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Q1RID6 (LON_RICBR) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 56. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
Ordered Locus Names:RBE_0797
OrganismRickettsia bellii (strain RML369-C) [Complete proteome] [HAMAP]
Taxonomic identifier336407 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Rickettsiaceae › Rickettsieae › Rickettsia › belli group ›

Protein attributes

Sequence length775 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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. HAMAP-Rule MF_01973

Catalytic activity

Hydrolysis of proteins in presence of ATP. HAMAP-Rule MF_01973

Subunit structure

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

Subcellular location

Cytoplasm By similarity.

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_processmisfolded or incompletely synthesized protein catabolic process

Inferred from electronic annotation. Source: InterPro

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 – 775775Lon protease HAMAP-Rule MF_01973
PRO_0000280891

Regions

Domain6 – 204199Lon
Nucleotide binding356 – 3638ATP By similarity

Sites

Active site6791 By similarity
Active site7221 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1RID6 [UniParc].

Last modified May 16, 2006. Version 1.
Checksum: 5F0AB73EE9EA39A8

FASTA77586,722
        10         20         30         40         50         60 
MNKKSLPLMA LRDIVVFPGV IAPVFVGRQK SLHALSNTTL SEEDNSKYIL VTLQKKFDQE 

        70         80         90        100        110        120 
NPNRNELYDV GILAKVIQIV KLPNTTAKIL VEAIARVKIS NIKGDEAFEA NYEIIPDEEI 

       130        140        150        160        170        180 
FDANNMRSLV DNAVQLFAKY AGSDKKINAE IIETINKEIS ETSNFINIIN ILASHLITSL 

       190        200        210        220        230        240 
EEKQRLLEET SPFKRISTII NILTSNIVNS ETEQALQQRV KKQIEKTQRD YYLHEQMKAI 

       250        260        270        280        290        300 
QKELDEDKSD LAEFDKKIKA AKLSKEAREK AEAELKKLRT MNQMSAESGV TRNYLETLLS 

       310        320        330        340        350        360 
LPWGKYDNSK IDINQAEKIL NRDHFGLEKV KERIIEYLAV LQRSSKIRGP ILCLIGPPGV 

       370        380        390        400        410        420 
GKTSLIKSIA EGMGRKYTKF ALGGVRDEAE IRGHRKTYLG SMPGKILTQL KKVKTSNPVM 

       430        440        450        460        470        480 
LLDEIDKMGS DFRGDPASAL LEVLDPEQNS HFVDHYLEVE YDLSNVIFIA TANSYNLPRA 

       490        500        510        520        530        540 
LIDRMEIIDI SGYMEEEKIQ IAKNYLVPKQ LKMHKIKKDE ITISDDAILD LIRYYTKESG 

       550        560        570        580        590        600 
VRSLEREIGA LTRKALKQIL ADKKVKHISV DSNNLEEFLG ARKYNFGLAE KNDQIGSTTG 

       610        620        630        640        650        660 
LAYTEVGGEL LTIEALSFPG KGEIKTTGKL GDVMKESAMA AYSCFRSRAA DFGLKYEDYK 

       670        680        690        700        710        720 
DFDVHIHVPA GAIPKDGPSA GCALFTTIVS LMTKIPVRRT VAMTGEVTLR GNVLPIGGLK 

       730        740        750        760        770 
EKLLAASRGG IKTVLIPEEN VKDLKDIPPN IKSSLEIIPV SNIDQVLEHA LTKKT

« Hide

References

[1]"Genome sequence of Rickettsia bellii illuminates the role of amoebae in gene exchanges between intracellular pathogens."
Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C., Fournier P.-E., Claverie J.-M., Raoult D.
PLoS Genet. 2:733-744(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RML369-C.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000087 Genomic DNA. Translation: ABE04878.1.
RefSeqYP_537967.1. NC_007940.1.

3D structure databases

ProteinModelPortalQ1RID6.
SMRQ1RID6. Positions 491-584, 594-774.
ModBaseSearch...

Protein-protein interaction databases

STRING336407.RBE_0797.

Protein family/group databases

MEROPSS16.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABE04878; ABE04878; RBE_0797.
GeneID3995620.
KEGGrbe:RBE_0797.
PATRIC17883093. VBIRicBel102610_0910.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0466.
HOGENOMHOG000261410.
KOK01338.
OMAMSKVGVK.
ProtClustDBCLSK870932.

Enzyme and pathway databases

BioCycRBEL336407:GJCY-819-MONOMER.

Family and domain databases

Gene3D3.30.230.10. 1 hit.
HAMAPMF_01973. lon_bact.
InterProIPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR027065. Lon_Prtase.
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.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
[Graphical view]
PANTHERPTHR10046. PTHR10046. 1 hit.
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_RICBR
AccessionPrimary (citable) accession number: Q1RID6
Entry history
Integrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: May 16, 2006
Last modified: May 1, 2013
This is version 56 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

Rickettsia bellii strain RML369-C

Rickettsia bellii (strain RML369-C): entries and gene names

SIMILARITY comments

Index of protein domains and families

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