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UniProtKB - P0A9M0 (LON_ECOLI)

Entry version 141 (07 Oct 2020)
Sequence version 1 (19 Jul 2005)
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Protein

Lon protease

Gene

lon

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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 at least type II 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). Overproduction leads to very high persister cell formation (cells highly resistant to antibiotics), but not when 10 mRNA interferases are deleted, nor when Lon catalytic residues are mutated (PubMed:21788497).9 Publications

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.

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

  • Hydrolysis of proteins in presence of ATP.UniRule annotation EC:3.4.21.53

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

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

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

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

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei6791
    Active sitei722UniRule annotation1 Publication1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi356 – 363ATPUniRule annotation8

    <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

    Complete GO annotation on QuickGO ...

    GO - Biological processi

    Complete GO annotation on QuickGO ...

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular functionHydrolase, Protease, Serine protease
    Biological processStress response
    LigandATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...    BioCyci    		EcoCyc:EG10542-MONOMER
    MetaCyc:EG10542-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...    BRENDAi    		3.4.21.53, 2026

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...    SABIO-RKi    		P0A9M0

    Protein family/group databases

    MEROPS protease database

    More...    MEROPSi    		S16.001

    <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
    Recommended name:
    Lon proteaseUniRule annotation (EC:3.4.21.53UniRule annotation)
    Alternative name(s):
    ATP-dependent protease LaUniRule annotation
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
    Name:lonUniRule annotation
    Synonyms:capR, deg, lopA, muc
    Ordered Locus Names:b0439, JW0429
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiEscherichia coli (strain K12)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri83333 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia ›
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
    • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    <p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation on QuickGO ...

    Keywords - Cellular componenti

    Cytoplasm

    <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

    <p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>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). Decreased persister cell formation, further reduced when 10 mRNA toxin interferases are also deleted (PubMed:21788497).3 Publications

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi362K → A: Loss of proteolytic activity and ATP-binding. No increased persister cell formation. 2 Publications1
    Mutagenesisi665H → Y: Loss of proteolytic activity. 1 Publication1
    Mutagenesisi667H → Y: Loss of proteolytic activity. 1 Publication1
    Mutagenesisi676D → N: Loss of proteolytic activity. 1 Publication1
    Mutagenesisi679S → A: Loss of proteolytic activity. No increased persister cell formation. 2 Publications1
    Mutagenesisi743D → N: No effect. 1 Publication1

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedUniRule annotation1 Publication
    <p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000761332 – 784Lon proteaseAdd BLAST783

    Proteomic databases

    jPOST - Japan Proteome Standard Repository/Database

    More...    jPOSTi    		P0A9M0

    PaxDb, a database of protein abundance averages across all three domains of life

    More...    PaxDbi    		P0A9M0

    PRoteomics IDEntifications database

    More...    PRIDEi    		P0A9M0

    <p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

    <p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

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

    <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

    <p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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

    <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

    Hide details

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGRID)

    More...    BioGRIDi    		4260734, 201 interactors
    849474, 1 interactor

    Database of interacting proteins

    More...    DIPi    		DIP-35845N

    Protein interaction database and analysis system

    More...    IntActi    		P0A9M0, 72 interactors

    Molecular INTeraction database

    More...    MINTi    		P0A9M0

    STRING: functional protein association networks

    More...    STRINGi    		511145.b0439

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    Secondary structure

    1784
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    Biological Magnetic Resonance Data Bank

    More...    BMRBi    		P0A9M0

    SWISS-MODEL Repository - a database of annotated 3D protein structure models

    More...    SMRi    		P0A9M0

    Database of comparative protein structure models

    More...    ModBasei    		Search...

    Protein Data Bank in Europe - Knowledge Base

    More...    PDBe-KBi    		Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...    EvolutionaryTracei    		P0A9M0

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini11 – 202Lon N-terminalPROSITE-ProRule annotationAdd BLAST192
    Domaini592 – 773Lon proteolyticPROSITE-ProRule annotationAdd BLAST182

    Compositional bias

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi211 – 219Arg/Lys-rich (basic)9
    Compositional biasi240 – 252Asp/Glu-rich (acidic)Add BLAST13
    Compositional biasi255 – 270Arg/Lys-rich (basic)Add BLAST16

    <p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

    Belongs to the peptidase S16 family.UniRule annotation

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...    eggNOGi    		COG0466, Bacteria

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...    HOGENOMi    		CLU_004109_4_3_6

    InParanoid: Eukaryotic Ortholog Groups

    More...    InParanoidi    		P0A9M0

    KEGG Orthology (KO)

    More...    KOi    		K01338

    Database for complete collections of gene phylogenies

    More...    PhylomeDBi    		P0A9M0

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...    Gene3Di    		3.30.230.10, 1 hit

    HAMAP database of protein families

    More...    HAMAPi    		MF_01973, lon_bact, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...    InterProi    		View protein in InterPro
    IPR003593, AAA+_ATPase
    IPR003959, ATPase_AAA_core
    IPR027543, Lon_bac
    IPR004815, Lon_bac/euk-typ
    IPR008269, Lon_proteolytic
    IPR027065, Lon_Prtase
    IPR003111, Lon_substr-bd
    IPR027417, P-loop_NTPase
    IPR008268, Peptidase_S16_AS
    IPR015947, PUA-like_sf
    IPR020568, Ribosomal_S5_D2-typ_fold
    IPR014721, Ribosomal_S5_D2-typ_fold_subgr

    The PANTHER Classification System

    More...    PANTHERi    		PTHR10046, PTHR10046, 1 hit

    Pfam protein domain database

    More...    Pfami    		View protein in Pfam
    PF00004, AAA, 1 hit
    PF05362, Lon_C, 1 hit
    PF02190, LON_substr_bdg, 1 hit

    PIRSF; a whole-protein classification database

    More...    PIRSFi    		PIRSF001174, Lon_proteas, 1 hit

    Simple Modular Architecture Research Tool; a protein domain database

    More...    SMARTi    		View protein in SMART
    SM00382, AAA, 1 hit
    SM00464, LON, 1 hit

    Superfamily database of structural and functional annotation

    More...    SUPFAMi    		SSF52540, SSF52540, 1 hit
    SSF54211, SSF54211, 1 hit
    SSF88697, SSF88697, 1 hit

    TIGRFAMs; a protein family database

    More...    TIGRFAMsi    		TIGR00763, lon, 1 hit

    PROSITE; a protein domain and family database

    More...    PROSITEi    		View protein in PROSITE
    PS51787, LON_N, 1 hit
    PS51786, LON_PROTEOLYTIC, 1 hit
    PS01046, LON_SER, 1 hit

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>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
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i4042499C97694EF8
    GO

    <p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

    The sequence AAA23537 differs from that shown. Reason: Frameshift.Curated
    The sequence AAB40195 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti264 – 317PKEAK…LRQAQ → RKRQKRKRTGVAEAENDVSD VGRSDRSAWLYRLDGTGAVE CAYEGQKRPASGA in AAA24078 (PubMed:3042779).CuratedAdd BLAST54
    Sequence conflicti273A → R in AAA16837 (PubMed:8226758).Curated1
    Sequence conflicti307S → T in AAA16837 (PubMed:8226758).Curated1
    Sequence conflicti539 – 563AGVRG…LLLDK → RACVVWSVKSPNCVAKRLSS YCSIT in AAA24078 (PubMed:3042779).CuratedAdd BLAST25
    Sequence conflicti772Q → R in AAA16837 (PubMed:8226758).Curated1
    Sequence conflicti779 – 784QVVTAK → HHSLRRRCSTASTYYWAKS in AAA24079 (PubMed:3289547).Curated6

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...    EMBLi

    GenBank nucleotide sequence database

    More...    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...    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.

