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Reviewed, UniProtKB/Swiss-Prot Q98M38 (CLPP1_RHILO)

Last modified January 19, 2010. Version 47. 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 1
    EC=3.4.21.92
Alternative name(s):
    Endopeptidase Clp 1
Gene names
Name: clpP1
Ordered Locus Names: mlr0748
OrganismRhizobium loti (Mesorhizobium loti) [Complete proteome] [HAMAP]
Taxonomic identifier381 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesPhyllobacteriaceaeMesorhizobium

Protein attributes

Sequence length201 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: 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 – 201201ATP-dependent Clp protease proteolytic subunit 1 HAMAP MF_00444
PRO_0000179631

Sites

Active site1021 By similarity
Active site1271 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q98M38-1 [UniParc].

Last modified September 26, 2001. Version 1.
Checksum: 1161C751F84D3AC6

FASTA20122,204
        10         20         30         40         50         60 
MSGLASLVPM VIEQSSRGER AFDIFSRLLR ERIIFINGEI NDDVSALVCA QLLSLESDNP 

        70         80         90        100        110        120 
DKEISLYINS PGGVVTSGFA IYDTMQYVSC PVSTVCMGFA ASMGSFLLMA GTPGRRIALP 

       130        140        150        160        170        180 
NATILLHQPL GGFQGQASDI QRHAERIGKT KQRMAELYAQ HCGRSYEEVE RTLDRDHFMT 

       190        200 
AREAQTWGIV DHVFDTRKKA A 

« Hide

References

[1]"Complete genome structure of the nitrogen-fixing symbiotic bacterium Mesorhizobium loti."
Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S., Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y., Nakayama S. expand/collapse author list , Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M., Tabata S.
DNA Res. 7:331-338(2000) [PubMed: 11214968] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MAFF303099.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000012 Genomic DNA. Translation: BAB48275.1.
RefSeqNP_102489.1.

3D structure databases

SMRQ98M38. Positions 16-197.
ModBaseSearch...

Protein family/group databases

MEROPSS14.001.

Genome annotation databases

GeneID1225152.
GenomeReviewsGene locus mlr0748 in contig BA000012_GR.
KEGGmlo:mlr0748.
NMPDRfig|266835.1.peg.594.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG558421.
OMAFINGEIN.

Enzyme and pathway databases

BRENDA3.4.21.92. 3315.

Family and domain databases

HAMAPMF_00444. ClpP.
[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.
PROSITEPS00382. CLP_PROTEASE_HIS. 1 hit.
PS00381. CLP_PROTEASE_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCLPP1_RHILO
AccessionPrimary (citable) accession number: Q98M38
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: September 26, 2001
Last modified: January 19, 2010
This is version 47 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