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Protein

Lon protease

Gene

lon

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins, including some antitoxins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner. Endogenous substrates include the regulatory proteins RcsA and SulA, the transcriptional activator SoxS, UmuD and antitoxins CcdA, HipB and MazE (PubMed:8022284, PubMed:16460757, PubMed:22720069, PubMed:24375411). Its overproduction specifically inhibits translation through at least two different pathways, one of them being the YoeB-YefM toxin-antitoxin system (PubMed:15009896).8 Publications

Catalytic activityi

Hydrolysis of proteins in presence of ATP.UniRule annotation

Enzyme regulationi

Contains an allosteric site (distinct from its active site), whose occupancy by an unfolded polypeptide leads to enzyme activation.

Kineticsi

  1. KM=0.201 mM for ATP for ATPase activity1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei679 – 6791
    Active sitei722 – 7221UniRule annotation1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi356 – 3638ATPUniRule annotation

    GO - Molecular functioni

    • ATPase activity Source: EcoliWiki
    • ATP binding Source: EcoCyc
    • ATP-dependent peptidase activity Source: EcoliWiki
    • DNA binding Source: EcoliWiki
    • peptidase activity Source: EcoliWiki
    • sequence-specific DNA binding Source: UniProtKB-HAMAP
    • serine-type endopeptidase activity Source: EcoliWiki

    GO - Biological processi

    • cellular response to stress Source: UniProtKB-HAMAP
    • misfolded or incompletely synthesized protein catabolic process Source: EcoCyc
    • proteolysis Source: EcoliWiki
    • response to heat Source: EcoliWiki
    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase, Protease, Serine protease

    Keywords - Biological processi

    Stress response

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:EG10542-MONOMER.
    ECOL316407:JW0429-MONOMER.
    MetaCyc:EG10542-MONOMER.
    BRENDAi3.4.21.53. 2026.

    Protein family/group databases

    MEROPSiS16.001.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lon proteaseUniRule annotation (EC:3.4.21.53UniRule annotation)
    Alternative name(s):
    ATP-dependent protease LaUniRule annotation
    Gene namesi
    Name:lonUniRule annotation
    Synonyms:capR, deg, lopA, muc
    Ordered Locus Names:b0439, JW0429
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG10542. lon.

    Subcellular locationi

    GO - Cellular componenti

    • cytoplasm Source: EcoliWiki
    • cytosol Source: EcoCyc
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Disruption phenotypei

    When both lon and ycgE are disrupted levels of OmpF decrease, leading to lower drug susceptibility, with a greater effect at 26 degrees than at 37 degrees Celsius. The mechanism is not yet understood (PubMed:19721064). Decreased persister cell formation upon antibiotic challenge due probably due to increased levels of MazF toxin (PubMed:24375411).2 Publications

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi362 – 3621K → A: Loss of proteolytic activity and ATP-binding. 1 Publication
    Mutagenesisi665 – 6651H → Y: Loss of proteolytic activity. 1 Publication
    Mutagenesisi667 – 6671H → Y: Loss of proteolytic activity. 1 Publication
    Mutagenesisi676 – 6761D → N: Loss of proteolytic activity. 1 Publication
    Mutagenesisi679 – 6791S → A: Loss of proteolytic activity. 1 Publication
    Mutagenesisi743 – 7431D → N: No effect. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methionineiRemovedUniRule annotation1 Publication
    Chaini2 – 784783Lon proteasePRO_0000076133Add
    BLAST

    Proteomic databases

    PaxDbiP0A9M0.
    PRIDEiP0A9M0.

    Expressioni

    Inductioni

    By accumulation of abnormal proteins, such as at high temperatures. Under stress conditions.

    Interactioni

    Subunit structurei

    Homohexamer. Organized in a ring with a central cavity. ATP binding and hydrolysis do not affect the oligomeric state of the enzyme.UniRule annotation1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    torAP332252EBI-547203,EBI-557008

    Protein-protein interaction databases

    BioGridi4260734. 24 interactions.
    DIPiDIP-35845N.
    IntActiP0A9M0. 69 interactions.
    MINTiMINT-1224190.
    STRINGi511145.b0439.

    Structurei

    Secondary structure

    1
    784
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi9 – 1810Combined sources
    Beta strandi26 – 316Combined sources
    Helixi34 – 4411Combined sources
    Turni45 – 473Combined sources
    Beta strandi48 – 558Combined sources
    Helixi65 – 673Combined sources
    Beta strandi70 – 8213Combined sources
    Beta strandi88 – 10518Combined sources
    Beta strandi107 – 11610Combined sources
    Helixi124 – 14522Combined sources
    Helixi150 – 1556Combined sources
    Helixi162 – 17110Combined sources
    Helixi177 – 1859Combined sources
    Helixi189 – 24254Combined sources
    Helixi495 – 50410Combined sources
    Helixi506 – 5138Combined sources
    Turni518 – 5203Combined sources
    Beta strandi521 – 5233Combined sources
    Helixi525 – 53511Combined sources
    Beta strandi539 – 5413Combined sources
    Helixi542 – 56019Combined sources
    Beta strandi568 – 5703Combined sources
    Turni572 – 5743Combined sources
    Helixi575 – 5795Combined sources
    Beta strandi596 – 6049Combined sources
    Beta strandi607 – 61913Combined sources
    Beta strandi624 – 6307Combined sources
    Helixi632 – 64716Combined sources
    Helixi649 – 6524Combined sources
    Turni656 – 6605Combined sources
    Beta strandi661 – 6677Combined sources
    Beta strandi675 – 6784Combined sources
    Helixi681 – 69313Combined sources
    Beta strandi701 – 7033Combined sources
    Beta strandi712 – 7143Combined sources
    Helixi719 – 72810Combined sources
    Beta strandi733 – 7375Combined sources
    Helixi738 – 7469Combined sources
    Helixi749 – 7546Combined sources
    Beta strandi755 – 7628Combined sources
    Helixi763 – 7708Combined sources
    Beta strandi771 – 7733Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1QZMX-ray1.90A491-584[»]
    1RR9X-ray2.10A/B/C/D/E/F585-784[»]
    1RREX-ray1.75A/B/C/D/E/F585-784[»]
    2ANEX-ray2.03A/B/C/D/E/F/G/H1-118[»]
    3LJCX-ray2.60A1-245[»]
    ProteinModelPortaliP0A9M0.
    SMRiP0A9M0. Positions 7-245, 250-784.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A9M0.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini11 – 202192Lon N-terminalPROSITE-ProRule annotationAdd
    BLAST
    Domaini592 – 773182Lon proteolyticPROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi211 – 2199Arg/Lys-rich (basic)
    Compositional biasi240 – 25213Asp/Glu-rich (acidic)Add
    BLAST
    Compositional biasi255 – 27016Arg/Lys-rich (basic)Add
    BLAST

    Sequence similaritiesi

    Belongs to the peptidase S16 family.UniRule annotation
    Contains 1 Lon N-terminal domain.PROSITE-ProRule annotation
    Contains 1 Lon proteolytic domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiENOG4105C6P. Bacteria.
    COG0466. LUCA.
    HOGENOMiHOG000261408.
    InParanoidiP0A9M0.
    KOiK01338.
    OMAiGIKKAGM.
    OrthoDBiEOG6XHC23.
    PhylomeDBiP0A9M0.

    Family and domain databases

    Gene3Di3.30.230.10. 1 hit.
    3.40.50.300. 1 hit.
    HAMAPiMF_01973. lon_bact.
    InterProiIPR003593. AAA+_ATPase.
    IPR003959. ATPase_AAA_core.
    IPR027543. Lon_bac.
    IPR004815. Lon_bac/euk-typ.
    IPR027065. Lon_Prtase.
    IPR003111. LON_substr-bd_dom.
    IPR027417. P-loop_NTPase.
    IPR008269. Pept_S16_C.
    IPR008268. Peptidase_S16_AS.
    IPR015947. PUA-like_domain.
    IPR020568. Ribosomal_S5_D2-typ_fold.
    IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
    [Graphical view]
    PANTHERiPTHR10046. PTHR10046. 1 hit.
    PfamiPF00004. AAA. 1 hit.
    PF05362. Lon_C. 1 hit.
    PF02190. LON_substr_bdg. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001174. Lon_proteas. 1 hit.
    SMARTiSM00382. AAA. 1 hit.
    SM00464. LON. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    SSF54211. SSF54211. 1 hit.
    SSF88697. SSF88697. 1 hit.
    TIGRFAMsiTIGR00763. lon. 1 hit.
    PROSITEiPS51787. LON_N. 1 hit.
    PS51786. LON_PROTEOLYTIC. 1 hit.
    PS01046. LON_SER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P0A9M0-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MNPERSERIE IPVLPLRDVV VYPHMVIPLF VGREKSIRCL EAAMDHDKKI
    60 70 80 90 100
    MLVAQKEAST DEPGVNDLFT VGTVASILQM LKLPDGTVKV LVEGLQRARI
    110 120 130 140 150
    SALSDNGEHF SAKAEYLESP TIDEREQEVL VRTAISQFEG YIKLNKKIPP
    160 170 180 190 200
    EVLTSLNSID DPARLADTIA AHMPLKLADK QSVLEMSDVN ERLEYLMAMM
    210 220 230 240 250
    ESEIDLLQVE KRIRNRVKKQ MEKSQREYYL NEQMKAIQKE LGEMDDAPDE
    260 270 280 290 300
    NEALKRKIDA AKMPKEAKEK AEAELQKLKM MSPMSAEATV VRGYIDWMVQ
    310 320 330 340 350
    VPWNARSKVK KDLRQAQEIL DTDHYGLERV KDRILEYLAV QSRVNKIKGP
    360 370 380 390 400
    ILCLVGPPGV GKTSLGQSIA KATGRKYVRM ALGGVRDEAE IRGHRRTYIG
    410 420 430 440 450
    SMPGKLIQKM AKVGVKNPLF LLDEIDKMSS DMRGDPASAL LEVLDPEQNV
    460 470 480 490 500
    AFSDHYLEVD YDLSDVMFVA TSNSMNIPAP LLDRMEVIRL SGYTEDEKLN
    510 520 530 540 550
    IAKRHLLPKQ IERNALKKGE LTVDDSAIIG IIRYYTREAG VRGLEREISK
    560 570 580 590 600
    LCRKAVKQLL LDKSLKHIEI NGDNLHDYLG VQRFDYGRAD NENRVGQVTG
    610 620 630 640 650
    LAWTEVGGDL LTIETACVPG KGKLTYTGSL GEVMQESIQA ALTVVRARAE
    660 670 680 690 700
    KLGINPDFYE KRDIHVHVPE GATPKDGPSA GIAMCTALVS CLTGNPVRAD
    710 720 730 740 750
    VAMTGEITLR GQVLPIGGLK EKLLAAHRGG IKTVLIPFEN KRDLEEIPDN
    760 770 780
    VIADLDIHPV KRIEEVLTLA LQNEPSGMQV VTAK
    Length:784
    Mass (Da):87,438
    Last modified:July 19, 2005 - v1
    Checksum:i4042499C97694EF8
    GO

    Sequence cautioni

    The sequence AAA23537.1 differs from that shown. Reason: Frameshift at position 16. Curated
    The sequence AAB40195.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti264 – 31754PKEAK…LRQAQ → RKRQKRKRTGVAEAENDVSD VGRSDRSAWLYRLDGTGAVE CAYEGQKRPASGA in AAA24078 (PubMed:3042779).CuratedAdd
    BLAST
    Sequence conflicti273 – 2731A → R in AAA16837 (PubMed:8226758).Curated
    Sequence conflicti307 – 3071S → T in AAA16837 (PubMed:8226758).Curated
    Sequence conflicti539 – 56325AGVRG…LLLDK → RACVVWSVKSPNCVAKRLSS YCSIT in AAA24078 (PubMed:3042779).CuratedAdd
    BLAST
    Sequence conflicti772 – 7721Q → R in AAA16837 (PubMed:8226758).Curated
    Sequence conflicti779 – 7846QVVTAK → HHSLRRRCSTASTYYWAKS in AAA24079 (PubMed:3289547).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    L12349 Unassigned DNA. Translation: AAC36871.1.
    M38347 Genomic DNA. Translation: AAA24079.1.
    L20572 Unassigned DNA. Translation: AAA16837.1.
    J03896 Genomic DNA. Translation: AAA24078.1.
    U82664 Genomic DNA. Translation: AAB40195.1. Different initiation.
    U00096 Genomic DNA. Translation: AAC73542.1.
    AP009048 Genomic DNA. Translation: BAE76219.1.
    M10153 Genomic DNA. Translation: AAA23537.1. Frameshift.
    PIRiA23101.
    G64773. SUECLA.
    RefSeqiNP_414973.1. NC_000913.3.
    WP_001295325.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC73542; AAC73542; b0439.
    BAE76219; BAE76219; BAE76219.
    GeneIDi945085.
    KEGGiecj:JW0429.
    eco:b0439.
    PATRICi32116031. VBIEscCol129921_0457.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    L12349 Unassigned DNA. Translation: AAC36871.1.
    M38347 Genomic DNA. Translation: AAA24079.1.
    L20572 Unassigned DNA. Translation: AAA16837.1.
    J03896 Genomic DNA. Translation: AAA24078.1.
    U82664 Genomic DNA. Translation: AAB40195.1. Different initiation.
    U00096 Genomic DNA. Translation: AAC73542.1.
    AP009048 Genomic DNA. Translation: BAE76219.1.
    M10153 Genomic DNA. Translation: AAA23537.1. Frameshift.
    PIRiA23101.
    G64773. SUECLA.
    RefSeqiNP_414973.1. NC_000913.3.
    WP_001295325.1. NZ_LN832404.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1QZMX-ray1.90A491-584[»]
    1RR9X-ray2.10A/B/C/D/E/F585-784[»]
    1RREX-ray1.75A/B/C/D/E/F585-784[»]
    2ANEX-ray2.03A/B/C/D/E/F/G/H1-118[»]
    3LJCX-ray2.60A1-245[»]
    ProteinModelPortaliP0A9M0.
    SMRiP0A9M0. Positions 7-245, 250-784.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4260734. 24 interactions.
    DIPiDIP-35845N.
    IntActiP0A9M0. 69 interactions.
    MINTiMINT-1224190.
    STRINGi511145.b0439.

    Protein family/group databases

    MEROPSiS16.001.

    Proteomic databases

    PaxDbiP0A9M0.
    PRIDEiP0A9M0.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC73542; AAC73542; b0439.
    BAE76219; BAE76219; BAE76219.
    GeneIDi945085.
    KEGGiecj:JW0429.
    eco:b0439.
    PATRICi32116031. VBIEscCol129921_0457.

    Organism-specific databases

    EchoBASEiEB0537.
    EcoGeneiEG10542. lon.

    Phylogenomic databases

    eggNOGiENOG4105C6P. Bacteria.
    COG0466. LUCA.
    HOGENOMiHOG000261408.
    InParanoidiP0A9M0.
    KOiK01338.
    OMAiGIKKAGM.
    OrthoDBiEOG6XHC23.
    PhylomeDBiP0A9M0.

    Enzyme and pathway databases

    BioCyciEcoCyc:EG10542-MONOMER.
    ECOL316407:JW0429-MONOMER.
    MetaCyc:EG10542-MONOMER.
    BRENDAi3.4.21.53. 2026.

    Miscellaneous databases

    EvolutionaryTraceiP0A9M0.
    PROiP0A9M0.

    Family and domain databases

    Gene3Di3.30.230.10. 1 hit.
    3.40.50.300. 1 hit.
    HAMAPiMF_01973. lon_bact.
    InterProiIPR003593. AAA+_ATPase.
    IPR003959. ATPase_AAA_core.
    IPR027543. Lon_bac.
    IPR004815. Lon_bac/euk-typ.
    IPR027065. Lon_Prtase.
    IPR003111. LON_substr-bd_dom.
    IPR027417. P-loop_NTPase.
    IPR008269. Pept_S16_C.
    IPR008268. Peptidase_S16_AS.
    IPR015947. PUA-like_domain.
    IPR020568. Ribosomal_S5_D2-typ_fold.
    IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
    [Graphical view]
    PANTHERiPTHR10046. PTHR10046. 1 hit.
    PfamiPF00004. AAA. 1 hit.
    PF05362. Lon_C. 1 hit.
    PF02190. LON_substr_bdg. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001174. Lon_proteas. 1 hit.
    SMARTiSM00382. AAA. 1 hit.
    SM00464. LON. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    SSF54211. SSF54211. 1 hit.
    SSF88697. SSF88697. 1 hit.
    TIGRFAMsiTIGR00763. lon. 1 hit.
    PROSITEiPS51787. LON_N. 1 hit.
    PS51786. LON_PROTEOLYTIC. 1 hit.
    PS01046. LON_SER. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Controlled high-level expression of the lon gene of Escherichia coli allows overproduction of Lon protease."
      Thomas C.D., Modha J., Razzaq T.M., Cullis P.M., Rivett A.
      Gene 136:237-242(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
    2. "Cloning, expression and structure of the functionally active shortened lon gene in Escherichia coli."
      Amerik A.Y., Chistyakova L.G., Ostroumova N.I., Gurevich A.I., Antonov V.K.
      Bioorg. Khim. 14:408-411(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Cloning, structure and expression of the full-size lon gene in Escherichia coli coding for ATP-dependent La-proteinase."
      Amerik A.I.U., Antonov V.K., Ostroumova N.I., Rotanova T.V., Chistiakova L.G.
      Bioorg. Khim. 16:869-880(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12.
    4. "ATP hydrolysis is not stoichiometrically linked with proteolysis in the ATP-dependent protease La from Escherichia coli."
      Fischer H., Glockshuber R.
      J. Biol. Chem. 268:22502-22507(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF SER-679.
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    5. "Sequence of the lon gene in Escherichia coli. A heat-shock gene which encodes the ATP-dependent protease La."
      Chin D.T., Goff S.A., Webster T., Smith T., Goldberg A.L.
      J. Biol. Chem. 263:11718-11728(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 783-783.
    6. "Sequence of minutes 4-25 of Escherichia coli."
      Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
      Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    8. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    9. "Regulatory region of the heat shock-inducible capR (lon) gene: DNA and protein sequences."
      Gayda R.C., Stephens P.E., Hewick R., Schoemaker J.M., Dreyer W.J., Markovitz A.
      J. Bacteriol. 162:271-275(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-58, PROTEIN SEQUENCE OF 1-14.
    10. "Bacterial protease Lon is a site-specific DNA-binding protein."
      Fu G.K., Smith M.J., Markovitz D.M.
      J. Biol. Chem. 272:534-538(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-9, DNA-BINDING.
      Strain: ATCC 37196 / Y1089.
    11. "A point mutation within the ATP-binding site inactivates both catalytic functions of the ATP-dependent protease La (Lon) from Escherichia coli."
      Fischer H., Glockshuber R.
      FEBS Lett. 356:101-103(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF LYS-362.
    12. "Lon-dependent proteolysis of CcdA is the key control for activation of CcdB in plasmid-free segregant bacteria."
      Van Melderen L., Bernard P., Couturier M.
      Mol. Microbiol. 11:1151-1157(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: CLEAVAGE OF CCDA ANTITOXIN.
      Strain: K12.
    13. "Escherichia coli proteome analysis using the gene-protein database."
      VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
      Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY 2D-GEL.
    14. "Mutations in the proteolytic domain of Escherichia coli protease Lon impair the ATPase activity of the enzyme."
      Starkova N.N., Koroleva E.P., Rumsh L.D., Ginodman L.M., Rotanova T.V.
      FEBS Lett. 422:218-220(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF HIS-665; HIS-667; ASP-676 AND ASP-743.
    15. "Lon-mediated proteolysis of the Escherichia coli UmuD mutagenesis protein: in vitro degradation and identification of residues required for proteolysis."
      Gonzalez M., Frank E.G., Levine A.S., Woodgate R.
      Genes Dev. 12:3889-3899(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: CLEAVAGE OF UMUD.
    16. "A conserved domain in Escherichia coli Lon protease is involved in substrate discriminator activity."
      Ebel W., Skinner M.M., Dierksen K.P., Scott J.M., Trempy J.E.
      J. Bacteriol. 181:2236-2243(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS.
    17. "Kinetic characterization of the peptidase activity of Escherichia coli Lon reveals the mechanistic similarities in ATP-dependent hydrolysis of peptide and protein substrates."
      Thomas-Wohlever J., Lee I.
      Biochemistry 41:9418-9425(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    18. "The Thermoplasma acidophilum Lon protease has a Ser-Lys dyad active site."
      Besche H., Zwickl P.
      Eur. J. Biochem. 271:4361-4365(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: BIOPHYSICOCHEMICAL PROPERTIES.
    19. "Overproduction of the Lon protease triggers inhibition of translation in Escherichia coli: involvement of the yefM-yoeB toxin-antitoxin system."
      Christensen S.K., Maenhaut-Michel G., Mine N., Gottesman S., Gerdes K., Van Melderen L.
      Mol. Microbiol. 51:1705-1717(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH THE YOEB-YEFM TOXIN-ANTITOXIN SYSTEM.
      Strain: K12 / MG1655 / ATCC 47076.
    20. "Single-turnover kinetic experiments confirm the existence of high- and low-affinity ATPase sites in Escherichia coli Lon protease."
      Vineyard D., Patterson-Ward J., Lee I.
      Biochemistry 45:4602-4610(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    21. "Sequence requirements for Lon-dependent degradation of the Escherichia coli transcription activator SoxS: identification of the SoxS residues critical to proteolysis and specific inhibition of in vitro degradation by a peptide comprised of the N-terminal 21 amino acid residues."
      Shah I.M., Wolf R.E. Jr.
      J. Mol. Biol. 357:718-731(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: CLEAVAGE OF SOXS.
    22. "Oligomeric structure of the ATP-dependent protease La (Lon) of Escherichia coli."
      Park S.C., Jia B., Yang J.K., Van D.L., Shao Y.G., Han S.W., Jeon Y.J., Chung C.H., Cheong G.W.
      Mol. Cells 21:129-134(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.
    23. "Combined inactivation of lon and ycgE decreases multidrug susceptibility by reducing the amount of OmpF porin in Escherichia coli."
      Duval V., Nicoloff H., Levy S.B.
      Antimicrob. Agents Chemother. 53:4944-4948(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ROLE IN REGULATION OF OMPF IN ASSOCIATION WITH YCGE, DISRUPTION PHENOTYPE.
      Strain: K12 / AG100.
    24. "Regulation of the Escherichia coli HipBA toxin-antitoxin system by proteolysis."
      Hansen S., Vulic M., Min J., Yen T.J., Schumacher M.A., Brennan R.G., Lewis K.
      PLoS ONE 7:E39185-E39185(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: CLEAVAGE OF HIPB ANTITOXIN.
    25. "MazF-induced growth inhibition and persister generation in Escherichia coli."
      Tripathi A., Dewan P.C., Siddique S.A., Varadarajan R.
      J. Biol. Chem. 289:4191-4205(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: CLEAVAGE OF ANTITOXIN MAZE, DISRUPTION PHENOTYPE.
      Strain: K12 / BW25113 and K12 / MC4100 / ATCC 35695 / DSM 6574.
    26. "The catalytic domain of Escherichia coli Lon protease has a unique fold and a Ser-Lys dyad in the active site."
      Botos I., Melnikov E.E., Cherry S., Tropea J.E., Khalatova A.G., Rasulova F., Dauter Z., Maurizi M.R., Rotanova T.V., Wlodawer A., Gustchina A.
      J. Biol. Chem. 279:8140-8148(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 585-784, ACTIVE SITE LYS-722.
    27. Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 491-584.
    28. "Crystal structure of the N-terminal domain of E. coli Lon protease."
      Li M., Rasulova F., Melnikov E.E., Rotanova T.V., Gustchina A., Maurizi M.R., Wlodawer A.
      Protein Sci. 14:2895-2900(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS) OF 1-118.

    Entry informationi

    Entry nameiLON_ECOLI
    AccessioniPrimary (citable) accession number: P0A9M0
    Secondary accession number(s): P08177, P78219, Q2MBY7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: July 19, 2005
    Last modified: March 16, 2016
    This is version 108 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Both its proteolytic and protein-activated ATPase activities are stimulated by DNA, especially single-stranded DNA.
    Both high- and low-affinity ATPase sites are present in the homooligomer. Optimal peptidase activity requires ATP binding and hydrolysis at both sites, but ATP hydrolysis is not stoichiometrically linked to peptide hydrolysis.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. Peptidase families
      Classification of peptidase families and list of entries
    4. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.