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Protein

ATP-dependent Clp protease proteolytic subunit

Gene

clpP

Organism
Escherichia coli (strain UTI89 / UPEC)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

Functioni

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.UniRule annotation

Catalytic activityi

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).UniRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei111NucleophileUniRule annotation1
Active sitei136UniRule annotation1

GO - Molecular functioni

Keywordsi

Molecular functionHydrolase, Protease, Serine protease

Protein family/group databases

MEROPSiS14.001

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-dependent Clp protease proteolytic subunitUniRule annotation (EC:3.4.21.92UniRule annotation)
Alternative name(s):
Endopeptidase ClpUniRule annotation
Gene namesi
Name:clpPUniRule annotation
Ordered Locus Names:UTI89_C0465
OrganismiEscherichia coli (strain UTI89 / UPEC)
Taxonomic identifieri364106 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000001952 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
PropeptideiPRO_00002680131 – 14By similarityAdd BLAST14
ChainiPRO_000025281615 – 207ATP-dependent Clp protease proteolytic subunitAdd BLAST193

Keywords - PTMi

Zymogen

Interactioni

Subunit structurei

Fourteen ClpP subunits assemble into 2 heptameric rings which stack back to back to give a disk-like structure with a central cavity, resembling the structure of eukaryotic proteasomes. Component of the ClpAP and ClpXP complexes.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ1RF98
SMRiQ1RF98
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S14 family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000285833
KOiK01358
OMAiKPPIATW

Family and domain databases

CDDicd07017 S14_ClpP_2, 1 hit
HAMAPiMF_00444 ClpP, 1 hit
InterProiView protein in InterPro
IPR001907 ClpP
IPR029045 ClpP/crotonase-like_dom_sf
IPR023562 ClpP/TepA
IPR033135 ClpP_His_AS
IPR018215 ClpP_Ser_AS
PANTHERiPTHR10381 PTHR10381, 1 hit
PfamiView protein in Pfam
PF00574 CLP_protease, 1 hit
PRINTSiPR00127 CLPPROTEASEP
SUPFAMiSSF52096 SSF52096, 1 hit
TIGRFAMsiTIGR00493 clpP, 1 hit
PROSITEiView protein in PROSITE
PS00382 CLP_PROTEASE_HIS, 1 hit
PS00381 CLP_PROTEASE_SER, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q1RF98-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSYSGERDNF APHMALVPMV IEQTSRGERS FDIYSRLLKE RVIFLTGQVE
60 70 80 90 100
DHMANLIVAQ MLFLEAENPE KDIYLYINSP GGVITAGMSI YDTMQFIKPD
110 120 130 140 150
VSTICMGQAA SMGAFLLTAG AKGKRFCLPN SRVMIHQPLG GYQGQATDIE
160 170 180 190 200
IHAREILKVK GRMNELMALH TGQSLEQIER DTERDRFLSA PEAVEYGLVD

SILTHRN
Length:207
Mass (Da):23,187
Last modified:May 16, 2006 - v1
Checksum:iA7843D036C8CB3C2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000243 Genomic DNA Translation: ABE05966.1
RefSeqiWP_000122253.1, NC_007946.1

Genome annotation databases

EnsemblBacteriaiABE05966; ABE05966; UTI89_C0465
KEGGieci:UTI89_C0465

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000243 Genomic DNA Translation: ABE05966.1
RefSeqiWP_000122253.1, NC_007946.1

3D structure databases

ProteinModelPortaliQ1RF98
SMRiQ1RF98
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiS14.001

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABE05966; ABE05966; UTI89_C0465
KEGGieci:UTI89_C0465

Phylogenomic databases

HOGENOMiHOG000285833
KOiK01358
OMAiKPPIATW

Family and domain databases

CDDicd07017 S14_ClpP_2, 1 hit
HAMAPiMF_00444 ClpP, 1 hit
InterProiView protein in InterPro
IPR001907 ClpP
IPR029045 ClpP/crotonase-like_dom_sf
IPR023562 ClpP/TepA
IPR033135 ClpP_His_AS
IPR018215 ClpP_Ser_AS
PANTHERiPTHR10381 PTHR10381, 1 hit
PfamiView protein in Pfam
PF00574 CLP_protease, 1 hit
PRINTSiPR00127 CLPPROTEASEP
SUPFAMiSSF52096 SSF52096, 1 hit
TIGRFAMsiTIGR00493 clpP, 1 hit
PROSITEiView protein in PROSITE
PS00382 CLP_PROTEASE_HIS, 1 hit
PS00381 CLP_PROTEASE_SER, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiCLPP_ECOUT
AccessioniPrimary (citable) accession number: Q1RF98
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 17, 2006
Last sequence update: May 16, 2006
Last modified: November 7, 2018
This is version 79 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Peptidase families
    Classification of peptidase families and list of entries
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Main funding by: National Institutes of Health

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