LON1_MYXXA
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 03-AUG-2022, entry version 113.
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; Proteobacteria; Deltaproteobacteria; 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_JABFNQ010000086.1.
DR AlphaFoldDB; P36773; -.
DR SMR; P36773; -.
DR MEROPS; S16.001; -.
DR PRIDE; P36773; -.
DR GeneID; 41359427; -.
DR OMA; GAWQVVD; -.
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 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..214
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
