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Q89A99 (LON_BUCBP) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Lon protease

EC=3.4.21.53
Alternative name(s):
ATP-dependent protease La
Gene names
Name:lon
Ordered Locus Names:bbp_421
OrganismBuchnera aphidicola subsp. Baizongia pistaciae (strain Bp) [Complete proteome] [HAMAP]
Taxonomic identifier224915 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera

Protein attributes

Sequence length780 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
   Technical termComplete proteome
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 – 780780Lon protease
PRO_0000076127

Regions

Domain10 – 201192Lon
Nucleotide binding356 – 3638ATP By similarity

Sites

Active site6791 By similarity
Active site7221 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q89A99 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 2C0AF017E21E6EAA

FASTA78088,203
        10         20         30         40         50         60 
MNPERSEYIE IPVLPLRDVV IYPYMVIPLF VGRDKSIKCI EASMNKNKKI MLVTQKEAEI 

        70         80         90        100        110        120 
DEPTDNDLFT IGTTASILQM LKLPDGTVKV LVEGLQRAKV KKINNENGYF TAQIQLICTP 

       130        140        150        160        170        180 
EITEKEQSIL IRTTLNQFEN YVKFNKKISP EILNSLNNIT NASQLSDMIA IHMPLKLSEK 

       190        200        210        220        230        240 
QSILETYNTN ERLERLMAIM ESEIDLLQVE KRIRNRVKKQ MEKSQREYYL NEQMKAIQKE 

       250        260        270        280        290        300 
LGEMDETLDE HEILKRKITT IKMPKEAQEK MASELHKLKM MSPMSAEATV VRSYIDWMIQ 

       310        320        330        340        350        360 
IPWNIRSKVK KNLTQAQKIL DSDHFGLDKV KERILEYLAV QSRINTVKGP ILCLVGPPGV 

       370        380        390        400        410        420 
GKTSLGQSIA RATGRKYIRM ALGGIRDEAE IRGHRRTYIG SMPGKIIQKM AKVGVKNPLF 

       430        440        450        460        470        480 
LLDEIDKMSC DIRVDPASAL LEVLDPEQNV AFNDHYLEVD YDLSNVMFIA TSNSTNIPAP 

       490        500        510        520        530        540 
LLDRMEIIRI SGYTEFEKLN IAKSYLKPKQ IKRNALKSNE LTIEDSVVTN IIRYYTREAG 

       550        560        570        580        590        600 
VRNLERELSK ICRKCVKNLI LNKSLKKIKI TTDNLHDYLG IKKYDFGKTN YKNQIGQVIG 

       610        620        630        640        650        660 
LAWTEVGGEL LTIEAACISG KGKLIYTGSL GEVMQESIQA ALTVVRSQAN KLGIKKNFYE 

       670        680        690        700        710        720 
KNDIHVHVPE GATPKDGPSA GIAMCTAIVS CLTGIPVKSD IAMTGEITLR GQILTIGGLK 

       730        740        750        760        770        780 
EKLLAAHRGG IKKVLIPYDN EKDLQEIPKT ILKGLFVHPV KHIKEVLNLS LENTPYFSSK 

« Hide

References

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016826 Genomic DNA. Translation: AAO27131.1.
RefSeqNP_778026.1. NC_004545.1.

3D structure databases

ProteinModelPortalQ89A99.
SMRQ89A99. Positions 9-117, 491-584, 594-775.
ModBaseSearch...

Protein family/group databases

MEROPSS16.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBUCT00000002268; EBBUCP00000002092; EBBUCG00000002268.
GeneID1058354.
GenomeReviewsGene locus bbp_421 in contig AE016826_GR.
KEGGbab:bbp421.
PATRIC21245659. VBIBucAph80364_0422.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000007957.
HOGENOMHBG566281.
OMAFMEGEIS.
PhylomeDBQ89A99.

Enzyme and pathway databases

BioCycBAPH224915:BBP_421-MONOMER.

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]
KOK01338.
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_BUCBP
AccessionPrimary (citable) accession number: Q89A99
Entry history
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: June 1, 2003
Last modified: January 25, 2012
This is version 66 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