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Protein

ATP-dependent Clp protease proteolytic subunit 1

Gene

clpP1

Organism
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

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 (By similarity). Probably partially responsible for degradation of ECF sigma factor SigR prime.UniRule annotation1 Publication

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 sitei113NucleophileUniRule annotation1
Active sitei138UniRule annotation1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Protein family/group databases

MEROPSiS14.008.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-dependent Clp protease proteolytic subunit 1UniRule annotation (EC:3.4.21.92UniRule annotation)
Alternative name(s):
Endopeptidase Clp 1UniRule annotation
Gene namesi
Name:clpP1UniRule annotation
Ordered Locus Names:SCO2619
ORF Names:SCC80.04c
OrganismiStreptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Taxonomic identifieri100226 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomycesStreptomyces albidoflavus group
Proteomesi
  • UP000001973 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

A double clpP1-clpP2 deletion increases the stability of ECF sigma factor SigR prime from 10 to 23 minutes.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001796641 – 219ATP-dependent Clp protease proteolytic subunit 1Add BLAST219

Proteomic databases

PRIDEiQ9F315.

Expressioni

Inductioni

Expressed from 2 promoters, 1 of which (clpP2) is positively regulated by the thio-oxidizing agent diamide, probably via SigR. Probably a clpP1-clpP2 operon.1 Publication

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.UniRule annotation

Protein-protein interaction databases

STRINGi100226.SCO2619.

Structurei

3D structure databases

ProteinModelPortaliQ9F315.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S14 family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CCQ. Bacteria.
COG0740. LUCA.
HOGENOMiHOG000285833.
InParanoidiQ9F315.
KOiK01358.
OMAiERWIDIY.
OrthoDBiPOG091H01WN.
PhylomeDBiQ9F315.

Family and domain databases

Gene3Di3.90.226.10. 1 hit.
HAMAPiMF_00444. ClpP. 1 hit.
InterProiIPR001907. ClpP.
IPR029045. ClpP/crotonase-like_dom.
IPR023562. ClpP/TepA.
IPR033135. ClpP_His_AS.
[Graphical view]
PANTHERiPTHR10381. PTHR10381. 1 hit.
PfamiPF00574. CLP_protease. 1 hit.
[Graphical view]
PRINTSiPR00127. CLPPROTEASEP.
SUPFAMiSSF52096. SSF52096. 1 hit.
PROSITEiPS00382. CLP_PROTEASE_HIS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9F315-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRRPGAVVRR AGGYVTNLMP SAAGEPSIGG GLGDQVYNRL LGERIIFLGQ
60 70 80 90 100
PVDDDIANKI TAQLLLLASD PDKDIFLYIN SPGGSITAGM AIYDTMQYIK
110 120 130 140 150
NDVVTIAMGL AASMGQFLLS AGTPGKRFAL PNAEILIHQP SAGLAGSASD
160 170 180 190 200
IKIHAERLLH TKRRMAELTS QHTGQTIEQI TRDSDRDRWF DAFEAKEYGL
210
IDDVIATAAG MPGGGGTGA
Length:219
Mass (Da):23,229
Last modified:March 1, 2001 - v1
Checksum:i235A828E5B1E0BDD
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti125 – 127GKR → RQ in AAC70947 (PubMed:10320574).Curated3

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF071885 Genomic DNA. Translation: AAC70947.1.
AL939113 Genomic DNA. Translation: CAC09995.1.
RefSeqiNP_626855.1. NC_003888.3.
WP_003976180.1. NC_003888.3.

Genome annotation databases

EnsemblBacteriaiCAC09995; CAC09995; CAC09995.
GeneIDi1098053.
KEGGisco:SCO2619.
PATRICi23734924. VBIStrCoe124346_2665.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF071885 Genomic DNA. Translation: AAC70947.1.
AL939113 Genomic DNA. Translation: CAC09995.1.
RefSeqiNP_626855.1. NC_003888.3.
WP_003976180.1. NC_003888.3.

3D structure databases

ProteinModelPortaliQ9F315.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi100226.SCO2619.

Protein family/group databases

MEROPSiS14.008.

Proteomic databases

PRIDEiQ9F315.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAC09995; CAC09995; CAC09995.
GeneIDi1098053.
KEGGisco:SCO2619.
PATRICi23734924. VBIStrCoe124346_2665.

Phylogenomic databases

eggNOGiENOG4105CCQ. Bacteria.
COG0740. LUCA.
HOGENOMiHOG000285833.
InParanoidiQ9F315.
KOiK01358.
OMAiERWIDIY.
OrthoDBiPOG091H01WN.
PhylomeDBiQ9F315.

Family and domain databases

Gene3Di3.90.226.10. 1 hit.
HAMAPiMF_00444. ClpP. 1 hit.
InterProiIPR001907. ClpP.
IPR029045. ClpP/crotonase-like_dom.
IPR023562. ClpP/TepA.
IPR033135. ClpP_His_AS.
[Graphical view]
PANTHERiPTHR10381. PTHR10381. 1 hit.
PfamiPF00574. CLP_protease. 1 hit.
[Graphical view]
PRINTSiPR00127. CLPPROTEASEP.
SUPFAMiSSF52096. SSF52096. 1 hit.
PROSITEiPS00382. CLP_PROTEASE_HIS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCLPP1_STRCO
AccessioniPrimary (citable) accession number: Q9F315
Secondary accession number(s): Q9ZH59
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: March 1, 2001
Last modified: October 5, 2016
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.