Skip Header

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

P63788 (CLPP_STRR6) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 54. 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
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
ATP-dependent Clp protease proteolytic subunit
EC=3.4.21.92
Alternative name(s):
Endopeptidase Clp
Gene names
Name:clpP
Ordered Locus Names:spr0656
OrganismStreptococcus pneumoniae (strain ATCC BAA-255 / R6)
Taxonomic identifier171101 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Lactobacillales › Streptococcaceae › Streptococcus

Protein attributes

Sequence length196 AA.
Sequence statusComplete.
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. HAMAP MF_00444

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 HAMAP MF_00444.

Sequence similarities

Belongs to the peptidase S14 family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionHydrolase
Protease
Serine protease
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological processproteolysis

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

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 – 196196ATP-dependent Clp protease proteolytic subunit HAMAP MF_00444
PRO_0000179671

Sites

Active site961 By similarity
Active site1211 By similarity

Secondary structure

1 ............................ 196
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P63788 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: 2C6C3A820A290B2B

FASTA19621,358
        10         20         30         40         50         60 
MIPVVIEQTS RGERSYDIYS RLLKDRIIML TGPVEDNMAN SVIAQLLFLD AQDSTKDIYL 

        70         80         90        100        110        120 
YVNTPGGSVS AGLAIVDTMN FIKADVQTIV MGMAASMGTV IASSGAKGKR FMLPNAEYMI 

       130        140        150        160        170        180 
HQPMGGTGGG TQQTDMAIAA EHLLKTRNTL EKILAENSGQ SMEKVHADAE RDNWMSAQET 

       190 
LEYGFIDEIM ANNSLN

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE007317 Genomic DNA. Translation: AAK99460.1.
PIRH97953.
RefSeqNP_358250.1. NC_003098.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1Y7OX-ray2.51A/B/C/D/E/F/G1-196[»]
ProteinModelPortalP63788.
SMRP63788. Positions 1-194.
ModBaseSearch...

Protein-protein interaction databases

STRINGP63788.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBSTRT00000014498; EBSTRP00000013894; EBSTRG00000014498.
GeneID934194.
GenomeReviewsGene locus spr0656 in contig AE007317_GR.
KEGGspr:spr0656.
PATRIC19701211. VBIStrPne107296_0728.

Phylogenomic databases

eggNOGCOG0740.
GeneTreeEBGT00050000027049.
HOGENOMHBG558421.
OMAERDYWMD.
PhylomeDBP63788.
ProtClustDBPRK00277.

Enzyme and pathway databases

BioCycSPNE171101:SPR0656-MONOMER.

Family and domain databases

HAMAPMF_00444. ClpP.
[Tree]
InterProIPR023562. Pept_S14/S49.
IPR001907. Pept_S14_ClpP.
IPR018215. Pept_S14_ClpP_AS.
[Graphical view]
KOK01358.
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. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCLPP_STRR6
AccessionPrimary (citable) accession number: P63788
Secondary accession number(s): P58279
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: January 25, 2012
This is version 54 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents