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Reviewed, UniProtKB/Swiss-Prot P46067 (LON_ERWAM)

Last modified June 16, 2009. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    ATP-dependent protease La
    EC=3.4.21.53
Gene names
Name: lon
OrganismErwinia amylovora (Fire blight bacteria)
Taxonomic identifier552 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeErwinia

Protein attributes

Sequence length784 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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 By similarity.

Catalytic activity

Hydrolysis of proteins in presence of ATP.

Subunit structure

Homotetramer By similarity.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the peptidase S16 family.

Contains 1 Lon domain.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionHydrolase
Protease
Serine protease
Gene Ontology (GO)
   Biological processproteolysis

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATP-dependent peptidase activity

Inferred from electronic annotation. Source: InterPro

serine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 784784ATP-dependent protease La
PRO_0000076135

Regions

Domain10 – 202193Lon
Nucleotide binding356 – 3638ATP Potential

Sites

Active site6791 By similarity
Active site7221 By similarity

Sequences

Sequence LengthMass (Da)Tools
P46067-1 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 1874DAE354EB05DB

FASTA78487,670
        10         20         30         40         50         60 
MNPERSERIE IPVLPLRDVV VYPHMVIPLF VGREKSIRCL EAAMDHDKKI MLVAQKEAST 

        70         80         90        100        110        120 
DEPGINDLFS VGTVASILQM LKLPDATVKV LVEGLQRARI SALSDNGDHF TAKAEYLTSP 

       130        140        150        160        170        180 
EIEEREQEVL VRTAINQFEG YIKLNKKIPP EVLTSLNSID DAARLADTVA AHMPLKLSDK 

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

       250        260        270        280        290        300 
LGEMDDAPDE NEALKRKIDA ARMPKEAREK TEAELQKLKM MSPMSAEATV VRGYIDWMVQ 

       310        320        330        340        350        360 
VPWNARSKVE KDLQKRRQTL DTDHFGLERV KDRILEYLAV QSRVSKIKGP ILCLVGPPGV 

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

       430        440        450        460        470        480 
LLDEIDKMSS DMRGDPASAL LEVLDPEQNI AFNDHYLEVD YDLSDVMFVA TSNSMNIPAP 

       490        500        510        520        530        540 
LLDRMEVIRL SGYTEDEKLN IAKKHLLSKQ IERNALKEHE LIVDDSAIVG IIRYYTRERG 

       550        560        570        580        590        600 
VRSLERELSK LCRKAVKTLL MDKSVKHIEI NADNLKDYLG VQRYDYGRAD SENRVGQVTG 

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

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

       730        740        750        760        770        780 
EKLLAAHRGG IKTVLIPDEN KRDLEEIPEN VIADLDIHPV KRIEEVLALA LQNAPYGMQV 


ASVK 

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References

[1]"Cloning, expression, and characterization of the lon gene of Erwinia amylovora: evidence for a heat shock response."
Eastgate J.A., Taylor N., Coleman M.J., Healy B., Thompson L., Roberts I.S.
J. Bacteriol. 177:932-937(1995) [PubMed: 7860603] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: OT1.

Cross-references

Sequence databases

X77706 Genomic DNA. Translation: CAA54779.1.
PIRS47270.

3D structure databases

SMRP46067. Positions 8-117, 491-584, 594-784.
ModBaseSearch...

Protein family/group databases

MEROPSS16.001.

Enzyme and pathway databases

BRENDA3.4.21.53. 81763.

Family and domain databases

InterProIPR003593. 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]
PfamPF00004. AAA. 1 hit.
PF02190. LON. 1 hit.
PF05362. Lon_C. 1 hit.
[Graphical view]
PRINTSPR00830. ENDOLAPTASE.
SMARTSM00382. AAA. 1 hit.
SM00464. LON. 1 hit.
[Graphical view]
TIGRFAMsTIGR00763. lon. 1 hit.
PROSITEPS01046. LON_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLON_ERWAM
AccessionPrimary (citable) accession number: P46067
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: June 16, 2009
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

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