LON_CAMC1
ID LON_CAMC1 Reviewed; 805 AA.
AC A7ZEJ3;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 88.
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=Ccon26_13520;
GN ORFNames=CCC13826_1958;
OS Campylobacter concisus (strain 13826).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=360104;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=13826;
RA Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G.,
RA Mandrell R.E., On S., Nelson K.E.;
RT "Genome sequence of Campylobacter concisus 13826 isolated from human
RT feces.";
RL Submitted (OCT-2007) 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 {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; CP000792; EAT98804.1; -; Genomic_DNA.
DR RefSeq; WP_012140105.1; NC_009802.2.
DR AlphaFoldDB; A7ZEJ3; -.
DR SMR; A7ZEJ3; -.
DR STRING; 360104.CCC13826_1958; -.
DR MEROPS; S16.001; -.
DR EnsemblBacteria; EAT98804; EAT98804; CCC13826_1958.
DR KEGG; cco:CCC13826_1958; -.
DR eggNOG; COG0466; Bacteria.
DR HOGENOM; CLU_004109_4_3_7; -.
DR OMA; KKMNPVM; -.
DR OrthoDB; 128102at2; -.
DR Proteomes; UP000001121; 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 Serine protease; Stress response.
FT CHAIN 1..805
FT /note="Lon protease"
FT /id="PRO_0000396542"
FT DOMAIN 13..203
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 603..803
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT ACT_SITE 708
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT ACT_SITE 751
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT BINDING 366..373
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
SQ SEQUENCE 805 AA; 90595 MW; 73F7680DC2B1E20D CRC64;
MQINENKGFP TEIPIIVEDE LFLYPFMITP LFLSDEENLK ALELAIQGET PILVVPTKPQ
QDGARDFDGI YDAGVIGTIM RRVPLPDGRV KVLFQGIDKG KILKQSGINP LRGIVDMLHV
KRPSQVKTDA LIVVLREKVR ELSQFNHFFP PDLLKTIEES AEAVRVCDLV SSALRLKKQI
AYSFFVEENL EQRLLKLIDY VIEEIEANKL QKEIKNKVHS KIDKTNKEYF LKEQLKQIQA
ELGADTSREE ELEEYRKKLD AKKKFMAEDA YKEIKKQIDK LSRMHPDSAD ANTLQSYLDW
VLEIPFENVA KKKSSIAEVS KHLNADHYSL EKPKERIEEY FALRELLELR GVGEKVNNGA
ILCFAGPPGV GKTSLANSIA KALKRELVRI ALGGLEDVNE LRGHRRTYIG AMPGRIVQGL
IEAKQMNPVV VLDEIDKVGR SYRGDPTAVL LEILDPEQNN KFRDYYLNFN IDLSKIIFIA
TANDVSMIPA ALRDRMEFIE LSSYTPQEKF EIAKKYLLPQ ELKKHGLKPS DVSISKEALE
LIISDYTRES GVRNLRRRIA DILRKVAKNI LTKKNEGKIS VTAKNLKEFL EKKVYEIEPA
DKKDQIGLVN GLAWTSVGGD VLRIEAIRIQ GKGSMQITGQ LGDVMKESAQ IAFSVVKVLI
DNKKLKVPMP IVPKFDDDKH KLEASDVYRR YDLHLHVPEG AVPKDGPSAG ITMATAIASI
LTDTKVKHDI AMTGEITLTG RVLPIGGLKE KLIAAHKAGI KTALIPRKNY DRDLVDIPAE
VKADMKIIAV DTIDDVLKNA LVAKK
