TLPLIPLEGA VVFPYIVVSL TLDELGSASA
EAAAREGRQV LLAARRPDAP ADAPITDQLF NVGVVARIEQ LGTLPNGASG VVVRGLVRAV
LGEAVQTTPY LRFRFTRRPD VFERTPELEQ LMVEVHAAID AVLELRPGVT QEIRNFVRSI
DDPGHLADNT GYSPDYTFAE RQELLETFDV SERLRKVLMF YRKQFALLEV QAKLRQEVQE
SAARQQREFY LRQQLRAIQK ELGEDTSEAA ELDDLRQKLA AADLPEVARK EADRELSRLA
RINASSPEYQ MVRTYLEWLA ELPWNKYTGQ PIDIAFARQV LDEDHHGLQK VKERILEYLA
VKQRRAALGE ENLRANREPI LAFVGPPGVG KTSLGQSIAR ALGRSFVRMS LGGVRDEAEL
RGFRRTYIGS QPGRIIQELR RAGTADPVIL LDEIDKLGID YRGDPAAALL EVLDPEQNHT
FTDHYLNLPF DLSRVLFLAT ANTWDTVPPA LRDRMEVIEL SGYIEDEKVQ IAQIHLVPRQ
LRANGLRPEE AVVTEDAIRC IINEYTREAG VRNLERSIGA VLRKVARRLS EGEIDPANTP
FVVDAAFVRA ALGRPRFTNE TRERIDQPGV AIGLVWTPVG GDIIFVEASA VEGKKELTIT
GQLGEVMRES AEAALTYVRS RARSLGIEPD FFETHAIHIH VPAGAVPKDG PSAGITMATA
LASAATGRLV RDDIAMTGEI SLRGRVLPIG GIKEKALGAH RAGIRTVILP RRNLIDLDDL
PPAVSAEMTF IPVDTLDEVL SIALLPPATT TDTLTVAQRS DVLTPAS