    Protein sequence database of the Protein Information Resource

    More...    PIRi    		A23101
    G64773, SUECLA

    NCBI Reference Sequences

    More...    RefSeqi    		NP_414973.1, NC_000913.3
    WP_001295325.1, NZ_STEB01000007.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...    EnsemblBacteriai    		AAC73542; AAC73542; b0439
    BAE76219; BAE76219; BAE76219

    Database of genes from NCBI RefSeq genomes

    More...    GeneIDi    		52075780
    945085

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...    KEGGi    		ecj:JW0429
    eco:b0439

    Pathosystems Resource Integration Center (PATRIC)

    More...    PATRICi    		fig|1411691.4.peg.1837

    <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

    <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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_STEB01000007.1

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe

    More...    PDBei

    Protein Data Bank RCSB

    More...    RCSB PDBi

    Protein Data Bank Japan

    More...    PDBji
    Links Updated
    		PDB 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[»]
    6N2IX-ray3.50A241-584[»]
    BMRBiP0A9M0
    SMRiP0A9M0
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    BioGRIDi4260734, 201 interactors
    849474, 1 interactor
    DIPiDIP-35845N
    IntActiP0A9M0, 72 interactors
    MINTiP0A9M0
    STRINGi511145.b0439

    Protein family/group databases

    MEROPSiS16.001

    Proteomic databases

    jPOSTiP0A9M0
    PaxDbiP0A9M0
    PRIDEiP0A9M0

    Genome annotation databases

    EnsemblBacteriaiAAC73542; AAC73542; b0439
    BAE76219; BAE76219; BAE76219
    GeneIDi52075780
    945085
    KEGGiecj:JW0429
    eco:b0439
    PATRICifig|1411691.4.peg.1837

    Organism-specific databases

    EchoBASE - an integrated post-genomic database for E. coli

    More...    EchoBASEi    		EB0537

    Phylogenomic databases

    eggNOGiCOG0466, Bacteria
    HOGENOMiCLU_004109_4_3_6
    InParanoidiP0A9M0
    KOiK01338
    PhylomeDBiP0A9M0

    Enzyme and pathway databases

    BioCyciEcoCyc:EG10542-MONOMER
    MetaCyc:EG10542-MONOMER
    BRENDAi3.4.21.53, 2026
    SABIO-RKiP0A9M0

    Miscellaneous databases

    EvolutionaryTraceiP0A9M0

    Protein Ontology

    More...    PROi    		PR:P0A9M0

    Family and domain databases

    Gene3Di3.30.230.10, 1 hit
    HAMAPiMF_01973, lon_bact, 1 hit
    InterProiView protein in InterPro
    IPR003593, AAA+_ATPase
    IPR003959, ATPase_AAA_core
    IPR027543, Lon_bac
    IPR004815, Lon_bac/euk-typ
    IPR008269, Lon_proteolytic
    IPR027065, Lon_Prtase
    IPR003111, Lon_substr-bd
    IPR027417, P-loop_NTPase
    IPR008268, Peptidase_S16_AS
    IPR015947, PUA-like_sf
    IPR020568, Ribosomal_S5_D2-typ_fold
    IPR014721, Ribosomal_S5_D2-typ_fold_subgr
    PANTHERiPTHR10046, PTHR10046, 1 hit
    PfamiView protein in Pfam
    PF00004, AAA, 1 hit
    PF05362, Lon_C, 1 hit
    PF02190, LON_substr_bdg, 1 hit
    PIRSFiPIRSF001174, Lon_proteas, 1 hit
    SMARTiView protein in SMART
    SM00382, AAA, 1 hit
    SM00464, LON, 1 hit
    SUPFAMiSSF52540, SSF52540, 1 hit
    SSF54211, SSF54211, 1 hit
    SSF88697, SSF88697, 1 hit
    TIGRFAMsiTIGR00763, lon, 1 hit
    PROSITEiView protein in PROSITE
    PS51787, LON_N, 1 hit
    PS51786, LON_PROTEOLYTIC, 1 hit
    PS01046, LON_SER, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...    ProtoNeti    		Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...    MobiDBi    		Search...

    <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

    <p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiLON_ECOLI
    <p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P0A9M0
    Secondary accession number(s): P08177, P78219, Q2MBY7
    <p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: July 19, 2005
    Last modified: October 7, 2020
    This is version 141 of the entry and version 1 of the sequence. See complete history.
    <p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    <p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing, Reference proteome

    Documents

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