LON_PARUW
ID LON_PARUW Reviewed; 835 AA.
AC Q6ME13;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 118.
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=pc0462;
OS Protochlamydia amoebophila (strain UWE25).
OC Bacteria; Chlamydiae; Parachlamydiales; Parachlamydiaceae;
OC Candidatus Protochlamydia.
OX NCBI_TaxID=264201;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UWE25;
RX PubMed=15073324; DOI=10.1126/science.1096330;
RA Horn M., Collingro A., Schmitz-Esser S., Beier C.L., Purkhold U.,
RA Fartmann B., Brandt P., Nyakatura G.J., Droege M., Frishman D., Rattei T.,
RA Mewes H.-W., Wagner M.;
RT "Illuminating the evolutionary history of chlamydiae.";
RL Science 304:728-730(2004).
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; BX908798; CAF23186.1; -; Genomic_DNA.
DR RefSeq; WP_011175012.1; NC_005861.1.
DR AlphaFoldDB; Q6ME13; -.
DR SMR; Q6ME13; -.
DR STRING; 264201.pc0462; -.
DR EnsemblBacteria; CAF23186; CAF23186; PC_RS02245.
DR KEGG; pcu:PC_RS02245; -.
DR eggNOG; COG0466; Bacteria.
DR HOGENOM; CLU_004109_4_3_0; -.
DR OMA; GAWQVVD; -.
DR OrthoDB; 128102at2; -.
DR Proteomes; UP000000529; 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; PTHR43718; PTHR43718; 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..835
FT /note="Lon protease"
FT /id="PRO_0000396594"
FT DOMAIN 36..232
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 646..828
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT ACT_SITE 734
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT ACT_SITE 777
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT BINDING 387..394
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
SQ SEQUENCE 835 AA; 94306 MW; 4E9091725FC94831 CRC64;
MLEEPIDALE TEFENALNSL EDNQLSKING QLPEQVHVFP LLRRPFFPGM AAPLVIEPGP
FYEVLKVVAK SDHKCVGLVL TRSEQAEIYK VGFSDLYQIG VLARVLRIIP MEQGGAQVIL
NMERRIKIEK PTSETKTLKA NVSYIEDDPI LTTELKAYAI SILSTIKELL KLNPLFKEEL
QIFLGHSDFT EPGKLADFAV ALTTASREEL QDVLETFDIR KRIDKALILL KKELDISILQ
HNINQKIEAT INKSQKDFFL REQLKTIKKE LGIERDDKSL DREKFEARLK ERVVPSDVMK
VITEELEKLS VLDMQSAEYS VVRGYLDWLT TIPWGIYSQE NHNLEEAEKI LAHDHYGLED
IKQRILEFIG VGKLAKGVRG SIICLVGPPG VGKTSIGKSI ARALNRKFYR FSVGGMRDEA
EIKGHRRTYV GAMPGKMIQA LKYCQTMNPV IMLDEVDKMG KSFQGDPASA LLEVLDPEQN
AEFLDHYLDV RCNLSEVLFI VTANVLDTIP EPLKDRMDIL RLSGYIMQEK LEIAKKYLIP
RNRKEMGLKA LEVSFTQEAL RSIINGYARE SGVRNLENLL KKILRKLAVN IVREQEEHDK
EQAKKKKSSR SKKPIAFVPT KHSITPSNLK DFLGKPVFTS DRFYERTPVG VCMGLAWTAM
GGATLYIESI KVAGEKTVMK LTGQAGDVMK ESAEIAWSYV HSSIHKYAPG YTFFEKSQVH
IHIPEGATPK DGPSAGITMV TSLLSLILDT PVLDNLGMTG ELTLTGRVLP IGGVKEKLVA
ARRSGLKVLI FPKDNLRDYE ELPEYIRKGI TVHFVDHYDQ VFKISFPNKH QMKLC
