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E0TR18 (E0TR18_STRZ6) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 21. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended name:
ATP-dependent Clp protease proteolytic subunit HAMAP-Rule MF_00444 RuleBase RU003567

EC=3.4.21.92 HAMAP-Rule MF_00444 RuleBase RU000549
Alternative name(s):
Endopeptidase Clp HAMAP-Rule MF_00444
Gene names
Name:clpP HAMAP-Rule MF_00444 EMBL ADM91633.1
Ordered Locus Names:SP670_1577 EMBL ADM91633.1
OrganismStreptococcus pneumoniae (strain 670-6B) [Complete proteome] [HAMAP] EMBL ADM91633.1
Taxonomic identifier189423 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length196 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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-Rule MF_00444 RuleBase RU000550

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-Rule MF_00444

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). RuleBase RU000549

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00444.

Sequence similarities

Belongs to the peptidase S14 family. HAMAP-Rule MF_00444 RuleBase RU003567

Ontologies

Keywords
   Cellular componentCytoplasm HAMAP-Rule MF_00444
   LigandATP-binding HAMAP-Rule MF_00444
Nucleotide-binding
   Molecular functionHydrolase
Protease
Serine protease HAMAP-Rule MF_00444 RuleBase RU000549
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processproteolysis

Inferred from electronic annotation. Source: UniProtKB-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: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site961 By similarity HAMAP-Rule MF_00444
Active site1211 By similarity HAMAP-Rule MF_00444

Sequences

Sequence LengthMass (Da)Tools
E0TR18 [UniParc].

Last modified November 2, 2010. 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

References

[1]"Structure and dynamics of the pan-genome of Streptococcus pneumoniae and closely related species."
Neuendorf B., Radune D., Fedorova N.B., Khouri H.M., Dodson R.J., Daugherty S.C., Hollingshead S., Tettelin H.
Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 670-6B EMBL ADM91633.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP002176 Genomic DNA. Translation: ADM91633.1.
RefSeqYP_003879733.1. NC_014498.1.

3D structure databases

ProteinModelPortalE0TR18.
SMRE0TR18. Positions 1-194.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADM91633; ADM91633; SP670_1577.
GeneID9730292.
KEGGsnb:SP670_1577.
PATRIC42517365. VBIStrPne54539_1666.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000285833.
KOK01358.
OMAERDYWMD.

Enzyme and pathway databases

BioCycSPNE189423:GHX7-1572-MONOMER.

Family and domain databases

HAMAPMF_00444. ClpP.
InterProIPR001907. ClpP.
IPR023562. ClpP/TepA.
IPR018215. ClpP_AS.
[Graphical view]
PANTHERPTHR10381. PTHR10381. 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 nameE0TR18_STRZ6
AccessionPrimary (citable) accession number: E0TR18
Entry history
Integrated into UniProtKB/TrEMBL: November 2, 2010
Last sequence update: November 2, 2010
Last modified: February 19, 2014
This is version 21 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)