LON_CYTH3
ID LON_CYTH3 Reviewed; 813 AA.
AC Q11QT1;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 96.
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=CHU_2992;
OS Cytophaga hutchinsonii (strain ATCC 33406 / DSM 1761 / CIP 103989 / NBRC
OS 15051 / NCIMB 9469 / D465).
OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Cytophagaceae;
OC Cytophaga.
OX NCBI_TaxID=269798;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33406 / DSM 1761 / CIP 103989 / NBRC 15051 / NCIMB 9469 / D465;
RX PubMed=17400776; DOI=10.1128/aem.00225-07;
RA Xie G., Bruce D.C., Challacombe J.F., Chertkov O., Detter J.C., Gilna P.,
RA Han C.S., Lucas S., Misra M., Myers G.L., Richardson P., Tapia R.,
RA Thayer N., Thompson L.S., Brettin T.S., Henrissat B., Wilson D.B.,
RA McBride M.J.;
RT "Genome sequence of the cellulolytic gliding bacterium Cytophaga
RT hutchinsonii.";
RL Appl. Environ. Microbiol. 73:3536-3546(2007).
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; CP000383; ABG60233.1; -; Genomic_DNA.
DR RefSeq; WP_011586343.1; NZ_FPJX01000002.1.
DR AlphaFoldDB; Q11QT1; -.
DR SMR; Q11QT1; -.
DR STRING; 269798.CHU_2992; -.
DR PRIDE; Q11QT1; -.
DR EnsemblBacteria; ABG60233; ABG60233; CHU_2992.
DR KEGG; chu:CHU_2992; -.
DR eggNOG; COG0466; Bacteria.
DR HOGENOM; CLU_004109_4_3_10; -.
DR OMA; GAWQVVD; -.
DR Proteomes; UP000001822; 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_0000396551"
FT DOMAIN 30..223
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 612..793
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT ACT_SITE 699
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT ACT_SITE 742
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT BINDING 376..383
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
SQ SEQUENCE 813 AA; 91748 MW; D62B6B9A65E3610A CRC64;
MLDTEPVDMI PLITPEEEAE MDKEEFPSVL PILPVRNIVL FPGVVLPITV GRQKSIRLVK
KFYKGDRTIG VVAQENQKSE EPSFQDIFKV GTVAKILRMF VLPDGNTTII IQGKRRFKIE
EQVQDEPFMQ AKVSMLKDIH PDMSKKEVKA LLQSVKESAT KILKMNPEIP QDAQIAINNI
ESENFLTHFL SSNINAELKD KQKLLEFDDA VERATWLLQL MDKDIQMLEI KREIHTKVHT
DIDQQQRDYF LRQQIKVLQD ELGDFSSEQE FERLKEKALT KKWSDKVRAH FDKEMSKLQR
VNPMAPDYPV TFNYLELLVD LPWGENSTDN FDLVRAKEIL DEDHFGLTKV KQRILEYLAV
LKLKNNMKAP ILCLYGPPGV GKTSLGKSIA KALDRKYIRM SLGGVHDESE IRGHRKTYIG
AMPGKIIQGI KRSETSNPVF ILDEIDKISK DFRGDPSSAL LEVLDPEQNS SFMDNFLEVE
YDLSKVLFIA TSNALDTIQP ALRDRMEIIE INGYTLEEKI QIAKKYLIPK QKEEHGLKAK
DISFTDAAIV KIIEDYTRES GVRNLERKIG AVVRNIAVAI AMETAYTKKI QPAQVREILG
SEDFEKDTYQ QDDLAGIVTG LAWTPYGGEI LTIESIISKG KGKLTLSGQL GDVMKESASA
ALSLLRANVD AIGIDHRVFD HFDLHVHVPA GATPKDGPSA GIALYTSLAS TFTQRKIKPA
LAMTGEITLR GKVLPVGGIK EKILAAKRAG IKEIILSKKN KKDIEEIHPP DIADLKFHFV
ETADEVLAIA LLKQKIKKPF NLEVPEEPKK KDK
