ECOLI:LON

Species (Taxon ID)	Escherichia coli (strain K12). (83333)
Gene Name(s)	lon (ECO:0000255 with HAMAP-Rule:MF_01973) (synonyms: capR, deg, lopA, muc)
Protein Name(s)	Lon protease (ECO:0000255 with HAMAP-Rule:MF_01973) ATP-dependent protease La (ECO:0000255 with HAMAP-Rule:MF_01973)
External Links
UniProt	P0A9M0
EMBL	L12349 M38347 L20572 J03896 U82664 U00096 AP009048 M10153
PIR	A23101 G64773
RefSeq	NP_414973.1 YP_488731.1
PDB	1QZM 1RR9 1RRE 2ANE 3LJC
PDBsum	1QZM 1RR9 1RRE 2ANE 3LJC
ProteinModelPortal	P0A9M0
SMR	P0A9M0
DIP	DIP-35845N
IntAct	P0A9M0
MINT	MINT-1224190
STRING	511145.b0439
MEROPS	S16.001
PaxDb	P0A9M0
PRIDE	P0A9M0
EnsemblBacteria	AAC73542 BAE76219
GeneID	12931740 945085
KEGG	ecj:Y75_p0427 eco:b0439
PATRIC	32116031
EchoBASE	EB0537
EcoGene	EG10542
eggNOG	COG0466
HOGENOM	HOG000261408
InParanoid	P0A9M0
KO	K01338
OMA	IPVARMD
OrthoDB	EOG6XHC23
PhylomeDB	P0A9M0
BioCyc	EcoCyc:EG10542-MONOMER ECOL316407:JW0429-MONOMER MetaCyc:EG10542-MONOMER
EvolutionaryTrace	P0A9M0
PRO	PR:P0A9M0
Proteomes	UP000000318 UP000000625
Genevestigator	P0A9M0
GO	GO:0005737 GO:0005524 GO:0004176 GO:0016887 GO:0003677 GO:0008233 GO:0043565 GO:0004252 GO:0006200 GO:0033554 GO:0006515 GO:0006508 GO:0009408
Gene3D	3.30.230.10 3.40.50.300
HAMAP	MF_01973
InterPro	IPR003593 IPR003959 IPR027543 IPR004815 IPR027065 IPR027417 IPR008269 IPR003111 IPR008268 IPR015947 IPR020568 IPR014721
PANTHER	PTHR10046
Pfam	PF00004 PF02190 PF05362
PIRSF	PIRSF001174
SMART	SM00382 SM00464
SUPFAM	SSF52540 SSF54211 SSF88697
TIGRFAMs	TIGR00763
PROSITE	PS01046

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
	GO:0009411	response to UV	PMID:4934518^[1]	ECO:0000315			P	table 5	complete
	GO:0009408	response to heat	PMID:6436819^[2]	ECO:0000270			P	Table 1. shows upregulation of Lon in response to heat exposure (42C)	complete
	GO:0006508	proteolysis	PMID:6436819^[2]	ECO:0000315			P	Fig. 1 and 2 show decreased proteolytic activity in the mutant phenotype	complete
	GO:0045471	response to ethanol	PMID:6436819^[2]	ECO:0000270			P	Table 1. shows enhanced Lon expression in the presence of ethanol (4%)	complete
	GO:0009411	response to UV	PMID:6436819^[2]	ECO:0000315			P	Table 3. Increased UV sensitivity in mutant lon	complete
enables	GO:0008236	serine-type peptidase activity	PMID:9620272^[3]	ECO:0000245	automatically integrated combinatorial evidence used in manual assertion	UniProtKB:P93647	F	Seeded From UniProt	complete
enables	GO:0005524	ATP binding	PMID:9620272^[3]	ECO:0000245	automatically integrated combinatorial evidence used in manual assertion	UniProtKB:P93647	F	Seeded From UniProt	complete
enables	GO:0016887	ATPase activity	PMID:6458036^[4]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0009408	response to heat	PMID:8349564^[5]	ECO:0000270	expression pattern evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0008233	peptidase activity	PMID:9720920^[6]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0006508	proteolysis	PMID:6458036^[4]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:8995294^[7]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0004252	serine-type endopeptidase activity	PMID:15606774^[8]	ECO:0000315	mutant phenotype evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0004176	ATP-dependent peptidase activity	PMID:9720920^[6]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0004176	ATP-dependent peptidase activity	PMID:6458036^[4]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0003677	DNA binding	PMID:8995294^[7]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0010165	response to X-ray	PMID:27718375^[9]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006515	protein quality control for misfolded or incompletely synthesized proteins	PMID:4584816^[10]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006515	protein quality control for misfolded or incompletely synthesized proteins	PMID:11886743^[11]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:18304323^[12]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:15911532^[13]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0005524	ATP binding	PMID:3312196^[14]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0004176	ATP-dependent peptidase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR004815 InterPro:IPR008268 InterPro:IPR008269 InterPro:IPR027065 InterPro:IPR027543	F	Seeded From UniProt	complete
enables	GO:0004252	serine-type endopeptidase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR008268 InterPro:IPR008269 InterPro:IPR027065 InterPro:IPR027543	F	Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR003959 InterPro:IPR004815 InterPro:IPR027065 InterPro:IPR027543	F	Seeded From UniProt	complete
involved_in	GO:0006508	proteolysis	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR004815 InterPro:IPR008268 InterPro:IPR008269 InterPro:IPR027543	P	Seeded From UniProt	complete
involved_in	GO:0030163	protein catabolic process	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR027065	P	Seeded From UniProt	complete
enables	GO:0043565	sequence-specific DNA binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR027543	F	Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000161584	F	Seeded From UniProt	complete
enables	GO:0016887	ATPase activity	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000161584	F	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000161584	C	Seeded From UniProt	complete
involved_in	GO:0006515	protein quality control for misfolded or incompletely synthesized proteins	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000161584	P	Seeded From UniProt	complete
enables	GO:0043565	sequence-specific DNA binding	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000161584	F	Seeded From UniProt	complete
involved_in	GO:0034605	cellular response to heat	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000161584	P	Seeded From UniProt	complete
enables	GO:0004176	ATP-dependent peptidase activity	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000161584	F	Seeded From UniProt	complete
enables	GO:0004252	serine-type endopeptidase activity	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000161584	F	Seeded From UniProt	complete
enables	GO:0008236	serine-type peptidase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0720	F	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963 UniProtKB-SubCell:SL-0086	C	Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0067	F	Seeded From UniProt	complete
involved_in	GO:0006508	proteolysis	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0645	P	Seeded From UniProt	complete
enables	GO:0000166	nucleotide binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0547	F	Seeded From UniProt	complete
enables	GO:0016787	hydrolase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0378	F	Seeded From UniProt	complete
enables	GO:0008233	peptidase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0645	F	Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ Takano, T (1971) Bacterial mutants defective in plasmid formation: requirement for the lon + allele. Proc. Natl. Acad. Sci. U.S.A. 68 1469-73 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 ^2.3 Goff, SA et al. (1984) Heat shock regulatory gene htpR influences rates of protein degradation and expression of the lon gene in Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 81 6647-51 PubMed GONUTS page
↑ ^3.0 ^3.1 Barakat, S et al. (1998) Maize contains a Lon protease gene that can partially complement a yeast pim1-deletion mutant. Plant Mol. Biol. 37 141-54 PubMed GONUTS page
↑ ^4.0 ^4.1 ^4.2 Charette, MF et al. (1981) ATP hydrolysis-dependent protease activity of the lon (capR) protein of Escherichia coli K-12. Proc. Natl. Acad. Sci. U.S.A. 78 4728-32 PubMed GONUTS page
↑ Chuang, SE & Blattner, FR (1993) Characterization of twenty-six new heat shock genes of Escherichia coli. J. Bacteriol. 175 5242-52 PubMed GONUTS page
↑ ^6.0 ^6.1 Rasulova, FS et al. (1998) The isolated proteolytic domain of Escherichia coli ATP-dependent protease Lon exhibits the peptidase activity. FEBS Lett. 432 179-81 PubMed GONUTS page
↑ ^7.0 ^7.1 Fu, GK et al. (1997) Bacterial protease Lon is a site-specific DNA-binding protein. J. Biol. Chem. 272 534-8 PubMed GONUTS page
↑ Rotanova, TV et al. (2004) Classification of ATP-dependent proteases Lon and comparison of the active sites of their proteolytic domains. Eur. J. Biochem. 271 4865-71 PubMed GONUTS page
↑ Sargentini, NJ et al. () Screen for genes involved in radiation survival of Escherichia coli and construction of a reference database. Mutat. Res. 793-794 1-14 PubMed GONUTS page
↑ Shineberg, B & Zipser, D (1973) The ion gene and degradation of beta-galactosidase nonsense fragments. J. Bacteriol. 116 1469-71 PubMed GONUTS page
↑ Rosen, R et al. (2002) Protein aggregation in Escherichia coli: role of proteases. FEMS Microbiol. Lett. 207 9-12 PubMed GONUTS page
↑ Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page
↑ Lopez-Campistrous, A et al. (2005) Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth. Mol. Cell Proteomics 4 1205-9 PubMed GONUTS page
↑ Menon, AS & Goldberg, AL (1987) Binding of nucleotides to the ATP-dependent protease La from Escherichia coli. J. Biol. Chem. 262 14921-8 PubMed GONUTS page

[PMID:4934518-1] Takano, T (1971) Bacterial mutants defective in plasmid formation: requirement for the lon + allele. Proc. Natl. Acad. Sci. U.S.A. 68 1469-73 PubMed GONUTS page

[PMID:6436819-2] 2.0 ^2.1 ^2.2 ^2.3 Goff, SA et al. (1984) Heat shock regulatory gene htpR influences rates of protein degradation and expression of the lon gene in Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 81 6647-51 PubMed GONUTS page

[PMID:9620272-3] 3.0 ^3.1 Barakat, S et al. (1998) Maize contains a Lon protease gene that can partially complement a yeast pim1-deletion mutant. Plant Mol. Biol. 37 141-54 PubMed GONUTS page

[PMID:6458036-4] 4.0 ^4.1 ^4.2 Charette, MF et al. (1981) ATP hydrolysis-dependent protease activity of the lon (capR) protein of Escherichia coli K-12. Proc. Natl. Acad. Sci. U.S.A. 78 4728-32 PubMed GONUTS page

[PMID:8349564-5] Chuang, SE & Blattner, FR (1993) Characterization of twenty-six new heat shock genes of Escherichia coli. J. Bacteriol. 175 5242-52 PubMed GONUTS page

[PMID:9720920-6] 6.0 ^6.1 Rasulova, FS et al. (1998) The isolated proteolytic domain of Escherichia coli ATP-dependent protease Lon exhibits the peptidase activity. FEBS Lett. 432 179-81 PubMed GONUTS page

[PMID:8995294-7] 7.0 ^7.1 Fu, GK et al. (1997) Bacterial protease Lon is a site-specific DNA-binding protein. J. Biol. Chem. 272 534-8 PubMed GONUTS page

[PMID:15606774-8] Rotanova, TV et al. (2004) Classification of ATP-dependent proteases Lon and comparison of the active sites of their proteolytic domains. Eur. J. Biochem. 271 4865-71 PubMed GONUTS page

[PMID:27718375-9] Sargentini, NJ et al. () Screen for genes involved in radiation survival of Escherichia coli and construction of a reference database. Mutat. Res. 793-794 1-14 PubMed GONUTS page

[PMID:4584816-10] Shineberg, B & Zipser, D (1973) The ion gene and degradation of beta-galactosidase nonsense fragments. J. Bacteriol. 116 1469-71 PubMed GONUTS page

[PMID:11886743-11] Rosen, R et al. (2002) Protein aggregation in Escherichia coli: role of proteases. FEMS Microbiol. Lett. 207 9-12 PubMed GONUTS page

[PMID:18304323-12] Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page

[PMID:15911532-13] Lopez-Campistrous, A et al. (2005) Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth. Mol. Cell Proteomics 4 1205-9 PubMed GONUTS page

[PMID:3312196-14] Menon, AS & Goldberg, AL (1987) Binding of nucleotides to the ATP-dependent protease La from Escherichia coli. J. Biol. Chem. 262 14921-8 PubMed GONUTS page

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ECOLI:LON

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