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Q92HZ1 (LON_RICCN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:RC0629
OrganismRickettsia conorii (strain ATCC VR-613 / Malish 7) [Complete proteome] [HAMAP]
Taxonomic identifier272944 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiaspotted fever group

Protein attributes

Sequence length778 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 By similarity.

Induction

By heat shock By similarity.

Sequence similarities

Belongs to the peptidase S16 family.

Contains 1 Lon domain.

Sequence caution

The sequence AAL03167.1 differs from that shown. Reason: Erroneous initiation.

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 – 778778Lon protease
PRO_0000280892

Regions

Domain6 – 204199Lon
Nucleotide binding356 – 3638ATP By similarity

Sites

Active site6791 By similarity
Active site7221 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q92HZ1 [UniParc].

Last modified March 20, 2007. Version 2.
Checksum: 2039A138A9C8F956

FASTA77887,000
        10         20         30         40         50         60 
MHKKSLPLMA LRDMVVFPGV IAPIFVGRPK SLQALSHTTI SEEDNSKYIL VTLQKKFDQE 

        70         80         90        100        110        120 
NPSTHELYNT AILAKIIQIV KLPNNTAKIL IEAVARVKLS NIKGEEAFEA NYEIIPDEEI 

       130        140        150        160        170        180 
FDVNNMRSLV DNAVQLFSKY AINDKKVNAE IIETINKEIS NSTNFIDIIN ILASHLITSL 

       190        200        210        220        230        240 
EAKQHLLEET SPFKRITTVI SMLNSNIVNS ETEQALQKRV RKQIEKTQRD YYLHEQMKAI 

       250        260        270        280        290        300 
QKELDEDKSE LADIENKIKS LKLSKEAKEK AEAELKKLRT MNQMSAESGV TRNYLETLLS 

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

       370        380        390        400        410        420 
GKTSLVKSIA EGMGRKYTKL ALGGVRDEAE IRGHRKTYLG SMPGKILGQL KKVKTSNPVM 

       430        440        450        460        470        480 
LLDEIDKMSS DFRGDPASAL LEVLDPEQNS HFVDHYLEVE YDLSNVIFIA TANSHDLPRA 

       490        500        510        520        530        540 
LSDRMEKIYI SGYVEETKLQ IARNYLVPKQ FKMHKIKKDE ITISETAILD LIRYYTKESG 

       550        560        570        580        590        600 
VRALEREIGA LTRKALKQIL ADKSVKHIAI DSNHLEEFLG AKKYNFGLAE KEDQIGSTTG 

       610        620        630        640        650        660 
LAYTEVGGEL LTIEALAFPG KGEIKTTGKL GDVMKESAMA AYSCFRSRAT NFGLKYDNYK 

       670        680        690        700        710        720 
DFDIHIHVPA GAIPKDGPSA GCALFTTIVS LMTKIPVHRT VAMTGEITLR GNVLPIGGLK 

       730        740        750        760        770 
EKLLAASRGG IKTVLIPEEN VKDLKDIPPN IKESLEIISV SNIDQVLKHA LVGTPINK 

« Hide

References

[1]"Mechanisms of evolution in Rickettsia conorii and R. prowazekii."
Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V., Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.
Science 293:2093-2098(2001) [PubMed: 11557893] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC VR-613 / Malish 7.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE006914 Genomic DNA. Translation: AAL03167.1. Different initiation.
PIRE97778.
RefSeqNP_360266.1. NC_003103.1.

3D structure databases

HSSPHSSP built from PDB template 1RR9 based on UniProtKB P0A9M0.
ProteinModelPortalQ92HZ1.
SMRQ92HZ1. Positions 491-584, 594-775.
ModBaseSearch...

Protein family/group databases

MEROPSS16.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID927716.
GenomeReviewsGene locus RC0629 in contig AE006914_GR.
KEGGrco:RC0629.
NMPDRfig|272944.1.peg.629.
PATRIC17888528. VBIRicCon45613_0715.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAFMEGEIS.
ProtClustDBCLSK870932.

Enzyme and pathway databases

BioCycRCON272944:RC0629-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_RICCN
AccessionPrimary (citable) accession number: Q92HZ1
Entry history
Integrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: March 20, 2007
Last modified: January 25, 2012
This is version 69 of the entry and version 2 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 conorii

(strain Malish 7): entries and gene names

SIMILARITY comments

Index of protein domains and families