LON_ECOLI
ID LON_ECOLI Reviewed; 784 AA.
AC P0A9M0; P08177; P78219; Q2MBY7;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 149.
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}; Synonyms=capR, deg, lopA, muc;
GN OrderedLocusNames=b0439, JW0429;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=8294008; DOI=10.1016/0378-1119(93)90471-e;
RA Thomas C.D., Modha J., Razzaq T.M., Cullis P.M., Rivett A.;
RT "Controlled high-level expression of the lon gene of Escherichia coli
RT allows overproduction of Lon protease.";
RL Gene 136:237-242(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3289547;
RA Amerik A.Y., Chistyakova L.G., Ostroumova N.I., Gurevich A.I.,
RA Antonov V.K.;
RT "Cloning, expression and structure of the functionally active shortened lon
RT gene in Escherichia coli.";
RL Bioorg. Khim. 14:408-411(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2242054;
RA Amerik A.I.U., Antonov V.K., Ostroumova N.I., Rotanova T.V.,
RA Chistiakova L.G.;
RT "Cloning, structure and expression of the full-size lon gene in Escherichia
RT coli coding for ATP-dependent La-proteinase.";
RL Bioorg. Khim. 16:869-880(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF SER-679.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8226758; DOI=10.1016/s0021-9258(18)41557-8;
RA Fischer H., Glockshuber R.;
RT "ATP hydrolysis is not stoichiometrically linked with proteolysis in the
RT ATP-dependent protease La from Escherichia coli.";
RL J. Biol. Chem. 268:22502-22507(1993).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 783-783.
RX PubMed=3042779; DOI=10.1016/s0021-9258(18)37843-8;
RA Chin D.T., Goff S.A., Webster T., Smith T., Goldberg A.L.;
RT "Sequence of the lon gene in Escherichia coli. A heat-shock gene which
RT encodes the ATP-dependent protease La.";
RL J. Biol. Chem. 263:11718-11728(1988).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-58, AND PROTEIN SEQUENCE OF 1-14.
RX PubMed=2984174; DOI=10.1128/jb.162.1.271-275.1985;
RA Gayda R.C., Stephens P.E., Hewick R., Schoemaker J.M., Dreyer W.J.,
RA Markovitz A.;
RT "Regulatory region of the heat shock-inducible capR (lon) gene: DNA and
RT protein sequences.";
RL J. Bacteriol. 162:271-275(1985).
RN [10]
RP PROTEIN SEQUENCE OF 2-9, AND DNA-BINDING.
RC STRAIN=ATCC 37196 / Y1089;
RX PubMed=8995294; DOI=10.1074/jbc.272.41.25678;
RA Fu G.K., Smith M.J., Markovitz D.M.;
RT "Bacterial protease Lon is a site-specific DNA-binding protein.";
RL J. Biol. Chem. 272:534-538(1997).
RN [11]
RP MUTAGENESIS OF LYS-362.
RX PubMed=7988699; DOI=10.1016/0014-5793(94)01244-x;
RA Fischer H., Glockshuber R.;
RT "A point mutation within the ATP-binding site inactivates both catalytic
RT functions of the ATP-dependent protease La (Lon) from Escherichia coli.";
RL FEBS Lett. 356:101-103(1994).
RN [12]
RP CLEAVAGE OF CCDA ANTITOXIN.
RC STRAIN=K12;
RX PubMed=8022284; DOI=10.1111/j.1365-2958.1994.tb00391.x;
RA Van Melderen L., Bernard P., Couturier M.;
RT "Lon-dependent proteolysis of CcdA is the key control for activation of
RT CcdB in plasmid-free segregant bacteria.";
RL Mol. Microbiol. 11:1151-1157(1994).
RN [13]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [14]
RP MUTAGENESIS OF HIS-665; HIS-667; ASP-676 AND ASP-743.
RX PubMed=9490010; DOI=10.1016/s0014-5793(98)00012-x;
RA Starkova N.N., Koroleva E.P., Rumsh L.D., Ginodman L.M., Rotanova T.V.;
RT "Mutations in the proteolytic domain of Escherichia coli protease Lon
RT impair the ATPase activity of the enzyme.";
RL FEBS Lett. 422:218-220(1998).
RN [15]
RP CLEAVAGE OF UMUD.
RX PubMed=9869642; DOI=10.1101/gad.12.24.3889;
RA Gonzalez M., Frank E.G., Levine A.S., Woodgate R.;
RT "Lon-mediated proteolysis of the Escherichia coli UmuD mutagenesis protein:
RT in vitro degradation and identification of residues required for
RT proteolysis.";
RL Genes Dev. 12:3889-3899(1998).
RN [16]
RP MUTAGENESIS.
RX PubMed=10094703; DOI=10.1128/jb.181.7.2236-2243.1999;
RA Ebel W., Skinner M.M., Dierksen K.P., Scott J.M., Trempy J.E.;
RT "A conserved domain in Escherichia coli Lon protease is involved in
RT substrate discriminator activity.";
RL J. Bacteriol. 181:2236-2243(1999).
RN [17]
RP FUNCTION.
RX PubMed=12135363; DOI=10.1021/bi0255470;
RA Thomas-Wohlever J., Lee I.;
RT "Kinetic characterization of the peptidase activity of Escherichia coli Lon
RT reveals the mechanistic similarities in ATP-dependent hydrolysis of peptide
RT and protein substrates.";
RL Biochemistry 41:9418-9425(2002).
RN [18]
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=15560777; DOI=10.1111/j.1432-1033.2004.04421.x;
RA Besche H., Zwickl P.;
RT "The Thermoplasma acidophilum Lon protease has a Ser-Lys dyad active
RT site.";
RL Eur. J. Biochem. 271:4361-4365(2004).
RN [19]
RP INTERACTION WITH THE YOEB-YEFM TOXIN-ANTITOXIN SYSTEM.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15009896; DOI=10.1046/j.1365-2958.2003.03941.x;
RA Christensen S.K., Maenhaut-Michel G., Mine N., Gottesman S., Gerdes K.,
RA Van Melderen L.;
RT "Overproduction of the Lon protease triggers inhibition of translation in
RT Escherichia coli: involvement of the yefM-yoeB toxin-antitoxin system.";
RL Mol. Microbiol. 51:1705-1717(2004).
RN [20]
RP FUNCTION.
RX PubMed=16584195; DOI=10.1021/bi052377t;
RA Vineyard D., Patterson-Ward J., Lee I.;
RT "Single-turnover kinetic experiments confirm the existence of high- and
RT low-affinity ATPase sites in Escherichia coli Lon protease.";
RL Biochemistry 45:4602-4610(2006).
RN [21]
RP CLEAVAGE OF SOXS.
RX PubMed=16460757; DOI=10.1016/j.jmb.2005.12.088;
RA Shah I.M., Wolf R.E. Jr.;
RT "Sequence requirements for Lon-dependent degradation of the Escherichia
RT coli transcription activator SoxS: identification of the SoxS residues
RT critical to proteolysis and specific inhibition of in vitro degradation by
RT a peptide comprised of the N-terminal 21 amino acid residues.";
RL J. Mol. Biol. 357:718-731(2006).
RN [22]
RP SUBUNIT.
RX PubMed=16511355;
RA Park S.C., Jia B., Yang J.K., Van D.L., Shao Y.G., Han S.W., Jeon Y.J.,
RA Chung C.H., Cheong G.W.;
RT "Oligomeric structure of the ATP-dependent protease La (Lon) of Escherichia
RT coli.";
RL Mol. Cells 21:129-134(2006).
RN [23]
RP ROLE IN REGULATION OF OMPF IN ASSOCIATION WITH YCGE, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=K12 / AG100;
RX PubMed=19721064; DOI=10.1128/aac.00787-09;
RA Duval V., Nicoloff H., Levy S.B.;
RT "Combined inactivation of lon and ycgE decreases multidrug susceptibility
RT by reducing the amount of OmpF porin in Escherichia coli.";
RL Antimicrob. Agents Chemother. 53:4944-4948(2009).
RN [24]
RP RETRACTED PAPER.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=21788497; DOI=10.1073/pnas.1100186108;
RA Maisonneuve E., Shakespeare L.J., Joergensen M.G., Gerdes K.;
RT "Bacterial persistence by RNA endonucleases.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:13206-13211(2011).
RN [25]
RP RETRACTION NOTICE OF PUBMED:21788497.
RX PubMed=29531044; DOI=10.1073/pnas.1803278115;
RA Maisonneuve E., Shakespeare L.J., Joergensen M.G., Gerdes K.;
RL Proc. Natl. Acad. Sci. U.S.A. 115:E2901-E2901(2018).
RN [26]
RP CLEAVAGE OF HIPB ANTITOXIN.
RX PubMed=22720069; DOI=10.1371/journal.pone.0039185;
RA Hansen S., Vulic M., Min J., Yen T.J., Schumacher M.A., Brennan R.G.,
RA Lewis K.;
RT "Regulation of the Escherichia coli HipBA toxin-antitoxin system by
RT proteolysis.";
RL PLoS ONE 7:E39185-E39185(2012).
RN [27]
RP CLEAVAGE OF ANTITOXIN MAZE, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / BW25113, and K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=24375411; DOI=10.1074/jbc.m113.510511;
RA Tripathi A., Dewan P.C., Siddique S.A., Varadarajan R.;
RT "MazF-induced growth inhibition and persister generation in Escherichia
RT coli.";
RL J. Biol. Chem. 289:4191-4205(2014).
RN [28]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 585-784, AND ACTIVE SITE LYS-722.
RX PubMed=14665623; DOI=10.1074/jbc.m312243200;
RA Botos I., Melnikov E.E., Cherry S., Tropea J.E., Khalatova A.G.,
RA Rasulova F., Dauter Z., Maurizi M.R., Rotanova T.V., Wlodawer A.,
RA Gustchina A.;
RT "The catalytic domain of Escherichia coli Lon protease has a unique fold
RT and a Ser-Lys dyad in the active site.";
RL J. Biol. Chem. 279:8140-8148(2004).
RN [29]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 491-584.
RX PubMed=15037242; DOI=10.1016/j.jsb.2003.09.003;
RA Botos I., Melnikov E.E., Cherry S., Khalatova A.G., Rasulova F.S.,
RA Tropea J.E., Maurizi M.R., Rotanova T.V., Gustchina A., Wlodawer A.;
RT "Crystal structure of the AAA+ alpha domain of E. coli Lon protease at 1.9A
RT resolution.";
RL J. Struct. Biol. 146:113-122(2004).
RN [30]
RP X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS) OF 1-118.
RX PubMed=16199667; DOI=10.1110/ps.051736805;
RA Li M., Rasulova F., Melnikov E.E., Rotanova T.V., Gustchina A.,
RA Maurizi M.R., Wlodawer A.;
RT "Crystal structure of the N-terminal domain of E. coli Lon protease.";
RL Protein Sci. 14:2895-2900(2005).
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, including some antitoxins. Required for
CC cellular homeostasis and for survival from DNA damage and developmental
CC changes induced by stress. Degrades polypeptides processively to yield
CC small peptide fragments that are 5 to 10 amino acids long. Binds to DNA
CC in a double-stranded, site-specific manner. Endogenous substrates
CC include the regulatory proteins RcsA and SulA, the transcriptional
CC activator SoxS, UmuD and at least type II antitoxins CcdA, HipB and
CC MazE (PubMed:8022284, PubMed:16460757, PubMed:22720069,
CC PubMed:24375411). Its overproduction specifically inhibits translation
CC through at least two different pathways, one of them being the YoeB-
CC YefM toxin-antitoxin system (PubMed:15009896).
CC {ECO:0000269|PubMed:12135363, ECO:0000269|PubMed:15009896,
CC ECO:0000269|PubMed:16460757, ECO:0000269|PubMed:16584195,
CC ECO:0000269|PubMed:19721064, ECO:0000269|PubMed:22720069,
CC ECO:0000269|PubMed:24375411, ECO:0000269|PubMed:8022284}.
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 -!- ACTIVITY REGULATION: Contains an allosteric site (distinct from its
CC active site), whose occupancy by an unfolded polypeptide leads to
CC enzyme activation.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.201 mM for ATP for ATPase activity
CC {ECO:0000269|PubMed:15560777};
CC -!- SUBUNIT: Homohexamer. Organized in a ring with a central cavity. ATP
CC binding and hydrolysis do not affect the oligomeric state of the
CC enzyme. {ECO:0000255|HAMAP-Rule:MF_01973, ECO:0000269|PubMed:16511355}.
CC -!- INTERACTION:
CC P0A9M0; P0A7R1: rplI; NbExp=4; IntAct=EBI-547203, EBI-546437;
CC P0A9M0; P33225: torA; NbExp=2; IntAct=EBI-547203, EBI-557008;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- INDUCTION: By accumulation of abnormal proteins, such as at high
CC temperatures. Under stress conditions.
CC -!- DISRUPTION PHENOTYPE: When both lon and ycgE are disrupted levels of
CC OmpF decrease, leading to lower drug susceptibility, with a greater
CC effect at 26 degrees than at 37 degrees Celsius. The mechanism is not
CC yet understood (PubMed:19721064). Decreased persister cell formation
CC upon antibiotic challenge due probably due to increased levels of MazF
CC toxin (PubMed:24375411). {ECO:0000269|PubMed:19721064,
CC ECO:0000269|PubMed:24375411}.
CC -!- MISCELLANEOUS: Both its proteolytic and protein-activated ATPase
CC activities are stimulated by DNA, especially single-stranded DNA.
CC -!- MISCELLANEOUS: Both high- and low-affinity ATPase sites are present in
CC the homooligomer. Optimal peptidase activity requires ATP binding and
CC hydrolysis at both sites, but ATP hydrolysis is not stoichiometrically
CC linked to peptide hydrolysis.
CC -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000255|HAMAP-
CC Rule:MF_01973}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA23537.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAB40195.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; L12349; AAC36871.1; -; Unassigned_DNA.
DR EMBL; M38347; AAA24079.1; -; Genomic_DNA.
DR EMBL; L20572; AAA16837.1; -; Unassigned_DNA.
DR EMBL; J03896; AAA24078.1; -; Genomic_DNA.
DR EMBL; U82664; AAB40195.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC73542.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76219.1; -; Genomic_DNA.
DR EMBL; M10153; AAA23537.1; ALT_FRAME; Genomic_DNA.
DR PIR; A23101; A23101.
DR PIR; G64773; SUECLA.
DR RefSeq; NP_414973.1; NC_000913.3.
DR RefSeq; WP_001295325.1; NZ_STEB01000007.1.
DR PDB; 1QZM; X-ray; 1.90 A; A=491-584.
DR PDB; 1RR9; X-ray; 2.10 A; A/B/C/D/E/F=585-784.
DR PDB; 1RRE; X-ray; 1.75 A; A/B/C/D/E/F=585-784.
DR PDB; 2ANE; X-ray; 2.03 A; A/B/C/D/E/F/G/H=1-118.
DR PDB; 3LJC; X-ray; 2.60 A; A=1-245.
DR PDB; 6N2I; X-ray; 3.50 A; A=241-584.
DR PDB; 6U5Z; EM; 3.50 A; A/B/C/D/E/F=1-784.
DR PDBsum; 1QZM; -.
DR PDBsum; 1RR9; -.
DR PDBsum; 1RRE; -.
DR PDBsum; 2ANE; -.
DR PDBsum; 3LJC; -.
DR PDBsum; 6N2I; -.
DR PDBsum; 6U5Z; -.
DR AlphaFoldDB; P0A9M0; -.
DR BMRB; P0A9M0; -.
DR SMR; P0A9M0; -.
DR BioGRID; 4260734; 201.
DR BioGRID; 849474; 1.
DR DIP; DIP-35845N; -.
DR IntAct; P0A9M0; 72.
DR MINT; P0A9M0; -.
DR STRING; 511145.b0439; -.
DR MEROPS; S16.001; -.
DR jPOST; P0A9M0; -.
DR PaxDb; P0A9M0; -.
DR PRIDE; P0A9M0; -.
DR EnsemblBacteria; AAC73542; AAC73542; b0439.
DR EnsemblBacteria; BAE76219; BAE76219; BAE76219.
DR GeneID; 67416486; -.
DR GeneID; 945085; -.
DR KEGG; ecj:JW0429; -.
DR KEGG; eco:b0439; -.
DR PATRIC; fig|1411691.4.peg.1837; -.
DR EchoBASE; EB0537; -.
DR eggNOG; COG0466; Bacteria.
DR HOGENOM; CLU_004109_4_3_6; -.
DR InParanoid; P0A9M0; -.
DR OMA; GAWQVVD; -.
DR PhylomeDB; P0A9M0; -.
DR BioCyc; EcoCyc:EG10542-MON; -.
DR BioCyc; MetaCyc:EG10542-MON; -.
DR BRENDA; 3.4.21.53; 2026.
DR BRENDA; 3.6.4.7; 2026.
DR SABIO-RK; P0A9M0; -.
DR EvolutionaryTrace; P0A9M0; -.
DR PRO; PR:P0A9M0; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:EcoliWiki.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IDA:EcoCyc.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:EcoliWiki.
DR GO; GO:0004176; F:ATP-dependent peptidase activity; IDA:EcoliWiki.
DR GO; GO:0003677; F:DNA binding; IDA:EcoliWiki.
DR GO; GO:0008233; F:peptidase activity; IDA:EcoliWiki.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IMP:EcoliWiki.
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; IMP:EcoCyc.
DR GO; GO:0006508; P:proteolysis; IDA:EcoliWiki.
DR GO; GO:0009408; P:response to heat; IEP:EcoliWiki.
DR GO; GO:0010165; P:response to X-ray; IMP:EcoCyc.
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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Direct protein sequencing; Hydrolase;
KW Nucleotide-binding; Protease; Reference proteome; Serine protease;
KW Stress response.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8995294"
FT CHAIN 2..784
FT /note="Lon protease"
FT /id="PRO_0000076133"
FT DOMAIN 11..202
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 592..773
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT ACT_SITE 679
FT ACT_SITE 722
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973,
FT ECO:0000269|PubMed:14665623"
FT BINDING 356..363
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT MUTAGEN 362
FT /note="K->A: Loss of proteolytic activity and ATP-binding.
FT No increased persister cell formation."
FT /evidence="ECO:0000269|PubMed:7988699"
FT MUTAGEN 665
FT /note="H->Y: Loss of proteolytic activity."
FT /evidence="ECO:0000269|PubMed:9490010"
FT MUTAGEN 667
FT /note="H->Y: Loss of proteolytic activity."
FT /evidence="ECO:0000269|PubMed:9490010"
FT MUTAGEN 676
FT /note="D->N: Loss of proteolytic activity."
FT /evidence="ECO:0000269|PubMed:9490010"
FT MUTAGEN 679
FT /note="S->A: Loss of proteolytic activity. No increased
FT persister cell formation."
FT /evidence="ECO:0000269|PubMed:8226758"
FT MUTAGEN 743
FT /note="D->N: No effect."
FT /evidence="ECO:0000269|PubMed:9490010"
FT CONFLICT 264..317
FT /note="PKEAKEKAEAELQKLKMMSPMSAEATVVRGYIDWMVQVPWNARSKVKKDLRQ
FT AQ -> RKRQKRKRTGVAEAENDVSDVGRSDRSAWLYRLDGTGAVECAYEGQKRPASGA
FT (in Ref. 5; AAA24078)"
FT /evidence="ECO:0000305"
FT CONFLICT 273
FT /note="A -> R (in Ref. 4; AAA16837)"
FT /evidence="ECO:0000305"
FT CONFLICT 307
FT /note="S -> T (in Ref. 4; AAA16837)"
FT /evidence="ECO:0000305"
FT CONFLICT 539..563
FT /note="AGVRGLEREISKLCRKAVKQLLLDK -> RACVVWSVKSPNCVAKRLSSYCS
FT IT (in Ref. 5; AAA24078)"
FT /evidence="ECO:0000305"
FT CONFLICT 772
FT /note="Q -> R (in Ref. 4; AAA16837)"
FT /evidence="ECO:0000305"
FT CONFLICT 779..784
FT /note="QVVTAK -> HHSLRRRCSTASTYYWAKS (in Ref. 2; AAA24079)"
FT /evidence="ECO:0000305"
FT STRAND 9..18
FT /evidence="ECO:0007829|PDB:2ANE"
FT STRAND 26..31
FT /evidence="ECO:0007829|PDB:2ANE"
FT HELIX 34..44
FT /evidence="ECO:0007829|PDB:2ANE"
FT TURN 45..47
FT /evidence="ECO:0007829|PDB:2ANE"
FT STRAND 48..55
FT /evidence="ECO:0007829|PDB:2ANE"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:2ANE"
FT STRAND 70..82
FT /evidence="ECO:0007829|PDB:2ANE"
FT STRAND 88..105
FT /evidence="ECO:0007829|PDB:2ANE"
FT STRAND 107..116
FT /evidence="ECO:0007829|PDB:2ANE"
FT HELIX 124..145
FT /evidence="ECO:0007829|PDB:3LJC"
FT HELIX 150..155
FT /evidence="ECO:0007829|PDB:3LJC"
FT HELIX 162..171
FT /evidence="ECO:0007829|PDB:3LJC"
FT HELIX 177..185
FT /evidence="ECO:0007829|PDB:3LJC"
FT HELIX 189..242
FT /evidence="ECO:0007829|PDB:3LJC"
FT TURN 250..259
FT /evidence="ECO:0007829|PDB:6N2I"
FT HELIX 268..276
FT /evidence="ECO:0007829|PDB:6N2I"
FT HELIX 287..299
FT /evidence="ECO:0007829|PDB:6N2I"
FT HELIX 314..320
FT /evidence="ECO:0007829|PDB:6N2I"
FT TURN 321..324
FT /evidence="ECO:0007829|PDB:6N2I"
FT TURN 327..330
FT /evidence="ECO:0007829|PDB:6N2I"
FT HELIX 331..340
FT /evidence="ECO:0007829|PDB:6N2I"
FT STRAND 343..345
FT /evidence="ECO:0007829|PDB:6N2I"
FT STRAND 353..355
FT /evidence="ECO:0007829|PDB:6N2I"
FT STRAND 360..362
FT /evidence="ECO:0007829|PDB:6N2I"
FT HELIX 363..372
FT /evidence="ECO:0007829|PDB:6N2I"
FT STRAND 376..381
FT /evidence="ECO:0007829|PDB:6N2I"
FT TURN 389..391
FT /evidence="ECO:0007829|PDB:6N2I"
FT HELIX 405..412
FT /evidence="ECO:0007829|PDB:6N2I"
FT STRAND 415..423
FT /evidence="ECO:0007829|PDB:6N2I"
FT STRAND 431..434
FT /evidence="ECO:0007829|PDB:6N2I"
FT HELIX 436..444
FT /evidence="ECO:0007829|PDB:6N2I"
FT TURN 446..448
FT /evidence="ECO:0007829|PDB:6N2I"
FT HELIX 449..451
FT /evidence="ECO:0007829|PDB:6U5Z"
FT STRAND 455..457
FT /evidence="ECO:0007829|PDB:6N2I"
FT STRAND 459..461
FT /evidence="ECO:0007829|PDB:6N2I"
FT STRAND 467..471
FT /evidence="ECO:0007829|PDB:6N2I"
FT STRAND 473..475
