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Q65E10 (CLPP2_BACLD) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 49. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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

Names and origin

Protein namesRecommended name:
ATP-dependent Clp protease proteolytic subunit 2

EC=3.4.21.92
Alternative name(s):
Endopeptidase Clp 2
Gene names
Name:clpP2
Ordered Locus Names:BLi03890, BL05355
OrganismBacillus licheniformis (strain DSM 13 / ATCC 14580) [Complete proteome] [HAMAP]
Taxonomic identifier279010 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillus

Protein attributes

Sequence length190 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 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 termComplete 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 – 190190ATP-dependent Clp protease proteolytic subunit 2 HAMAP MF_00444
PRO_0000179498

Sites

Active site981 By similarity
Active site1231 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q65E10 [UniParc].

Last modified October 25, 2004. Version 1.
Checksum: D5325BCB7C954FFC

FASTA19021,049
        10         20         30         40         50         60 
MNTIPYVIEK TAAGERSYDI FSRLLKDRII MIGSEFNDDL ANRVTAQLLF LSAEDNEKDI 

        70         80         90        100        110        120 
SIYINSPGGS TSAGYAILDT MDYVKPDVRT ICVGMAASMG AILLAGGAKG KRYALKNSEI 

       130        140        150        160        170        180 
MIHQPLGGVK GQATDMEISA KRIIKLREKI ERFFHERTGQ PIEKLKADME RDYFMDADEA 

       190 
KAYGVIDAVL 

« Hide

References

[1]"The complete genome sequence of Bacillus licheniformis DSM13, an organism with great industrial potential."
Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P., Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.
J. Mol. Microbiol. Biotechnol. 7:204-211(2004) [PubMed: 15383718] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 13 / ATCC 14580.
[2]"Complete genome sequence of the industrial bacterium Bacillus licheniformis and comparisons with closely related Bacillus species."
Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J., Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B., Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A., Bolotin A., Lapidus A. expand/collapse author list , Galleron N., Ehrlich S.D., Berka R.M.
Genome Biol. 5:R77.1-R77.12(2004) [PubMed: 15461803] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 13 / ATCC 14580.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017333 Genomic DNA. Translation: AAU42704.1.
CP000002 Genomic DNA. Translation: AAU25330.1.
RefSeqYP_080968.1. NC_006270.3.
YP_093397.1. NC_006322.1.

3D structure databases

ProteinModelPortalQ65E10.
SMRQ65E10. Positions 12-190.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ65E10.

Protein family/group databases

MEROPSS14.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000057777; EBBACP00000056308; EBBACG00000057768.
EBBACT00000058715; EBBACP00000057148; EBBACG00000058706.
GeneID3028091.
3101125.
GenomeReviewsGene locus BLi03890 in contig AE017333_GR.
Gene locus BL05355 in contig CP000002_GR.
KEGGbld:BLi03890.
bli:BL05355.
NMPDRfig|279010.5.peg.4133.
PATRIC18953574. VBIBacLic203714_3962.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0740.
GeneTreeEBGT00050000002046.
HOGENOMHBG558421.
OMAKHDINKI.
PhylomeDBQ65E10.
ProtClustDBCLSK737604.

Enzyme and pathway databases

BioCycBLIC279010-1:BLI03890-MONOMER.
BLIC279010:BL05355-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. False negative.
PS00381. CLP_PROTEASE_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCLPP2_BACLD
AccessionPrimary (citable) accession number: Q65E10
Secondary accession number(s): Q62PI1
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: October 25, 2004
Last modified: January 25, 2012
This is version 49 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

SIMILARITY comments

Index of protein domains and families