UniProtKB - P0A9M0 (LON_ECOLI)

BLAST

>sp|P0A9M0|LON_ECOLI Lon protease OS=Escherichia coli (strain K12) OX=83333 GN=lon PE=1 SV=1
MNPERSERIEIPVLPLRDVVVYPHMVIPLFVGREKSIRCLEAAMDHDKKIMLVAQKEAST
DEPGVNDLFTVGTVASILQMLKLPDGTVKVLVEGLQRARISALSDNGEHFSAKAEYLESP
TIDEREQEVLVRTAISQFEGYIKLNKKIPPEVLTSLNSIDDPARLADTIAAHMPLKLADK
QSVLEMSDVNERLEYLMAMMESEIDLLQVEKRIRNRVKKQMEKSQREYYLNEQMKAIQKE
LGEMDDAPDENEALKRKIDAAKMPKEAKEKAEAELQKLKMMSPMSAEATVVRGYIDWMVQ
VPWNARSKVKKDLRQAQEILDTDHYGLERVKDRILEYLAVQSRVNKIKGPILCLVGPPGV
GKTSLGQSIAKATGRKYVRMALGGVRDEAEIRGHRRTYIGSMPGKLIQKMAKVGVKNPLF
LLDEIDKMSSDMRGDPASALLEVLDPEQNVAFSDHYLEVDYDLSDVMFVATSNSMNIPAP
LLDRMEVIRLSGYTEDEKLNIAKRHLLPKQIERNALKKGELTVDDSAIIGIIRYYTREAG
VRGLEREISKLCRKAVKQLLLDKSLKHIEINGDNLHDYLGVQRFDYGRADNENRVGQVTG
LAWTEVGGDLLTIETACVPGKGKLTYTGSLGEVMQESIQAALTVVRARAEKLGINPDFYE
KRDIHVHVPEGATPKDGPSAGIAMCTALVSCLTGNPVRADVAMTGEITLRGQVLPIGGLK
EKLLAAHRGGIKTVLIPFENKRDLEEIPDNVIADLDIHPVKRIEEVLTLALQNEPSGMQV
VTAK

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History
Entry version 125 (07 Nov 2018)
Sequence version 1 (19 Jul 2005)
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Protein

Lon protease

Gene

lon

Organism

Escherichia coli (strain K12)

Status

Reviewed-Annotation score: -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 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

Activity regulationⁱ

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

Kineticsⁱ

K_M=
0.201 mM for ATP for ATPase activity
1 Publication
Manual assertion based on experiment inⁱ
- Ref.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.

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
Inferred from direct assayⁱ
- 6458036
ATP binding
Source: EcoCyc
Inferred from direct assayⁱ
- 3312196
ATP-dependent peptidase activity
Source: EcoliWiki
Inferred from direct assayⁱ
- 6458036
- 9720920
DNA binding
Source: EcoliWiki
Inferred from direct assayⁱ
- 8995294
peptidase activity
Source: EcoliWiki
Inferred from direct assayⁱ
- 9720920
sequence-specific DNA binding Source: UniProtKB-UniRule
serine-type endopeptidase activity
Source: EcoliWiki
Inferred from mutant phenotypeⁱ
- 15606774

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

cellular response to heat Source: UniProtKB-UniRule
protein quality control for misfolded or incompletely synthesized proteins
Source: EcoCyc
Inferred from mutant phenotypeⁱ
- 11886743
- 4584816
proteolysis
Source: EcoliWiki
Inferred from direct assayⁱ
- 6458036
response to heat
Source: EcoliWiki
Inferred from expression patternⁱ
- 8349564
response to X-ray
Source: EcoCyc
Inferred from mutant phenotypeⁱ
- 27718375

View the complete GO annotation on QuickGO ...

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

Protein family/group databases

MEROPS protease database More...MEROPSⁱ	S16.001

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	cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › Escherichia coli
Proteomesⁱ	UP000000318 Componentⁱ: Chromosome UP000000625 Componentⁱ: Chromosome

Organism-specific databases

EcoGeneⁱ	EG10542 lon

EcoGeneⁱ

EG10542 lon

Subcellular locationⁱ

Cytoplasm

GO - Cellular componentⁱ

cytoplasm
Source: EcoliWiki
Inferred from direct assayⁱ
- 8995294
cytosol
Source: EcoCyc
Inferred from direct assayⁱ
- 15911532
- 18304323

View the complete GO annotation on QuickGO ...

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). Decreased persister cell formation, further reduced when 10 mRNA toxin interferases are also deleted (PubMed:21788497).3 Publications

Mutagenesis

Feature key	Position(s)	DescriptionActions	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

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 Publication

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
rplI	P0A7R1	4	EBI-547203,EBI-546437
torA	P33225	2	EBI-547203,EBI-557008

Protein-protein interaction databases

BioGridⁱ	4260734, 201 interactors
Database of interacting proteins More...DIPⁱ	DIP-35845N
IntActⁱ	P0A9M0, 72 interactors
Molecular INTeraction database More...MINTⁱ	P0A9M0
STRINGⁱ	316385.ECDH10B_0395

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	9 – 18	Combined sources	10
Beta strandⁱ	26 – 31	Combined sources	6
Helixⁱ	34 – 44	Combined sources	11
Turnⁱ	45 – 47	Combined sources	3
Beta strandⁱ	48 – 55	Combined sources	8
Helixⁱ	65 – 67	Combined sources	3
Beta strandⁱ	70 – 82	Combined sources	13
Beta strandⁱ	88 – 105	Combined sources	18
Beta strandⁱ	107 – 116	Combined sources	10
Helixⁱ	124 – 145	Combined sources	22
Helixⁱ	150 – 155	Combined sources	6
Helixⁱ	162 – 171	Combined sources	10
Helixⁱ	177 – 185	Combined sources	9
Helixⁱ	189 – 242	Combined sources	54
Helixⁱ	495 – 504	Combined sources	10
Helixⁱ	506 – 513	Combined sources	8
Turnⁱ	518 – 520	Combined sources	3
Beta strandⁱ	521 – 523	Combined sources	3
Helixⁱ	525 – 535	Combined sources	11
Beta strandⁱ	539 – 541	Combined sources	3
Helixⁱ	542 – 560	Combined sources	19
Beta strandⁱ	568 – 570	Combined sources	3
Turnⁱ	572 – 574	Combined sources	3
Helixⁱ	575 – 579	Combined sources	5
Beta strandⁱ	596 – 604	Combined sources	9
Beta strandⁱ	607 – 619	Combined sources	13
Beta strandⁱ	624 – 630	Combined sources	7
Helixⁱ	632 – 647	Combined sources	16
Helixⁱ	649 – 652	Combined sources	4
Turnⁱ	656 – 660	Combined sources	5
Beta strandⁱ	661 – 667	Combined sources	7
Beta strandⁱ	675 – 678	Combined sources	4
Helixⁱ	681 – 693	Combined sources	13
Beta strandⁱ	701 – 703	Combined sources	3
Beta strandⁱ	712 – 714	Combined sources	3
Helixⁱ	719 – 728	Combined sources	10
Beta strandⁱ	733 – 737	Combined sources	5
Helixⁱ	738 – 746	Combined sources	9
Helixⁱ	749 – 754	Combined sources	6
Beta strandⁱ	755 – 762	Combined sources	8
Helixⁱ	763 – 770	Combined sources	8
Beta strandⁱ	771 – 773	Combined sources	3

Show more details

3D structure databases

ProteinModelPortalⁱ	P0A9M0
SMRⁱ	P0A9M0
ModBaseⁱ	Search...
MobiDBⁱ	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	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	ENOG4105C6P Bacteria COG0466 LUCA
HOGENOMⁱ	HOG000261408
InParanoidⁱ	P0A9M0
KEGG Orthology (KO) More...KOⁱ	K01338
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
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
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

Sequenceⁱ

Sequence statusⁱ: Complete.

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

P0A9M0-1 [UniParc]FASTA Add 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

Sequence cautionⁱ

The sequence AAA23537 differs from that shown. Reason: Frameshift at position 16.Curated

The sequence AAB40195 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature key	Position(s)	DescriptionActions	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
NCBI Reference Sequences More...RefSeqⁱ	NP_414973.1, NC_000913.3 WP_001295325.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaⁱ	AAC73542; AAC73542; b0439 BAE76219; BAE76219; BAE76219
GeneIDⁱ	945085
KEGGⁱ	ecj:JW0429 eco:b0439
PATRICⁱ	fig\|1411691.4.peg.1837

Protein	Similar proteins		Species	Score	Length	Source
P0A9M0	Lon protease		ECOL6		784	UniRef100_P0A9M1
Lon protease		ECOLX		799
Lon protease		Klebsiella pneumoniae IS22		799
Lon protease		Escherichia coli H605		799
Lon protease		ECOCB		799
+158

Protein	Similar proteins		Species	Score	Length	Source
P0A9M0	Lon protease		ECOL6		784	UniRef90_P0A9M1
Lon protease		ERWAM		784
Lon protease		ECOLX		799
Lon protease		Klebsiella pneumoniae IS22		799
Lon protease		Escherichia coli H605		799
+1678

Protein	Similar proteins		Species	Score	Length	Source
P0A9M0	Lon protease 1	)	BACSU		774	UniRef50_P37945
Lon protease 1		SYNFM		815
Lon protease		AZOBR		810
Lon protease 2		DESPS		774
Lon protease		HELMI		813
+16162

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_LN832404.1

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 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	[»]
ProteinModelPortalⁱ	P0A9M0
SMRⁱ	P0A9M0
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	4260734, 201 interactors
DIPⁱ	DIP-35845N
IntActⁱ	P0A9M0, 72 interactors
MINTⁱ	P0A9M0
STRINGⁱ	316385.ECDH10B_0395

Protein family/group databases

MEROPSⁱ	S16.001

MEROPSⁱ

S16.001

Proteomic databases

PaxDbⁱ	P0A9M0
PRIDEⁱ	P0A9M0

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

EnsemblBacteriaⁱ	AAC73542; AAC73542; b0439 BAE76219; BAE76219; BAE76219
GeneIDⁱ	945085
KEGGⁱ	ecj:JW0429 eco:b0439
PATRICⁱ	fig\|1411691.4.peg.1837

Organism-specific databases

EchoBASEⁱ	EB0537
EcoGeneⁱ	EG10542 lon

Phylogenomic databases

eggNOGⁱ	ENOG4105C6P Bacteria COG0466 LUCA
HOGENOMⁱ	HOG000261408
InParanoidⁱ	P0A9M0
KOⁱ	K01338
PhylomeDBⁱ	P0A9M0

Enzyme and pathway databases

BioCycⁱ	EcoCyc:EG10542-MONOMER MetaCyc:EG10542-MONOMER
BRENDAⁱ	3.4.21.53 2026

Miscellaneous databases

EvolutionaryTraceⁱ	P0A9M0
Protein Ontology More...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...

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:	November 7, 2018
	This is version 125 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, Complete proteome, Direct protein sequencing, Reference proteome

Documents

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

UniProtKB

UniParc

Help

UniRef

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Supporting data

UniProtKB - P0A9M0 (LON_ECOLI)

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Lon protease

lon

Select a section on the left to see content.

<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

Miscellaneous

<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

Sites

Regions

<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

GO - Biological processi

Enzyme and pathway databases

Protein family/group databases

<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

Organism-specific databases

<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

Keywords - Cellular componenti

<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

Mutagenesis

<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

Proteomic databases

<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 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

Protein-protein interaction databases

<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

3D structure databases

Miscellaneous databases

<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

Compositional bias

<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

Phylogenomic databases

Family and domain databases

<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

Experimental Info

Sequence databases

Genome annotation databases

<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

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<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 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

Documents

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Functionⁱ

Kineticsⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Expressionⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Sequence cautionⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