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Reviewed, UniProtKB/Swiss-Prot P38002 (CLPP1_CHLTR)

Last modified November 3, 2009. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    ATP-dependent Clp protease proteolytic subunit 1
    EC=3.4.21.92
Alternative name(s):
    Endopeptidase Clp 1
Gene names
Name: clpP1
Ordered Locus Names: CT_431
OrganismChlamydia trachomatis [Complete proteome] [HAMAP]
Taxonomic identifier813 [NCBI]
Taxonomic lineageBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia

Protein attributes

Sequence length192 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins By similarity.

Catalytic activity

Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. Alpha-casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec; and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds also occurs). HAMAP MF_00444

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the peptidase S14 family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionHydrolase
Protease
Serine protease
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processproteolysis

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

serine-type endopeptidase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 192191ATP-dependent Clp protease proteolytic subunit 1 HAMAP MF_00444
PRO_0000179535

Sites

Active site921 By similarity
Active site1171 By similarity

Sequences

Sequence LengthMass (Da)Tools
P38002-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 33EEEE8CD3B8AACE

FASTA19221,162
        10         20         30         40         50         60 
MPEGEMMHKL QDVIDRKLLD SRRIFFSEPV TEKSATEAIK KLWYLELTNP GQPIVFVINS 

        70         80         90        100        110        120 
PGGSVDAGFA VWDQIKMISS PLTTVVTGLA ASMGSVLSLC AVPGRRFATP HARIMIHQPS 

       130        140        150        160        170        180 
IGGTITGQAT DLDIHAREIL KTKARIIDVY VEATGQSREV IEKAIDRDMW MSANEAMEFG 

       190 
LLDGILFSFN DL 

« Hide

References

[1]"Genome sequence of an obligate intracellular pathogen of humans: Chlamydia trachomatis."
Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L., Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.
Science 282:754-759(1998) [PubMed: 9784136] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: D/UW-3/Cx.

Cross-references

Sequence databases

AE001273 Genomic DNA. Translation: AAC68028.1.
PIRG71516.
RefSeqNP_219943.1.

3D structure databases

HSSPHSSP built from PDB template 1TYF based on UniProtKB P19245.
ModBaseSearch...

Protein family/group databases

MEROPSS14.005.

2-D gel databases

PHCI-2DPAGEP38002.
Siena-2DPAGEP38002.

Genome annotation databases

GeneID884217.
GenomeReviewsGene locus CT_431 in contig AE001273_GR.
KEGGctr:CT431.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMP38002.
OMATPHSRIM.

Enzyme and pathway databases

BioCycCTRA315277:CT431-MON.
BRENDA3.4.21.92. 108.

Family and domain databases

HAMAPMF_00444.
[Tree]
InterProIPR001907. Pept_S14_ClpP.
IPR018215. Pept_S14_ClpP_AS.
[Graphical view]
PANTHERPTHR10381. Pept_S14_ClpP. 1 hit.
PfamPF00574. CLP_protease. 1 hit.
[Graphical view]
PRINTSPR00127. CLPPROTEASEP.
PROSITEPS00382. CLP_PROTEASE_HIS. 1 hit.
PS00381. CLP_PROTEASE_SER. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCLPP1_CHLTR
AccessionPrimary (citable) accession number: P38002
Secondary accession number(s): O84438
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: January 23, 2007
Last modified: November 3, 2009
This is version 66 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents