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P36772 (LON_BRECH) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Lon protease

EC=3.4.21.53
Alternative name(s):
ATP-dependent protease La
Gene names
Name:lon
OrganismBrevibacillus choshinensis
Taxonomic identifier54911 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesPaenibacillaceaeBrevibacillus

Protein attributes

Sequence length779 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. 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 By similarity.

Catalytic activity

Hydrolysis of proteins in presence of ATP.

Subunit structure

Homohexamer. Organized in a ring with a central cavity By similarity.

Subcellular location

Cytoplasm.

Induction

By heat shock By similarity.

Sequence similarities

Belongs to the peptidase S16 family.

Contains 1 Lon domain.

Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-KW

response to stress

Inferred from electronic annotation. Source: UniProtKB-KW

   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 – 779779Lon protease
PRO_0000076120

Regions

Domain9 – 200192Lon
Nucleotide binding355 – 3628ATP By similarity

Sites

Active site6781 By similarity
Active site7211 By similarity

Sequences

Sequence LengthMass (Da)Tools
P36772 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: 625E0DA9B98941B5

FASTA77987,422
        10         20         30         40         50         60 
MGERSGKREL PLLPLRGLLV YPTMVLHLDV GREKSIRALE QAMVDDNKIL LATQEEVHIE 

        70         80         90        100        110        120 
EPDAEQIYSI GTVARVKQML KLPNGTIRVL VEGLQRAKIE EYLQKEDYFV VSITYLKEEK 

       130        140        150        160        170        180 
AEENEVEALM RSLLTHFEQY IKLSKKVSPE TLTSVQDIEE PGRLADVIAS HLPLKMKDKQ 

       190        200        210        220        230        240 
EILETVNIQE RLEILLTILN NEREVLELER KIGNRVKKQM ERTQKEYYLR EQMKAIQKEL 

       250        260        270        280        290        300 
GDKDGRQGEV DELRAQLEKS DAPERIKAKI EKELERLEKM PSTSAEGSVI RTYIDTLFAL 

       310        320        330        340        350        360 
PWTKTTEDNL DIKHAEEVLD EDHYGLEKPK ERVLEYLAVQ KLVNSMRGPI LCLVGPPGVG 

       370        380        390        400        410        420 
KTSLARSVAR ALGREFVRIS LGGVRDEAEI RGHRRTYVGA LPGRIIQGMK QAGTINPVFL 

       430        440        450        460        470        480 
LDEIDKLASD FRGDPASALL EVLDPNQNDK FSDHYIEETY DLTNVMFITT ANSLDTIPRP 

       490        500        510        520        530        540 
LLDRMEVISI SGYTELEKLN ILRGYLLPKQ MEDHGLGKDK LQMNEDAMLK LVRLYTREAG 

       550        560        570        580        590        600 
VRNLNREAAN VCRKAAKIIV GGEKKRVVVT AKTLEALLGK PRYRYGLAEK KDQVGSVTGL 

       610        620        630        640        650        660 
AWTQAGGDTL NVEVSILAGK GKLTLTGQLG DVMKESAQAA FSYIRSRASE WGIDPEFHEK 

       670        680        690        700        710        720 
NDIHIHVPEG AIPKDGPSAG ITMATALVSA LTGIPVKKEV GMTGEITLRG RVLPIGGLKE 

       730        740        750        760        770 
KCMSAHRAGL TTIILPKDNE KDIEDIPESV REALTFYPVE HLDEVLRHAL TKQPVGDKK 

« Hide

References

[1]"Cloning, characterization, and inactivation of the Bacillus brevis lon gene."
Ito K., Udaka S., Yamagata H.
J. Bacteriol. 174:2281-2287(1992) [PubMed: 1551846] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: HPD31.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D00863 Genomic DNA. Translation: BAA00737.1.

3D structure databases

ProteinModelPortalP36772.
SMRP36772. Positions 491-585, 593-774.
ModBaseSearch...

Protein family/group databases

MEROPSS16.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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.
IPR015947. PUA-like_domain.
IPR020568. Ribosomal_S5_D2-typ_fold.
[Graphical view]
PfamPF00004. AAA. 1 hit.
PF02190. LON. 1 hit.
PF05362. Lon_C. 1 hit.
[Graphical view]
PIRSFPIRSF001174. Lon_proteas. 1 hit.
SMARTSM00382. AAA. 1 hit.
SM00464. LON. 1 hit.
[Graphical view]
SUPFAMSSF88697. PUA-like. 1 hit.
SSF54211. Ribosomal_S5_D2-typ_fold. 1 hit.
TIGRFAMsTIGR00763. Lon. 1 hit.
PROSITEPS01046. LON_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLON_BRECH
AccessionPrimary (citable) accession number: P36772
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: January 25, 2012
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families