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P77810 (LON_AZOBR) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 72. 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
OrganismAzospirillum brasilense
Taxonomic identifier192 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesRhodospirillaceaeAzospirillum

Protein attributes

Sequence length810 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. Involved in iron uptake.

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. Ref.1

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 – 810810Lon protease
PRO_0000076115

Regions

Domain17 – 206190Lon
Nucleotide binding361 – 3688ATP By similarity

Sites

Active site6851 By similarity
Active site7281 By similarity

Sequences

Sequence LengthMass (Da)Tools
P77810 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: 2833882C69886C4B

FASTA81090,143
        10         20         30         40         50         60 
MKEAQSMFEI PRGALYPVPP LRDIVVFPHM IVPLFVGREK SVRALEDVMK DDKQILLVTQ 

        70         80         90        100        110        120 
KNAAQDDPTP ADIYSVGTVG TVLQLLKLPD GTVKVLVEGG QRASITKFAE NEDFFQAHAD 

       130        140        150        160        170        180 
LVEEKVGESQ ELEALGRAVV SQFEQYIKLN KKIPPEVLVS INQIEEPGKL ADTVASHLAL 

       190        200        210        220        230        240 
KIPEKQQLLE CATVSERLER VYAFMEGEIG VLQVEKRIRN RVKRQMEKTQ REYYLNEQLK 

       250        260        270        280        290        300 
AIQKELGETE DGRDESAELE EKINKTRFSK EARDKALAEL KKLRSMSPMS AEATVVRNYL 

       310        320        330        340        350        360 
DWMLSIPWKK RTKVKKDLKL AQKILDADHY GLEKVKERIL EYLRVQNRMN KVKGPIQSLV 

       370        380        390        400        410        420 
GPPGVGKTSL GKSIAKSTGR NFVRMSLGGV RDEAEVRGHR RTYIGSMPGK VIQGMKKAKS 

       430        440        450        460        470        480 
SNPLFLLDEI DKLGADWRGD PSSALLEVLD PEQNGTFNDH YLEVDYDLSD VMFVCTANTM 

       490        500        510        520        530        540 
RMPQPLLDRM EIIRVAGYTE DEKVEISKRH LIEKQVEANG LKKGEFAISD DALRDLIRYY 

       550        560        570        580        590        600 
TREAGVRSLE REIANLCRKA VKEILMKGSA GAKVSVTRRN LDKYAGVRRF HFGEAELEDL 

       610        620        630        640        650        660 
VGVTTGLAWT EVGGELLSIE AVSLPGKGRV TTTGKLGDVM KESVQAAESY VKSRATAFGI 

       670        680        690        700        710        720 
KPTLFEKRDI HVHVPEGATP KDGPSAGVAM ITSIVSVLTG IAVRKDVAMT GEITLRGRVL 

       730        740        750        760        770        780 
PIGGLKEKLL AALRGGLKHV LIPKDNEKDL AEIPDNVKRG LEIIPVSTVD DVLKHALVRE 

       790        800        810 
VEPIEWKEPE AVEPAVAKPQ TDGGGEVLRH 

« Hide

References

[1]"Cloning, nucleotide sequencing, and expression of the Azospirillum brasilense lon gene: involvement in iron uptake."
Mori E., Fulchieri M., Indorato C., Fani R., Bazzicalupo M.
J. Bacteriol. 178:3440-3446(1996) [PubMed: 8655539] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION.
Strain: SpF94.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U35611 Genomic DNA. Translation: AAB16819.1.
PIRJC6045.

3D structure databases

ProteinModelPortalP77810.
SMRP77810. Positions 17-120, 496-592, 601-780.
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_AZOBR
AccessionPrimary (citable) accession number: P77810
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: February 1, 1997
Last modified: January 25, 2012
This is version 72 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