LON_MYCSM
ID LON_MYCSM Reviewed; 779 AA.
AC O31147;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 116.
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};
OS Mycolicibacterium smegmatis (Mycobacterium smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=1772;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, ACTIVITY REGULATION, AND
RP MUTAGENESIS OF SER-675.
RX PubMed=9425059; DOI=10.1021/bi971732f;
RA Roudiak S.G., Seth A., Knipfer N., Shrader T.E.;
RT "The lon protease from Mycobacterium smegmatis: molecular cloning, sequence
RT analysis, functional expression, and enzymatic characterization.";
RL Biochemistry 37:377-386(1998).
RN [2]
RP SUBUNIT.
RX PubMed=11478899; DOI=10.1021/bi0102508;
RA Rudyak S.G., Brenowitz M., Shrader T.E.;
RT "Mg2+-linked oligomerization modulates the catalytic activity of the Lon
RT (La) protease from Mycobacterium smegmatis.";
RL Biochemistry 40:9317-9323(2001).
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 ECO:0000269|PubMed:9425059}.
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 -!- ACTIVITY REGULATION: Stimulated by unfolded protein.
CC {ECO:0000269|PubMed:9425059}.
CC -!- SUBUNIT: Homohexamer. Organized in a ring with a central cavity (By
CC similarity). Oligomerization is Mg(2+)-dependent. {ECO:0000255|HAMAP-
CC Rule:MF_01973, ECO:0000269|PubMed:11478899}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
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; AF030688; AAB86425.1; -; Genomic_DNA.
DR AlphaFoldDB; O31147; -.
DR SMR; O31147; -.
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 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Hydrolase; Nucleotide-binding; Protease;
KW Serine protease; Stress response.
FT CHAIN 1..779
FT /note="Lon protease"
FT /id="PRO_0000076141"
FT DOMAIN 7..188
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 589..769
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT ACT_SITE 675
FT ACT_SITE 718
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT BINDING 352..359
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT MUTAGEN 675
FT /note="S->A,T: Loss of activity."
FT /evidence="ECO:0000269|PubMed:9425059"
FT MUTAGEN 675
FT /note="S->C: Retains some activity."
FT /evidence="ECO:0000269|PubMed:9425059"
SQ SEQUENCE 779 AA; 83676 MW; EA063D92BD26CD9F CRC64;
MAEAKTVPVL FLNDSIVLPG MVVPIELDDA ARAAVDAARA SESGELLIAP RLEDRYPAYG
VLASIVQIGR LPNGDAAAVV RGERRAHIGS GTSGPGAALW VQVEEVTDPE PTDETKKLAG
EYKKLLLAML QRRDAWQIVD MVNKITDPSA LADTAGYASY LTGTQKRELL ETTDVDRRLS
LLIGWTGDHL AETEVNDKIA EDVRTGMEKQ QKEFLLRQQL AAIRKELGEL DDNGDGSSDD
YRARIEQADL PEKVREAALR EVGKLERASD QSPEGGWIRT WLDTVLDLPW NVRTEDSTDL
ARAREILDTD HHGLSDVKDR IVEYLAVRGA APQRGMAVVG GRGSGAVMVL AGPPGVGKTS
LGESVARALD RKFVRVALGG VRDEAEIRGH RRTYVGALPG RIVRAIGEAG SMNPVVLLDE
IDKVGSDYRG DPAAALLEVL DPAQNHTFRD HYLDLDLDLS DVVFLVTANV IENIPSALLD
RMELVEIDGY TADDKLAIAQ GFLLPRQRER GGLTSDEVTV TEAALRKIAA DYTREPGVRQ
FERLLAKAMR KAATKLADHP QAAPITIDEP DLVEYLGRPR FLPESAERTA VPGVATGLAV
TGLGGDVLYI EANSTEGEPG LQLTGQLGDV MKESAQIAMS YVRAHAKQLG VDPEALNRRI
HIHVPAGAVP KDGPSAGVTM VTALVSMATG RKVRGDVGMT GEVTLNGRVL PIGGVKQKLL
AAQRAGLSTV FIPQRNQPDL DDVPADVLDA LDVRPMTDVA DIIAAALEPA HEASTAAAA
