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Reviewed, UniProtKB/Swiss-Prot Q81X63 (CLPP2_BACAN)

Last modified November 3, 2009. Version 42. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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: BA_5380, GBAA_5380, BAS5000
OrganismBacillus anthracis [Complete proteome] [HAMAP]
Taxonomic identifier1392 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length193 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

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.

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: 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: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 193193ATP-dependent Clp protease proteolytic subunit 2 HAMAP MF_00444
PRO_0000179485

Sites

Active site981 By similarity
Active site1231 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q81X63-1 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: AB177E38F7AB3D20

FASTA19321,392
        10         20         30         40         50         60 
MNLIPTVIEQ TNRGERAYDI YSRLLKDRII MLGSAIDDNV ANSIVSQLLF LESQDPEKDI 

        70         80         90        100        110        120 
HIYINSPGGS ITAGMAIYDT MQFIKPQVST ICIGMAASMG AFLLAAGEKG KRYALPNSEA 

       130        140        150        160        170        180 
MIHQPLGGAQ GQATEIEIAA KRILFLREKL NQILADRTGQ PLEVLQRDTD RDNFMTAEKA 

       190 
LEYGLIDKIF TNR 

« Hide

References

[1]"The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria."
Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., Kolonay J.F., Beanan M.J., Dodson R.J. expand/collapse author list , Brinkac L.M., Gwinn M.L., DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C., Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y., Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M., Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E., White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M., Hanna P.C., Kolstoe A.-B., Fraser C.M.
Nature 423:81-86(2003) [PubMed: 12721629] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ames / isolate Porton.
[2]"Bacillus anthracis comparative genomics."
Ravel J., Rasko D.A., Shumway M.F., Jiang L., Cer R.Z., Federova N.B., Wilson M., Stanley S., Decker S., Read T.D., Salzberg S.L., Fraser C.M.
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ames ancestor.
[3]"Complete genome sequence of Bacillus anthracis Sterne."
Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., Richardson P., Rubin E., Tice H.
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Sterne.

Cross-references

Sequence databases

AE016879 Genomic DNA. Translation: AAP29039.1.
AE017334 Genomic DNA. Translation: AAT34514.1.
AE017225 Genomic DNA. Translation: AAT57289.1.
RefSeqNP_847553.1.
YP_022039.1.
YP_031239.1.

3D structure databases

HSSPHSSP built from PDB template 1TYF based on UniProtKB P19245.
ModBaseSearch...

Protein family/group databases

MEROPSS14.001.

Genome annotation databases

GeneID1084924.
2818633.
2848145.
GenomeReviewsGene locus BA_5380 in contig AE016879_GR.
Gene locus BAS5000 in contig AE017225_GR.
Gene locus GBAA_5380 in contig AE017334_GR.
KEGGban:BA5380.
bar:GBAA5380.
bat:BAS5000.
TIGRBA_5380.
GBAA_5380.

Phylogenomic databases

HOGENOMQ81X63.
OMAVEQTAKG.

Enzyme and pathway databases

BioCycBANT260799:BAS5000-MON.
BANT261594:GBAA5380-MON.
BRENDA3.4.21.92. 267517.

Family and domain databases

HAMAPMF_00444.
[Tree]
InterProIPR001907. Pept_S14_ClpP.
IPR018215. Pept_S14_ClpP_AS.
[Graphical view]
PANTHERPTHR10381. Pept_S14_ClpP. 1 hit.
PfamPF00574. CLP_protease. 1 hit.
[Graphical view]
PRINTSPR00127. CLPPROTEASEP.
TIGRFAMsTIGR00493. clpP. 1 hit.
PROSITEPS00382. CLP_PROTEASE_HIS. False negative.
PS00381. CLP_PROTEASE_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCLPP2_BACAN
AccessionPrimary (citable) accession number: Q81X63
Secondary accession number(s): Q6HQZ9, Q6KKB8
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 1, 2003
Last modified: November 3, 2009
This is version 42 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents