ATP-dependent protease La - Escherichia coli (strain K12)

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Reviewed, UniProtKB/Swiss-Prot P0A9M0 (LON_ECOLI)

Last modified June 16, 2009. Version 41. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
ATP-dependent protease La
EC=3.4.21.53

Gene names

Name:	lon
Synonyms:	capR, deg, lopA, muc
Ordered Locus Names:	b0439, JW0429

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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Protein attributes

Sequence length	784 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Degrades short-lived regulatory and abnormal proteins in presence of ATP. Degrades the regulatory proteins rcsA and sulA. Hydrolyzes two ATPs for each peptide bond cleaved in the protein substrate. Its overproduction specifically inhibits translation trough at least two different pathways, one of them being the yoeB-yefM toxin-antitoxin system.
Catalytic activity	Hydrolysis of proteins in presence of ATP.
Enzyme regulation	Contains an allosteric site (distinct from its active site), whose occupancy by an unfolded polypeptide leads to enzyme activation.
Subunit structure	Homotetramer.
Subcellular location	Cytoplasm.
Induction	By accumulation of abnormal proteins, such as at high temperatures. Under stress conditions.
Miscellaneous	Both its proteolytic and protein-activated ATPase activities are stimulated by DNA, especially single-stranded DNA.
Sequence similarities	Belongs to the peptidase S16 family. Contains 1 Lon domain.
Sequence caution	The sequence AAA23537.1 differs from that shown. Reason: Frameshift at position 16.

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Ontologies

Keywords
Biological process	Stress response
Cellular component	Cytoplasm
Ligand	ATP-binding DNA-binding Nucleotide-binding
Molecular function	Hydrolase Protease Serine protease
Technical term	3D-structure Allosteric enzyme Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: InterPro response to stress Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATP-dependent peptidase activity Inferred from electronic annotation. Source: InterPro DNA binding Inferred from electronic annotation. Source: UniProtKB-KW serine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 784

784

ATP-dependent protease La

PRO_0000076133

Regions

Domain

10 – 202

193

Lon

Nucleotide binding

356 – 363

ATP Potential

Compositional bias

211 – 219

Arg/Lys-rich (basic)

Compositional bias

240 – 252

Asp/Glu-rich (acidic)

Compositional bias

255 – 270

Arg/Lys-rich (basic)

Sites

Active site

679

Active site

722

Ref.13

Experimental info

Mutagenesis

362

K → A: Loss of proteolytic activity and ATP-binding. Ref.10

Mutagenesis

679

S → A: Loss of proteolytic activity. Ref.4

Sequence conflict

188

D → E Ref.3

Sequence conflict

264 – 317

PKEAK…LRQAQ → RKRQKRKRTGVAEAENDVSD VGRSDRSAWLYRLDGTGAVE CAYEGQKRPASGA Ref.5

Sequence conflict

273

A → R in AAA16837. Ref.4

Sequence conflict

307

S → T in AAA16837. Ref.4

Sequence conflict

539 – 563

AGVRG…LLLDK → RACVVWSVKSPNCVAKRLSS YCSIT in AAA24078. Ref.5

Sequence conflict

772

Q → R in AAA16837. Ref.4

Sequence conflict

779 – 784

QVVTAK → HHSLRRRCSTASTYYWAKS Ref.2

Secondary structure

784

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P0A9M0-1 [UniParc].

Last modified July 19, 2005. Version 1.
Checksum: 4042499C97694EF8
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FASTA

784

87,438

        10         20         30         40         50         60 
MNPERSERIE IPVLPLRDVV VYPHMVIPLF VGREKSIRCL EAAMDHDKKI MLVAQKEAST 

        70         80         90        100        110        120 
DEPGVNDLFT VGTVASILQM LKLPDGTVKV LVEGLQRARI SALSDNGEHF SAKAEYLESP 

       130        140        150        160        170        180 
TIDEREQEVL VRTAISQFEG YIKLNKKIPP EVLTSLNSID DPARLADTIA AHMPLKLADK 

       190        200        210        220        230        240 
QSVLEMSDVN ERLEYLMAMM ESEIDLLQVE KRIRNRVKKQ MEKSQREYYL NEQMKAIQKE 

       250        260        270        280        290        300 
LGEMDDAPDE NEALKRKIDA AKMPKEAKEK AEAELQKLKM MSPMSAEATV VRGYIDWMVQ 

       310        320        330        340        350        360 
VPWNARSKVK KDLRQAQEIL DTDHYGLERV KDRILEYLAV QSRVNKIKGP ILCLVGPPGV 

       370        380        390        400        410        420 
GKTSLGQSIA KATGRKYVRM ALGGVRDEAE IRGHRRTYIG SMPGKLIQKM AKVGVKNPLF 

       430        440        450        460        470        480 
LLDEIDKMSS DMRGDPASAL LEVLDPEQNV AFSDHYLEVD YDLSDVMFVA TSNSMNIPAP 

       490        500        510        520        530        540 
LLDRMEVIRL SGYTEDEKLN IAKRHLLPKQ IERNALKKGE LTVDDSAIIG IIRYYTREAG 

       550        560        570        580        590        600 
VRGLEREISK LCRKAVKQLL LDKSLKHIEI NGDNLHDYLG VQRFDYGRAD NENRVGQVTG 

       610        620        630        640        650        660 
LAWTEVGGDL LTIETACVPG KGKLTYTGSL GEVMQESIQA ALTVVRARAE KLGINPDFYE 

       670        680        690        700        710        720 
KRDIHVHVPE GATPKDGPSA GIAMCTALVS CLTGNPVRAD VAMTGEITLR GQVLPIGGLK 

       730        740        750        760        770        780 
EKLLAAHRGG IKTVLIPFEN KRDLEEIPDN VIADLDIHPV KRIEEVLTLA LQNEPSGMQV 


VTAK

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 8294008] [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: 3289547] [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: 2242054] [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: 8226758] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF SER-679.
[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: 3042779] [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]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] 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: 16738553] [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: 2984174] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-58, PROTEIN SEQUENCE OF 1-14.
[10]	"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: 7988699] [Abstract] Cited for: MUTAGENESIS OF LYS-362.
[11]	"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: 10094703] [Abstract] Cited for: MUTAGENESIS.
[12]	"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: 15009896] [Abstract] Cited for: INTERACTION WITH THE YOEB-YEFM TOXIN-ANTITOXIN SYSTEM. Strain: K12 / MG1655 / ATCC 47076.
[13]	"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: 14665623] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 585-784, ACTIVE SITE LYS-722.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

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.

PIR

A23101.
SUECLA. G64773.

RefSeq

AP_001089.1.
NP_414973.1.

3D structure databases

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	[»]

ModBase

Search...

Protein family/group databases

MEROPS

S16.001.

2-D gel databases

ECO2DBASE

H094.0. 6TH EDITION.
H094.1. 6TH EDITION.

Genome annotation databases

GeneID

945085.

GenomeReviews

Gene locus JW0429 in contig AP009048_GR.
Gene locus b0439 in contig U00096_GR.

KEGG

ecj:JW0429.
eco:b0439.

Organism-specific databases

EchoBASE

EB0537.

EcoGene

EG10542. lon.

CMR

Search...

Phylogenomic databases

HOGENOM

P0A9M0.

OMA

P0A9M0. VMKESIQ.

Enzyme and pathway databases

BioCyc

EcoCyc:EG10542-MON.

Family and domain databases

InterPro

IPR003593. ATPase_AAA+_core.
IPR003959. ATPase_AAA_core.
IPR008269. Pept_S16_C.
IPR004815. Pept_S16_lon.
IPR003111. Pept_S16_N.
IPR008268. Peptidase_S16_AS.
IPR001984. Peptidase_S16_C.
[Graphical view]

Pfam

PF00004. AAA. 1 hit.
PF02190. LON. 1 hit.
PF05362. Lon_C. 1 hit.
[Graphical view]

PRINTS

PR00830. ENDOLAPTASE.

SMART

SM00382. AAA. 1 hit.
SM00464. LON. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00763. lon. 1 hit.

PROSITE

PS01046. LON_SER. 1 hit.
[Graphical view]

ProtoNet

Search...

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Entry information

Entry name

LON_ECOLI

Accession

Primary (citable) accession number: P0A9M0
Secondary accession number(s): P08177, P78219, Q2MBY7

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	July 19, 2005
Last modified:	June 16, 2009
This is version 41 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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