Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q9PK50 (LON_CHLMU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 75. 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:TC_0623
OrganismChlamydia muridarum [Complete proteome] [HAMAP]
Taxonomic identifier83560 [NCBI]
Taxonomic lineageBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydia

Protein attributes

Sequence length819 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.

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 – 819819Lon protease
PRO_0000076130

Regions

Domain41 – 237197Lon
Nucleotide binding392 – 3998ATP By similarity

Sites

Active site7241 By similarity
Active site7671 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9PK50 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: DD87D5D701E1B063

FASTA81991,844
        10         20         30         40         50         60 
MNSTNNTDSQ NLDPNASEVE KLLDESAEAE EKTDDHTPPS ELFILPLNKR PFFPGMAAPL 

        70         80         90        100        110        120 
LIEAGPHYEV LTLLAKSSQK HIGLVLTKKE DANTLKIGFN QLHRVGVSAR ILRIMPIEGG 

       130        140        150        160        170        180 
SAQVLLSIED RIRIVKPVQD KYLKAKVAYH KENKELTEEL KAYSISIVSI IKDLLKLNPL 

       190        200        210        220        230        240 
FKEELQIFLG HSDFTEPGKL ADFSVALTTA TREELQEVLE TTDMHDRIDK ALVLLKKELD 

       250        260        270        280        290        300 
LSRLQSSINQ KIEATITKSQ KEFFLKEQLK TIKKELGLEK DDHAVDLEKF MERLNKRDVP 

       310        320        330        340        350        360 
QYAMDVIQDE MDKLQTLETS SAEYAVCRNY LDWLTIVPWG IQTKEYHDLK KAESILNKDH 

       370        380        390        400        410        420 
YGLEDIKQRI LELISVGKLA NGMKGSIICL VGPPGVGKTS IGRSIAKVLH RKFFRFSVGG 

       430        440        450        460        470        480 
MRDEAEIKGH RRTYIGAMPG KLVQALKQSA IMNPVIMIDE VDKIGSSYHG DPASALLEVL 

       490        500        510        520        530        540 
DPEQNKDFLD HYLDVRVDLS NVLFILTANV LDSIPDPLLD RMEVLRLSGY ILEEKLQIAT 

       550        560        570        580        590        600 
KYLVPRARKE MGLSAQNVSF QPEALKHMIN NYAREAGVRT LNENIKKVLR KVALKIVQNQ 

       610        620        630        640        650        660 
EKNPSKKSRF TITPKNLQDY LGKPIFSSDR FYEKTPVGVA TGLAWTSLGG ATLYIESVQV 

       670        680        690        700        710        720 
PSSSGKADMH LTGQAGDVMK ESSQIAWTYL HSALERYAPG RPFFEKSQVH IHIPEGATPK 

       730        740        750        760        770        780 
DGPSAGITMV TSLLSLLLDV PVLNNLGMTG ELTLTGRVLG IGGIREKLIA ARRSKLNVLI 

       790        800        810 
FPEDNRRDYD ELPAYLKKGL KVHFVTHYDD VFKIAFPGV 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE002160 Genomic DNA. Translation: AAF39454.1.
PIRE81681.
RefSeqNP_296997.1. NC_002620.2.

3D structure databases

ProteinModelPortalQ9PK50.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1245983.
GenomeReviewsGene locus TC_0623 in contig AE002160_GR.
KEGGcmu:TC0623.
PATRIC20372698. VBIChlMur19118_0662.
TIGRTC_0623.

Phylogenomic databases

HOGENOMHBG566281.
OMALPEPNRG.
PhylomeDBQ9PK50.
ProtClustDBCLSK2459232.

Enzyme and pathway databases

BioCycCMUR243161:TC_0623-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_CHLMU
AccessionPrimary (citable) accession number: Q9PK50
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: October 1, 2000
Last modified: January 25, 2012
This is version 75 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