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P0A526 (CLPP1_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 51. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
ATP-dependent Clp protease proteolytic subunit 1
EC=3.4.21.92
Alternative name(s):
Endopeptidase Clp 1
Gene names
Name:clpP1
Synonyms:clpP
Ordered Locus Names:Rv2461c, MT2536
ORF Names:MTV008.17c
OrganismMycobacterium tuberculosis
Taxonomic identifier1773 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

Protein attributes

Sequence length200 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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 term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological processproteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytosol

Inferred from direct assay. Source: MTBBASE

plasma membrane

Inferred from direct assay. Source: MTBBASE

   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 – 200200ATP-dependent Clp protease proteolytic subunit 1 HAMAP MF_00444
PRO_0000179596

Sites

Active site981 By similarity
Active site1231 By similarity

Secondary structure

1 ............................... 200
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A526 [UniParc].

Last modified March 15, 2005. Version 1.
Checksum: 2FDF6B71DE206953

FASTA20021,708
        10         20         30         40         50         60 
MSQVTDMRSN SQGLSLTDSV YERLLSERII FLGSEVNDEI ANRLCAQILL LAAEDASKDI 

        70         80         90        100        110        120 
SLYINSPGGS ISAGMAIYDT MVLAPCDIAT YAMGMAASMG EFLLAAGTKG KRYALPHARI 

       130        140        150        160        170        180 
LMHQPLGGVT GSAADIAIQA EQFAVIKKEM FRLNAEFTGQ PIERIEADSD RDRWFTAAEA 

       190        200 
LEYGFVDHII TRAHVNGEAQ

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BX842579 Genomic DNA. Translation: CAE55492.1.
AE000516 Genomic DNA. Translation: AAK46836.1.
PIRD70865.
RefSeqNP_337022.1. NC_002755.2.
YP_177883.1. NC_000962.2.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2C8TX-ray3.00A/B/C/D/E/F/G/H/I/J/K/L/M/N2-200[»]
2CBYX-ray2.60A/B/C/D/E/F/G1-200[»]
2CE3X-ray2.60A/B/C/D/E/F/G/H/I/J/K/L/M/N1-200[»]
ProteinModelPortalP0A526.
SMRP0A526. Positions 15-194.
ModBaseSearch...

Protein family/group databases

MEROPSS14.008.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBMYCT00000001586; EBMYCP00000001586; EBMYCG00000001586.
EBMYCT00000071224; EBMYCP00000069283; EBMYCG00000071219.
GeneID888176.
925798.
GenomeReviewsGene locus MT2536 in contig AE000516_GR.
Gene locus Rv2461c in contig AL123456_GR.
KEGGmtc:MT2536.
mtu:Rv2461c.
PATRIC18127330. VBIMycTub22151_2773.
TIGRMT2536.

Organism-specific databases

TubercuListRv2461c.

Phylogenomic databases

GeneTreeEBGT00050000015874.
HOGENOMHBG558421.
OMANAICAQL.
PhylomeDBP0A526.
ProtClustDBPRK00277.

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. 1 hit.
PS00381. CLP_PROTEASE_SER. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCLPP1_MYCTU
AccessionPrimary (citable) accession number: P0A526
Secondary accession number(s): O53188
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: March 15, 2005
Last modified: January 25, 2012
This is version 51 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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