ID   LON1_MYXXA              Reviewed;         817 AA.
AC   P36773;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   02-SEP-2026, entry version 128.
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}; Synonyms=lonV;
OS   Myxococcus xanthus.
OC   Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
OC   Cystobacterineae; Myxococcaceae; Myxococcus.
OX   NCBI_TaxID=34;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DZF1;
RX   PubMed=8468287; DOI=10.1128/jb.175.8.2271-2277.1993;
RA   Tojo N., Inouye S., Komano T.;
RT   "Cloning and nucleotide sequence of the Myxococcus xanthus lon gene:
RT   indispensability of lon for vegetative growth.";
RL   J. Bacteriol. 175:2271-2277(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DZF1;
RA   Ueki T., Inouye S.;
RL   Submitted (FEB-1999) 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.
CC   -!- DEVELOPMENTAL STAGE: Expressed during vegetative growth.
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; D12923; BAA02307.1; -; Genomic_DNA.
DR   EMBL; AF127082; AAD31005.1; -; Genomic_DNA.
DR   PIR; A49844; A49844.
DR   RefSeq; WP_011552101.1; NZ_CBCSLF010000073.1.
DR   AlphaFoldDB; P36773; -.
DR   SMR; P36773; -.
DR   MEROPS; S16.001; -.
DR   GeneID; 41359427; -.
DR   OMA; ICTANTM; -.
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   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd19500; RecA-like_Lon; 1.
DR   FunFam; 3.30.230.10:FF:000010; Lon protease; 1.
DR   FunFam; 1.20.5.5270:FF:000002; Lon protease homolog; 1.
DR   FunFam; 3.40.50.300:FF:000021; Lon protease homolog; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 1.20.5.5270; -; 1.
DR   Gene3D; 1.20.58.1480; -; 1.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 2.30.130.40; LON domain-like; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; IPR054594; Lon_lid.
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_Su5_D2-typ_SF.
DR   InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR   NCBIfam; TIGR00763; lon; 1.
DR   NCBIfam; NF008053; PRK10787.1; 1.
DR   PANTHER; PTHR10046; ATP DEPENDENT LON PROTEASE FAMILY MEMBER; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF05362; Lon_C; 1.
DR   Pfam; PF22667; Lon_lid; 1.
DR   Pfam; PF02190; LON_substr_bdg; 1.
DR   PIRSF; PIRSF001174; Lon_proteas; 1.
DR   PRINTS; PR00830; ENDOLAPTASE.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00464; LON; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF88697; PUA domain-like; 1.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR   PROSITE; PS51787; LON_N; 1.
DR   PROSITE; PS51786; LON_PROTEOLYTIC; 1.
DR   PROSITE; PS01046; LON_SER; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Cytoplasm; Hydrolase; Nucleotide-binding; Protease;
KW   Serine protease; Stress response.
FT   CHAIN           1..817
FT                   /note="Lon protease 1"
FT                   /id="PRO_0000076142"
FT   DOMAIN          18..216
FT                   /note="Lon N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT   DOMAIN          604..785
FT                   /note="Lon proteolytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT   REGION          789..817
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        691
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT   ACT_SITE        734
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT   BINDING         368..375
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
SQ   SEQUENCE   817 AA;  91815 MW;  BE2DAD65502883DF CRC64;
     MFFGRDDKKE AQKRGLTVPL LPLRDIIVFP HMVVPLFVGR EKSIAALKDA MAHKGPDDKA
     VILLAAQKKA KTNDPTPDDI FHFGTLGHVI QLLPLPDGTV KVLVEGVRRA KVKKFHPNDA
     FFMVEVEEVE EQTEKTVELE ALVRSVHSVF EAFVKLNKRI PPEMLMQVAS IDDPARLADT
     IVAHLSLKLN DKQALLETES PAKRLEKLYE LMQGEIEILQ VEKKIRTRVK KQMEKTQKEY
     YLNEQMQAIQ KELGERDEFK NEIQEIEEKL KNKRMSKEAT LKVKKELKKL RMMSPMSAEA
     TVVRNYIDWI ISLPWYDETQ DRLDVTEAET VLNEDHYGLK KPKERILEYL AVQQLVKKLK
     GPVLCFVGPP GVGKTSLARS IARATGRKFV RLSLGGVRDE AEIRGHRRTY IGAMPGKLIQ
     SLKKAGSNNP VFLLDEIDKM STDFRGDPSA ALLEVLDPEQ NHTFNDHYLD LDYDLSKVMF
     ICTANTMHNI PGPLQDRMEV IRIAGYTEPE KLSIARRYLI PKEQEANGLS DLKVDISDPA
     LRTIIHRYTR ESGVRSLERE IGGVFRKIAR DVLKNGKRDI DVDRKMAMKF LGTPRYRYGM
     AEAEDQVGIV TGLAWTELGG EILTTEATIM PGKGKLIITG KLGEVMQESA QAAMSYVRSR
     AERFGIDRKV FENYDIHVHL PEGAIPKDGP SAGVTICTAL VSALTRVLIR RDVAMTGEIT
     LRGRVLPIGG LKEKTLAAHR AGIKTVLIPK ANKKDLKDIP LKIRKQLRIV PVEFVDDVLR
     EALVLEKPEE FGRKPTTDGG KLGGTTELPA SPAVAPA
//