LON_CHLT3
ID LON_CHLT3 Reviewed; 836 AA.
AC B3QSJ7;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 86.
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=Ctha_1586;
OS Chloroherpeton thalassium (strain ATCC 35110 / GB-78).
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; Chloroherpeton.
OX NCBI_TaxID=517418;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35110 / GB-78;
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., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Liu Z., Li T., Zhao F., Overmann J.,
RA Bryant D.A., Richardson P.;
RT "Complete sequence of Chloroherpeton thalassium ATCC 35110.";
RL Submitted (JUN-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; CP001100; ACF14044.1; -; Genomic_DNA.
DR RefSeq; WP_012500128.1; NC_011026.1.
DR AlphaFoldDB; B3QSJ7; -.
DR SMR; B3QSJ7; -.
DR STRING; 517418.Ctha_1586; -.
DR EnsemblBacteria; ACF14044; ACF14044; Ctha_1586.
DR KEGG; cts:Ctha_1586; -.
DR eggNOG; COG0466; Bacteria.
DR HOGENOM; CLU_004109_4_3_10; -.
DR OMA; NANFRDH; -.
DR OrthoDB; 128102at2; -.
DR Proteomes; UP000001208; 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..836
FT /note="Lon protease"
FT /id="PRO_0000396545"
FT DOMAIN 41..231
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 627..811
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT REGION 816..836
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 817..836
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 714
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT ACT_SITE 757
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 836 AA; 93003 MW; 0F94A1E657B53C7F CRC64;
MTDHTKEHEN TPSMGFLDGL VNSISQQPKA IEEEIKFDGA LPVLPLRNTV LFPDVIVPIG
VARQRSIALL ESLAPNSPVV FLMQTDADID APTPDELHKN GSVGLVLRTL RMPDNSMSVI
VQGVKRVVVE AFTQTEPYLA AKVTPKDEEE LEGVEFDAYA RTTKQLASKI IELSPNSPNE
ASYAIQSIEN TRFLIHFIAS NISVPAAEKQ KMIEAEGMKA RAERLIHFLN REVQVLELSK
QIQTKVKTDM DRSQREFILR QQLKTIQQEL GEQDAQMQDV EKLREAVEKK NLPEEVTSVV
SKEIDKLSRI PQASPDYSVT RNYVDTILAL PWGHFSETVI NLHEAEKILN QDHYGLGKVK
DRILEYLAVL KLKSNMKAPI LCFCGPPGVG KTSLGRSIAR ALGRKFIRIS LGGVRDEAEI
RGHRRTYIGS MPGRIIQGIK TAGTSNPVFM LDEIDKIGAD FRGNPSSALL EVLDPAQNNA
FSDHYLEIPY DLSKVMFIAT ANTLDPIPVP LRDRMEIINL SGYTEYEKLH IAERYLIPRQ
LEEHGIRPED VSFDALTTKK IINAYTREAG VRNLERQIAN VCRVIAKDIV IRRESDQPDE
TPITVVTADL KKYLGMEQFY PDVSEPVMLS GVAVGLAWTP VGGDILFIES TVMKGTGRLI
LTGQLGDVMK ESAQAALSYL KSCADYFKIP DEAFRYWDVH VHVPQGAIPK DGPSAGVTIL
TSLASIYTQR KVKPCIAMTG EITLRGRILP VGGIKEKVLA AKRAGITEIL LPEKNEKDVK
EALETNGGAF SDVSFKYFHE MDDLIDYVLE PAENGAPQFK VEDKDHTPET TGNESE
