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Q04SJ1 (Q04SJ1_LEPBJ) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 38. Feed History...

Clusters with 100%, 90%, 50% identity | 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 2 HAMAP MF_00444

EC=3.4.21.92 HAMAP MF_00444
Alternative name(s):
Endopeptidase Clp 2 HAMAP MF_00444
Gene names
Name:clpP-2 EMBL ABJ76129.1
Synonyms:clpP2 HAMAP MF_00444
Ordered Locus Names:LBJ_1559
OrganismLeptospira borgpetersenii serovar Hardjo-bovis (strain JB197) [Complete proteome] [HAMAP]
Taxonomic identifier355277 [NCBI]
Taxonomic lineageBacteriaSpirochaetesSpirochaetalesLeptospiraceaeLeptospira

Protein attributes

Sequence length197 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 RuleBase RU000550

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 RuleBase RU000549

Subcellular location

Cytoplasm By similarity HAMAP MF_00444.

Sequence similarities

Belongs to the peptidase S14 family. HAMAP MF_00444 RuleBase RU003567

Ontologies

Keywords
   Cellular componentCytoplasm HAMAP MF_00444
   LigandATP-binding HAMAP MF_00444
Nucleotide-binding
   Molecular functionHydrolase
Protease
Serine protease HAMAP MF_00444 RuleBase RU000549
   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

Sites

Active site971 By similarity HAMAP MF_00444
Active site1221 By similarity HAMAP MF_00444

Sequences

Sequence LengthMass (Da)Tools
Q04SJ1 [UniParc].

Last modified November 14, 2006. Version 1.
Checksum: 8802E9434E6CBEA8

FASTA19721,606
        10         20         30         40         50         60 
MPEIEKITEV FEELTGSKIS KKFLDHRKIF LWGPVTDESS KDLVGKLLYL EMKDPGKPIT 

        70         80         90        100        110        120 
FYINSPGGVV TSGMTVFDTI KMISSPVHTV CMGMAASMGS VLLAAGTKGE RSIWPNGKVM 

       130        140        150        160        170        180 
IHQPSIGGQI VAPATDLKIH AEEILKTKAK LNQILADACG QPVSKIEEDT DRDYYMDAEE 

       190 
AIQYGIVNKL ATKIDFN 

« Hide

References

[1]"Genome reduction in Leptospira borgpetersenii reflects limited transmission potential."
Bulach D.M., Zuerner R.L., Wilson P., Seemann T., McGrath A., Cullen P.A., Davis J., Johnson M., Kuczek E., Alt D.P., Peterson-Burch B., Coppel R.L., Rood J.I., Davies J.K., Adler B.
Proc. Natl. Acad. Sci. U.S.A. 103:14560-14565(2006) [PubMed: 16973745] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000350 Genomic DNA. Translation: ABJ76129.1.
RefSeqYP_800887.1. NC_008510.1.

3D structure databases

ProteinModelPortalQ04SJ1.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ04SJ1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4411490.
GenomeReviewsGene locus LBJ_1559 in contig CP000350_GR.
KEGGlbj:LBJ_1559.
PATRIC22358535. VBILepBor13265_1980.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0740.
HOGENOMHBG558421.
OMAFSEPVTD.
ProtClustDBCLSK574113.

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. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameQ04SJ1_LEPBJ
AccessionPrimary (citable) accession number: Q04SJ1
Entry history
Integrated into UniProtKB/TrEMBL: November 14, 2006
Last sequence update: November 14, 2006
Last modified: December 14, 2011
This is version 38 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)