FT /evidence="ECO:0007829|PDB:6N2I"
FT HELIX 479..482
FT /evidence="ECO:0007829|PDB:6N2I"
FT STRAND 487..489
FT /evidence="ECO:0007829|PDB:6N2I"
FT HELIX 495..504
FT /evidence="ECO:0007829|PDB:1QZM"
FT HELIX 506..513
FT /evidence="ECO:0007829|PDB:1QZM"
FT TURN 518..520
FT /evidence="ECO:0007829|PDB:1QZM"
FT STRAND 521..523
FT /evidence="ECO:0007829|PDB:1QZM"
FT HELIX 525..535
FT /evidence="ECO:0007829|PDB:1QZM"
FT STRAND 539..541
FT /evidence="ECO:0007829|PDB:1QZM"
FT HELIX 542..560
FT /evidence="ECO:0007829|PDB:1QZM"
FT STRAND 568..570
FT /evidence="ECO:0007829|PDB:1QZM"
FT TURN 572..574
FT /evidence="ECO:0007829|PDB:1QZM"
FT HELIX 575..579
FT /evidence="ECO:0007829|PDB:1QZM"
FT STRAND 596..604
FT /evidence="ECO:0007829|PDB:1RRE"
FT STRAND 607..619
FT /evidence="ECO:0007829|PDB:1RRE"
FT STRAND 624..630
FT /evidence="ECO:0007829|PDB:1RRE"
FT HELIX 632..647
FT /evidence="ECO:0007829|PDB:1RRE"
FT HELIX 649..652
FT /evidence="ECO:0007829|PDB:1RRE"
FT TURN 656..660
FT /evidence="ECO:0007829|PDB:1RRE"
FT STRAND 661..667
FT /evidence="ECO:0007829|PDB:1RRE"
FT TURN 669..672
FT /evidence="ECO:0007829|PDB:6U5Z"
FT STRAND 675..678
FT /evidence="ECO:0007829|PDB:1RRE"
FT HELIX 681..693
FT /evidence="ECO:0007829|PDB:1RRE"
FT STRAND 701..703
FT /evidence="ECO:0007829|PDB:1RRE"
FT STRAND 705..707
FT /evidence="ECO:0007829|PDB:6U5Z"
FT STRAND 712..714
FT /evidence="ECO:0007829|PDB:1RRE"
FT HELIX 719..728
FT /evidence="ECO:0007829|PDB:1RRE"
FT STRAND 733..737
FT /evidence="ECO:0007829|PDB:1RRE"
FT HELIX 738..746
FT /evidence="ECO:0007829|PDB:1RRE"
FT HELIX 749..754
FT /evidence="ECO:0007829|PDB:1RRE"
FT STRAND 755..762
FT /evidence="ECO:0007829|PDB:1RRE"
FT HELIX 763..770
FT /evidence="ECO:0007829|PDB:1RRE"
FT STRAND 771..773
FT /evidence="ECO:0007829|PDB:1RRE"
SQ SEQUENCE 784 AA; 87438 MW; 4042499C97694EF8 CRC64;
MNPERSERIE IPVLPLRDVV VYPHMVIPLF VGREKSIRCL EAAMDHDKKI MLVAQKEAST
DEPGVNDLFT VGTVASILQM LKLPDGTVKV LVEGLQRARI SALSDNGEHF SAKAEYLESP
TIDEREQEVL VRTAISQFEG YIKLNKKIPP EVLTSLNSID DPARLADTIA AHMPLKLADK
QSVLEMSDVN ERLEYLMAMM ESEIDLLQVE KRIRNRVKKQ MEKSQREYYL NEQMKAIQKE
LGEMDDAPDE NEALKRKIDA AKMPKEAKEK AEAELQKLKM MSPMSAEATV VRGYIDWMVQ
VPWNARSKVK KDLRQAQEIL DTDHYGLERV KDRILEYLAV QSRVNKIKGP ILCLVGPPGV
GKTSLGQSIA KATGRKYVRM ALGGVRDEAE IRGHRRTYIG SMPGKLIQKM AKVGVKNPLF
LLDEIDKMSS DMRGDPASAL LEVLDPEQNV AFSDHYLEVD YDLSDVMFVA TSNSMNIPAP
LLDRMEVIRL SGYTEDEKLN IAKRHLLPKQ IERNALKKGE LTVDDSAIIG IIRYYTREAG
VRGLEREISK LCRKAVKQLL LDKSLKHIEI NGDNLHDYLG VQRFDYGRAD NENRVGQVTG
LAWTEVGGDL LTIETACVPG KGKLTYTGSL GEVMQESIQA ALTVVRARAE KLGINPDFYE
KRDIHVHVPE GATPKDGPSA GIAMCTALVS CLTGNPVRAD VAMTGEITLR GQVLPIGGLK
EKLLAAHRGG IKTVLIPFEN KRDLEEIPDN VIADLDIHPV KRIEEVLTLA LQNEPSGMQV
VTAK
