LON_HELMI
ID LON_HELMI Reviewed; 813 AA.
AC B0TFI9;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 89.
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=Helmi_02960;
GN ORFNames=HM1_0474;
OS Heliobacterium modesticaldum (strain ATCC 51547 / Ice1).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Heliobacteriaceae;
OC Heliomicrobium.
OX NCBI_TaxID=498761;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51547 / Ice1;
RX PubMed=18441057; DOI=10.1128/jb.00299-08;
RA Sattley W.M., Madigan M.T., Swingley W.D., Cheung P.C., Clocksin K.M.,
RA Conrad A.L., Dejesa L.C., Honchak B.M., Jung D.O., Karbach L.E.,
RA Kurdoglu A., Lahiri S., Mastrian S.D., Page L.E., Taylor H.L., Wang Z.T.,
RA Raymond J., Chen M., Blankenship R.E., Touchman J.W.;
RT "The genome of Heliobacterium modesticaldum, a phototrophic representative
RT of the Firmicutes containing the simplest photosynthetic apparatus.";
RL J. Bacteriol. 190:4687-4696(2008).
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; CP000930; ABZ83088.1; -; Genomic_DNA.
DR RefSeq; WP_012281466.1; NC_010337.2.
DR AlphaFoldDB; B0TFI9; -.
DR SMR; B0TFI9; -.
DR STRING; 498761.HM1_0474; -.
DR MEROPS; S16.001; -.
DR EnsemblBacteria; ABZ83088; ABZ83088; HM1_0474.
DR KEGG; hmo:HM1_0474; -.
DR eggNOG; COG0466; Bacteria.
DR HOGENOM; CLU_004109_4_3_9; -.
DR OMA; GAWQVVD; -.
DR OrthoDB; 128102at2; -.
DR Proteomes; UP000008550; 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..813
FT /note="Lon protease"
FT /id="PRO_0000396573"
FT DOMAIN 14..205
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 595..776
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT ACT_SITE 682
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT ACT_SITE 725
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT BINDING 359..366
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
SQ SEQUENCE 813 AA; 91309 MW; EEA175E8922C854B CRC64;
MAEEEKIRQT IQELPLLPLR GIIVFPYMVM HLDVGRERSV NAIEEAMAQD RIIFLATQKE
AQTDQPGAED IYQIGVIAEI KQLLKLPGGT IRVLVEGLAR AEILEYIDME PLIRVRVREH
IEPDVKSNAV EALMRSLINQ FEQYVKISKK IPPETFVSVV AVEDPGRLTD TISSHLTLKT
QDKQRILEAL DVTERLEILT EILAREMEIL ELERKINVRV RKQMEKTQKE YYLREQIKAI
QKELGEKEDR QAEGEDLRNK IAKAKLPKEV EEKALREVER LEKMPPMVAE ATVVRNYLDW
LLALPWAKQT KDRLDIDKAE AILNEDHFGL DKVKERIIEY LAIRKLAQKM KGPIICFVGP
PGVGKTSLAR SIARALERKF VRLSLGGVRD EAEIRGHRRT YVGAMPGRLI QGLRTAGSKN
PVFLLDEIDK MSMDFRGDPA SALLEVLDPE QNSTFSDHFI EVPFDLSKVL FITTANGMHN
IPRPLLDRME VIYIPGYTEE EKTRIALDHL VPKQLKEHGL KKEQVQISEN TVRRLIREYT
REAGVRNLER EIASLCRKSA RAIVKNPERR LSISAGNLPS YLGIPRFRYG LAEAESQVGV
ATGLAWTETG GDTLAIEVAH MPGKGNLALT GKLGDVMKES AQASLTYVRS RARELGIADN
FHQNTDIHIH VPEGAIPKDG PSAGITIATA LTSALSRRPV RREVAMTGEI TLRGRVLPVG
GIKEKMLAAN RAGCTTVILP AENKKDLEEV PANVKKKLRF VLVEHMDQVI REALLEPVPV
QAPEPPETIP AAIETSVPVY QGMLEETPPG LQT
