ID   LON_CAMJE               Reviewed;         791 AA.
AC   O69300; Q0P9I1; Q9PNM1;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   03-AUG-2022, entry version 131.
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=Cj1073c;
OS   Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS   11168).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=192222;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RX   PubMed=9742705; DOI=10.1111/j.1574-6968.1998.tb13165.x;
RA   Thies F.L., Hartung H.-P., Giegerich G.;
RT   "Cloning and expression of the Campylobacter jejuni lon gene detected by
RT   RNA arbitrarily primed PCR.";
RL   FEMS Microbiol. Lett. 165:329-334(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700819 / NCTC 11168;
RX   PubMed=10688204; DOI=10.1038/35001088;
RA   Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA   Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA   Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA   Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA   Barrell B.G.;
RT   "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT   reveals hypervariable sequences.";
RL   Nature 403:665-668(2000).
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       ECO:0000269|PubMed:9742705}.
CC   -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000255|HAMAP-
CC       Rule:MF_01973}.
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DR   EMBL; Y17166; CAA76672.1; -; Genomic_DNA.
DR   EMBL; AL111168; CAL35190.1; -; Genomic_DNA.
DR   PIR; D81310; D81310.
DR   RefSeq; WP_002868636.1; NC_002163.1.
DR   RefSeq; YP_002344466.1; NC_002163.1.
DR   AlphaFoldDB; O69300; -.
DR   SMR; O69300; -.
DR   IntAct; O69300; 1.
DR   STRING; 192222.Cj1073c; -.
DR   MEROPS; S16.001; -.
DR   PaxDb; O69300; -.
DR   PRIDE; O69300; -.
DR   EnsemblBacteria; CAL35190; CAL35190; Cj1073c.
DR   GeneID; 905364; -.
DR   KEGG; cje:Cj1073c; -.
DR   PATRIC; fig|192222.6.peg.1055; -.
DR   eggNOG; COG0466; Bacteria.
DR   HOGENOM; CLU_004109_4_3_7; -.
DR   OMA; KKMNPVM; -.
DR   Proteomes; UP000000799; 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   2: Evidence at transcript level;
KW   ATP-binding; Cytoplasm; Hydrolase; Nucleotide-binding; Protease;
KW   Reference proteome; Serine protease; Stress response.
FT   CHAIN           1..791
FT                   /note="Lon protease"
FT                   /id="PRO_0000076128"
FT   DOMAIN          13..201
FT                   /note="Lon N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT   DOMAIN          600..791
FT                   /note="Lon proteolytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT   ACT_SITE        697
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT   ACT_SITE        740
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT   BINDING         364..371
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT   CONFLICT        302
FT                   /note="I -> V (in Ref. 1; CAA76672)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        531
FT                   /note="S -> F (in Ref. 1; CAA76672)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   791 AA;  90100 MW;  970A3C6E84BBE600 CRC64;
     MQIEEIQNYP ANLPVLVEDE LFLYPFMITP IFINDSSNMK ALDLAIKNDS MLFVAPSKLE
     NGRNFDEIYN CGVIGTIMRK VPLPDGRVKI LFQGYAKGKI IEQISNKPLE AKIELIKEDF
     LEGTKKEALL EVLKEKVKNL ANISHYFSPD LLRTIEEGFD ASRICDLILN TVRIKKQVAY
     EFFVLTDLEQ KLVKLIDLIA QEIEANKIQK EIKNKVHSRI DKVNKEYFLK EQLRQIQKEL
     GSDTQKEDEV REYQKRLELK KKFMHEDAYK EIKKQIEKFE RIHQDNSEAS MIQTYIETAL
     DIPFEKISKK KLDIKEVSKQ LNHDHYALNK PKERIEEYFA VRELLEKRKI AEKDGAKVIL
     CLYGPPGVGK TSLANSVSKA LKRELIRIAL GGLEDVNELR GHRRTYIGAM PGRITQGLIE
     AKQINPVIVL DEIDKLNRSF RGDPSAVLLE ILDPEQNSKF RDYYLNFNID LSKVIFIATA
     NDISNIPAPL RDRMEFIELS SYTPSEKFHI MKKYLIPDEL KKHGLKSNEL SIDDETIELI
     ISDYTRESGV RNLRRKVAEL CRKSAKKLLL ENIKKVIINT KNLNEFLDKK VFEIEKNNGE
     NQVGQVNGLA WTSVGGDVLK VEAVKIKGKG ELTLTGSLGD VMKESARIAF SMIKVLIDEG
     KIKIPKKIII DPKVNVYDSY NIHIHVPDGA TPKDGPSAGI TISTAIASIF SDKKVKADVA
     MTGEIDLKGK VLPIGGLKEK LIAAYKADIK TALIPRKNYE RDLKDIPSEV RDNMEIIAVD
     TFSDVLEYTL V