LON1_HERA2
ID LON1_HERA2 Reviewed; 815 AA.
AC A9B5N1;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Lon protease 1 {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 1 {ECO:0000255|HAMAP-Rule:MF_01973};
GN Name=lon1 {ECO:0000255|HAMAP-Rule:MF_01973}; OrderedLocusNames=Haur_1621;
OS Herpetosiphon aurantiacus (strain ATCC 23779 / DSM 785 / 114-95).
OC Bacteria; Chloroflexi; Chloroflexia; Herpetosiphonales; Herpetosiphonaceae;
OC Herpetosiphon.
OX NCBI_TaxID=316274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23779 / DSM 785 / 114-95;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Bryant D.A., Richardson P.;
RT "Complete sequence of chromosome of Herpetosiphon aurantiacus ATCC 23779.";
RL Submitted (OCT-2007) 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; CP000875; ABX04264.1; -; Genomic_DNA.
DR AlphaFoldDB; A9B5N1; -.
DR SMR; A9B5N1; -.
DR STRING; 316274.Haur_1621; -.
DR EnsemblBacteria; ABX04264; ABX04264; Haur_1621.
DR KEGG; hau:Haur_1621; -.
DR eggNOG; COG0466; Bacteria.
DR HOGENOM; CLU_004109_4_3_0; -.
DR OMA; KKMNPVM; -.
DR Proteomes; UP000000787; 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..815
FT /note="Lon protease 1"
FT /id="PRO_0000396575"
FT DOMAIN 14..209
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 606..787
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT ACT_SITE 693
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT ACT_SITE 736
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT BINDING 370..377
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
SQ SEQUENCE 815 AA; 90406 MW; D4B9A338EE6109AA CRC64;
MSEVERTTTI PDEIAILPLL GTVAYPQTIM PLAIGQPESI RLIDDLMAGQ RIVGLMALKN
EDERPNPVLP EDFYQLGSAA VVHKLMKLPD GTLRAAMQVL ERIEIVEIIQ TEPYYRAKIR
VMPDALAESE QLEVTALMRS IGTIASQIAP LIPQFPTELL NSVLSEEDPR RLAYLVASYA
RMSVTDRQAV LAEPSIKQKL LKLNEVLTRE LNVLQIGQQI QSQVQDEMSK TQREYVLREQ
LKAIRKELGE NNEQEVEVDR LAEQIEAAGM SAEAHQQAMR ELDRLRQMPT AAAEYSVIRG
YLETLIALPW QKRSDDTIDV AQATEVLDAD HYGLDEIKER ILDYLAVREL RRKRSPERDP
GRGAILCFVG PPGVGKTSLG RSIAKAMNRE FVRLSLGGVH DEAEIRGHRR TYIGAMPGSL
IQAIRRSGVN NPVVLLDEID KLSSDHRGDP TSAMLEVLDP AQNTNFRDHY LDVAWDLSPV
MFIATANTLQ TIPAPLRDRL EIIQLGSYTM REKYEIASRY LVPEQREQHS LAPNEVEIDH
EALLVAIEEY TREAGVRNLE QQIGTLMRKA ARQVALGSAT PIVLDPAKTR EYLGKRRYFS
EIHERTDRPG IVTGLVWTPV GGDIIFIEAT KMTGRGNFAL SGQLGDVMKE SARAALSWVR
AEGEAYGIDP NFAQHYDLHV HVPAGAQPKD GPSAGIAMAT ALVSLLTGRV LRDDVAMTGE
ITLRGKVLPI GGVREKVLAA HRAGIRTIIL PQRNLADLDE IPADVLAEVQ FHGVEHVGQV
IELALRAEAS EAPVSVPESA VMPNLFQSDV EVLVH
