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Q68WS8

- LON_RICTY

UniProt

Q68WS8 - LON_RICTY

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Protein
Lon protease
Gene
lon, RT0437
Organism
Rickettsia typhi (strain ATCC VR-144 / Wilmington)
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

Functioni

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.UniRule annotation

Catalytic activityi

Hydrolysis of proteins in presence of ATP.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei679 – 6791 By similarity
Active sitei722 – 7221 By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi356 – 3638ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-HAMAP
  2. ATP-dependent peptidase activity Source: UniProtKB-HAMAP
  3. sequence-specific DNA binding Source: UniProtKB-HAMAP
  4. serine-type endopeptidase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. cellular response to stress Source: UniProtKB-HAMAP
  2. misfolded or incompletely synthesized protein catabolic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Stress response

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciRTYP257363:GJEQ-459-MONOMER.

Protein family/group databases

MEROPSiS16.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Lon protease (EC:3.4.21.53)
Alternative name(s):
ATP-dependent protease La
Gene namesi
Name:lon
Ordered Locus Names:RT0437
OrganismiRickettsia typhi (strain ATCC VR-144 / Wilmington)
Taxonomic identifieri257363 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiatyphus group
ProteomesiUP000000604: Chromosome

Subcellular locationi

Cytoplasm By similarity UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 784784Lon proteaseUniRule annotation
PRO_0000280894Add
BLAST

Expressioni

Inductioni

By heat shock By similarity.UniRule annotation

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi257363.RT0437.

Structurei

3D structure databases

ProteinModelPortaliQ68WS8.
SMRiQ68WS8. Positions 594-775.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini6 – 203198Lon
Add
BLAST

Sequence similaritiesi

Belongs to the peptidase S16 family.
Contains 1 Lon domain.

Phylogenomic databases

eggNOGiCOG0466.
HOGENOMiHOG000261410.
KOiK01338.
OMAiITEYTEL.
OrthoDBiEOG6XHC23.

Family and domain databases

Gene3Di3.30.230.10. 1 hit.
3.40.50.300. 1 hit.
HAMAPiMF_01973. lon_bact.
InterProiIPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR027543. Lon_bac.
IPR004815. Lon_bac/euk-typ.
IPR027065. Lon_Prtase.
IPR027417. P-loop_NTPase.
IPR008269. Pept_S16_C.
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]
PANTHERiPTHR10046. PTHR10046. 1 hit.
PfamiPF00004. AAA. 1 hit.
PF02190. LON. 1 hit.
PF05362. Lon_C. 1 hit.
[Graphical view]
PIRSFiPIRSF001174. Lon_proteas. 1 hit.
SMARTiSM00382. AAA. 1 hit.
SM00464. LON. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
SSF54211. SSF54211. 1 hit.
SSF88697. SSF88697. 1 hit.
TIGRFAMsiTIGR00763. lon. 1 hit.
PROSITEiPS01046. LON_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q68WS8-1 [UniParc]FASTAAdd to Basket

« Hide

MNKKSLPLMA LRDMVLFPGV IAPIFVGRKK SLQALSRTTI SEENNTKYIL    50
VTLQKKFDQE NPSKHELYNT AILAKIIQIV KLPNNTAKIL IEAVARVKLS 100
DIKDEESFEA NYEIIPDEEI LDMHNMRSLV DNAVQLFNKY AMNDKKVNTE 150
IIETINKEIS NKTNFINIIN ILASHLITSL ETKQQLLEET SPVKRITTVI 200
TTLTSNIVNS ETEHALQQRV RKQIEKTQRD YYLHEQMKAI QKELDEDKSE 250
LADIEKKIKS LKLSKEAKEK AESEFKKLRA MNQMSAESGV TRNYLETLLS 300
LPWGKYDNSK IDINQAEKIL NRDHFGLEKV KERIIEYLAV LQRSNKIRGP 350
ILCLIGPPGV GKTSLVKSIA EGMGRKYAKF SLGGVRDEAE IRGHRKTYLG 400
SMPGKILGQL KKVKTSNPVM LLDEIDKMSS DFRGDPASAL LEVLDPEQNS 450
HFVDHYLEVE YDLSNVVFIA TANSHDLPRA LSDRMEKIYI SGYVEEEKLQ 500
IAKNYLVPKQ FKVHKIKKDE ITISEDAILD LIRYYTKESG VRALEREICA 550
LTRKALKQIL ADNTVKNISI DSNNLEEFLG AKKYNFGLVE KEDQIGSTTG 600
LAYTEVGGEL LTIEALAFSG KGEIKTTGKL GDVMKESAMA AYSCFRSRAP 650
NFGLKYDNYK DFDIHIHVPA GAIPKDGPSA GCALFTTIVS LMTKIPVHRT 700
VAMTGEITLR GNVLPIGGLK EKLLAASRGG IKTVLIPEEN VKDLKDIPPN 750
IKENLEIISV SNIDQVLKHA LVEMPINKGL SYDL 784
Length:784
Mass (Da):88,102
Last modified:October 11, 2004 - v1
Checksum:i1475B928B9428BC7
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE017197 Genomic DNA. Translation: AAU03914.1.
RefSeqiYP_067396.1. NC_006142.1.

Genome annotation databases

EnsemblBacteriaiAAU03914; AAU03914; RT0437.
GeneIDi2958989.
KEGGirty:RT0437.
PATRICi17910112. VBIRicTyp34752_0468.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE017197 Genomic DNA. Translation: AAU03914.1 .
RefSeqi YP_067396.1. NC_006142.1.

3D structure databases

ProteinModelPortali Q68WS8.
SMRi Q68WS8. Positions 594-775.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 257363.RT0437.

Protein family/group databases

MEROPSi S16.001.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAU03914 ; AAU03914 ; RT0437 .
GeneIDi 2958989.
KEGGi rty:RT0437.
PATRICi 17910112. VBIRicTyp34752_0468.

Phylogenomic databases

eggNOGi COG0466.
HOGENOMi HOG000261410.
KOi K01338.
OMAi ITEYTEL.
OrthoDBi EOG6XHC23.

Enzyme and pathway databases

BioCyci RTYP257363:GJEQ-459-MONOMER.

Family and domain databases

Gene3Di 3.30.230.10. 1 hit.
3.40.50.300. 1 hit.
HAMAPi MF_01973. lon_bact.
InterProi IPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR027543. Lon_bac.
IPR004815. Lon_bac/euk-typ.
IPR027065. Lon_Prtase.
IPR027417. P-loop_NTPase.
IPR008269. Pept_S16_C.
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 ]
PANTHERi PTHR10046. PTHR10046. 1 hit.
Pfami PF00004. AAA. 1 hit.
PF02190. LON. 1 hit.
PF05362. Lon_C. 1 hit.
[Graphical view ]
PIRSFi PIRSF001174. Lon_proteas. 1 hit.
SMARTi SM00382. AAA. 1 hit.
SM00464. LON. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 1 hit.
SSF54211. SSF54211. 1 hit.
SSF88697. SSF88697. 1 hit.
TIGRFAMsi TIGR00763. lon. 1 hit.
PROSITEi PS01046. LON_SER. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC VR-144 / Wilmington.

Entry informationi

Entry nameiLON_RICTY
AccessioniPrimary (citable) accession number: Q68WS8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: October 11, 2004
Last modified: May 14, 2014
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. Rickettsia typhi
    Rickettsia typhi (strain Wilmington): entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi