UniProtKB - P0A9M0 (LON_ECOLI)
Protein
Lon protease
Gene
lon
Organism
Escherichia coli (strain K12)
Status
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.
Catalytic activityi
- Hydrolysis of proteins in presence of ATP.UniRule annotation EC:3.4.21.53
Activity regulationi
Contains an allosteric site (distinct from its active site), whose occupancy by an unfolded polypeptide leads to enzyme activation.
Kineticsi
- KM=0.201 mM for ATP for ATPase activity1 Publication
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 679 | 1 | ||
Active sitei | 722 | UniRule annotation1 Publication | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 356 – 363 | ATPUniRule annotation | 8 |
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-UniRule
- serine-type endopeptidase activity Source: EcoliWiki
GO - Biological processi
- cellular response to heat Source: UniProtKB-UniRule
- protein quality control for misfolded or incompletely synthesized proteins Source: EcoCyc
- proteolysis Source: EcoliWiki
- response to heat Source: EcoliWiki
- response to X-ray Source: EcoCyc
Keywordsi
Molecular function | Hydrolase, Protease, Serine protease |
Biological process | Stress response |
Ligand | ATP-binding, Nucleotide-binding |
Enzyme and pathway databases
BioCyci | EcoCyc:EG10542-MONOMER MetaCyc:EG10542-MONOMER |
BRENDAi | 3.4.21.53, 2026 |
SABIO-RKi | P0A9M0 |
Protein family/group databases
MEROPSi | S16.001 |
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 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
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). Decreased persister cell formation, further reduced when 10 mRNA toxin interferases are also deleted (PubMed:21788497).3 Publications
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 362 | K → A: Loss of proteolytic activity and ATP-binding. No increased persister cell formation. 2 Publications | 1 | |
Mutagenesisi | 665 | H → Y: Loss of proteolytic activity. 1 Publication | 1 | |
Mutagenesisi | 667 | H → Y: Loss of proteolytic activity. 1 Publication | 1 | |
Mutagenesisi | 676 | D → N: Loss of proteolytic activity. 1 Publication | 1 | |
Mutagenesisi | 679 | S → A: Loss of proteolytic activity. No increased persister cell formation. 2 Publications | 1 | |
Mutagenesisi | 743 | D → N: No effect. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | RemovedUniRule annotation1 Publication | |||
ChainiPRO_0000076133 | 2 – 784 | Lon proteaseAdd BLAST | 783 |
Proteomic databases
jPOSTi | P0A9M0 |
PaxDbi | P0A9M0 |
PRIDEi | P0A9M0 |
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 PublicationBinary interactionsi
Hide detailsProtein-protein interaction databases
BioGRIDi | 4260734, 201 interactors 849474, 1 interactor |
DIPi | DIP-35845N |
IntActi | P0A9M0, 72 interactors |
MINTi | P0A9M0 |
STRINGi | 511145.b0439 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
BMRBi | P0A9M0 |
SMRi | P0A9M0 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P0A9M0 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 11 – 202 | Lon N-terminalPROSITE-ProRule annotationAdd BLAST | 192 | |
Domaini | 592 – 773 | Lon proteolyticPROSITE-ProRule annotationAdd BLAST | 182 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 211 – 219 | Arg/Lys-rich (basic) | 9 | |
Compositional biasi | 240 – 252 | Asp/Glu-rich (acidic)Add BLAST | 13 | |
Compositional biasi | 255 – 270 | Arg/Lys-rich (basic)Add BLAST | 16 |
Sequence similaritiesi
Belongs to the peptidase S16 family.UniRule annotation
Phylogenomic databases
eggNOGi | COG0466, Bacteria |
HOGENOMi | CLU_004109_4_3_6 |
InParanoidi | P0A9M0 |
PhylomeDBi | P0A9M0 |
Family and domain databases
Gene3Di | 3.30.230.10, 1 hit |
HAMAPi | MF_01973, lon_bact, 1 hit |
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 |
PANTHERi | PTHR10046, PTHR10046, 1 hit |
Pfami | View protein in Pfam PF00004, AAA, 1 hit PF05362, Lon_C, 1 hit PF02190, LON_substr_bdg, 1 hit |
PIRSFi | PIRSF001174, Lon_proteas, 1 hit |
SMARTi | View protein in SMART SM00382, AAA, 1 hit SM00464, LON, 1 hit |
SUPFAMi | SSF52540, SSF52540, 1 hit SSF54211, SSF54211, 1 hit SSF88697, SSF88697, 1 hit |
TIGRFAMsi | TIGR00763, lon, 1 hit |
PROSITEi | View protein in PROSITE PS51787, LON_N, 1 hit PS51786, LON_PROTEOLYTIC, 1 hit PS01046, LON_SER, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P0A9M0-1 [UniParc]FASTAAdd to basket
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
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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 264 – 317 | PKEAK…LRQAQ → RKRQKRKRTGVAEAENDVSD VGRSDRSAWLYRLDGTGAVE CAYEGQKRPASGA in AAA24078 (PubMed:3042779).CuratedAdd BLAST | 54 | |
Sequence conflicti | 273 | A → R in AAA16837 (PubMed:8226758).Curated | 1 | |
Sequence conflicti | 307 | S → T in AAA16837 (PubMed:8226758).Curated | 1 | |
Sequence conflicti | 539 – 563 | AGVRG…LLLDK → RACVVWSVKSPNCVAKRLSS YCSIT in AAA24078 (PubMed:3042779).CuratedAdd BLAST | 25 | |
Sequence conflicti | 772 | Q → R in AAA16837 (PubMed:8226758).Curated | 1 | |
Sequence conflicti | 779 – 784 | QVVTAK → HHSLRRRCSTASTYYWAKS in AAA24079 (PubMed:3289547).Curated | 6 |
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. |
PIRi | A23101 G64773, SUECLA |
RefSeqi | NP_414973.1, NC_000913.3 WP_001295325.1, NZ_STEB01000007.1 |
Genome annotation databases
EnsemblBacteriai | AAC73542; AAC73542; b0439 BAE76219; BAE76219; BAE76219 |
GeneIDi | 57731618 945085 |
KEGGi | ecj:JW0429 eco:b0439 |
PATRICi | fig|1411691.4.peg.1837 |
Similar proteinsi
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. |
PIRi | A23101 G64773, SUECLA |
RefSeqi | NP_414973.1, NC_000913.3 WP_001295325.1, NZ_STEB01000007.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1QZM | X-ray | 1.90 | A | 491-584 | [»] | |
1RR9 | X-ray | 2.10 | A/B/C/D/E/F | 585-784 | [»] | |
1RRE | X-ray | 1.75 | A/B/C/D/E/F | 585-784 | [»] | |
2ANE | X-ray | 2.03 | A/B/C/D/E/F/G/H | 1-118 | [»] | |
3LJC | X-ray | 2.60 | A | 1-245 | [»] | |
6N2I | X-ray | 3.50 | A | 241-584 | [»] | |
6U5Z | electron microscopy | 3.50 | A/B/C/D/E/F | 1-784 | [»] | |
BMRBi | P0A9M0 | |||||
SMRi | P0A9M0 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 4260734, 201 interactors 849474, 1 interactor |
DIPi | DIP-35845N |
IntActi | P0A9M0, 72 interactors |
MINTi | P0A9M0 |
STRINGi | 511145.b0439 |
Protein family/group databases
MEROPSi | S16.001 |
Proteomic databases
jPOSTi | P0A9M0 |
PaxDbi | P0A9M0 |
PRIDEi | P0A9M0 |
Genome annotation databases
EnsemblBacteriai | AAC73542; AAC73542; b0439 BAE76219; BAE76219; BAE76219 |
GeneIDi | 57731618 945085 |
KEGGi | ecj:JW0429 eco:b0439 |
PATRICi | fig|1411691.4.peg.1837 |
Organism-specific databases
EchoBASEi | EB0537 |
Phylogenomic databases
eggNOGi | COG0466, Bacteria |
HOGENOMi | CLU_004109_4_3_6 |
InParanoidi | P0A9M0 |
PhylomeDBi | P0A9M0 |
Enzyme and pathway databases
BioCyci | EcoCyc:EG10542-MONOMER MetaCyc:EG10542-MONOMER |
BRENDAi | 3.4.21.53, 2026 |
SABIO-RKi | P0A9M0 |
Miscellaneous databases
EvolutionaryTracei | P0A9M0 |
PROi | PR:P0A9M0 |
Family and domain databases
Gene3Di | 3.30.230.10, 1 hit |
HAMAPi | MF_01973, lon_bact, 1 hit |
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 |
PANTHERi | PTHR10046, PTHR10046, 1 hit |
Pfami | View protein in Pfam PF00004, AAA, 1 hit PF05362, Lon_C, 1 hit PF02190, LON_substr_bdg, 1 hit |
PIRSFi | PIRSF001174, Lon_proteas, 1 hit |
SMARTi | View protein in SMART SM00382, AAA, 1 hit SM00464, LON, 1 hit |
SUPFAMi | SSF52540, SSF52540, 1 hit SSF54211, SSF54211, 1 hit SSF88697, SSF88697, 1 hit |
TIGRFAMsi | TIGR00763, lon, 1 hit |
PROSITEi | View protein in PROSITE PS51787, LON_N, 1 hit PS51786, LON_PROTEOLYTIC, 1 hit PS01046, LON_SER, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | LON_ECOLI | |
Accessioni | P0A9M0Primary (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: | April 7, 2021 | |
This is version 144 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- Peptidase families
Classification of peptidase families and list of entries - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families