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P96084 (PIP_THEAC) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Proline iminopeptidase

Short name=PIP
EC=3.4.11.5
Alternative name(s):
Prolyl aminopeptidase
Short name=PAP
Tricorn protease-interacting factor F1
Gene names
Name:pip
Ordered Locus Names:Ta0830
OrganismThermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Taxonomic identifier273075 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermoplasmataThermoplasmatalesThermoplasmataceaeThermoplasma

Protein attributes

Sequence length293 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Cleaves H-Pro-AMC as well as a wide spectrum of amino acid substrates and several peptide substrates without a proline at the N-terminus. Proteases F1, F2 and F3 degrade oligopeptides produced by Tricorn (themselves probably produced by the proteasome) yielding free amino acids.

Catalytic activity

Release of N-terminal proline from a peptide.

Subunit structure

Part of the tricorn proteolytic complex.

Sequence similarities

Belongs to the peptidase S33 family.

Ontologies

Keywords
   Molecular functionAminopeptidase
Hydrolase
Protease
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological processproteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: InterPro

   Molecular functionaminopeptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 293293Proline iminopeptidase
PRO_0000080851

Sites

Active site1051Nucleophile
Active site2441 By similarity
Active site2711Proton donor

Secondary structure

................................................... 293
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P96084 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: 4FD91EE29668FB65

FASTA29333,487
        10         20         30         40         50         60 
MDQECIENYA KVNGIYIYYK LCKAPEEKAK LMTMHGGPGM SHDYLLSLRD MTKEGITVLF 

        70         80         90        100        110        120 
YDQFGCGRSE EPDQSKFTID YGVEEAEALR SKLFGNEKVF LMGSSYGGAL ALAYAVKYQD 

       130        140        150        160        170        180 
HLKGLIVSGG LSSVPLTVKE MNRLIDELPA KYRDAIKKYG SSGSYENPEY QEAVNYFYHQ 

       190        200        210        220        230        240 
HLLRSEDWPP EVLKSLEYAE RRNVYRIMNG PNEFTITGTI KDWDITDKIS AIKIPTLITV 

       250        260        270        280        290 
GEYDEVTPNV ARVIHEKIAG SELHVFRDCS HLTMWEDREG YNKLLSDFIL KHL 

« Hide

References

« Hide 'large scale' references
[1]"Tricorn protease (TRI) interacting factor 1 from Thermoplasma acidophilum is a proline iminopeptidase."
Tamura T., Tamura N., Lottspeich F., Baumeister W.
FEBS Lett. 398:101-105(1996) [PubMed: 8946961] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
Strain: ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165.
[2]"The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum."
Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C., Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.
Nature 407:508-513(2000) [PubMed: 11029001] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165.
[3]"Structures of the tricorn-interacting aminopeptidase F1 with different ligands explain its catalytic mechanism."
Goettig P., Groll M., Kim J.S., Huber R., Brandstetter H.
EMBO J. 21:5343-5352(2002) [PubMed: 12374735] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U72710 Genomic DNA. Translation: AAC44636.1.
AL445065 Genomic DNA. Translation: CAC11959.1.
PIRT37465.
RefSeqNP_394291.1. NC_002578.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1MT3X-ray2.00A1-293[»]
1MTZX-ray1.80A1-293[»]
1MU0X-ray2.40A1-293[»]
1XQVX-ray2.30A1-293[»]
1XQWX-ray2.00A1-293[»]
1XQXX-ray2.10A1-293[»]
1XQYX-ray3.20A1-293[»]
1XRLX-ray1.82A1-293[»]
1XRMX-ray2.70A1-293[»]
1XRNX-ray2.80A1-293[»]
1XROX-ray1.80A1-293[»]
1XRPX-ray2.30A1-293[»]
1XRQX-ray2.80A1-293[»]
1XRRX-ray2.40A1-293[»]
ProteinModelPortalP96084.
SMRP96084. Positions 1-293.
ModBaseSearch...

Protein family/group databases

MEROPSS33.005.

Proteomic databases

PRIDEP96084.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1456375.
GenomeReviewsGene locus Ta0830 in contig AL139299_GR.
KEGGtac:Ta0830.
NMPDRfig|273075.1.peg.813.

Phylogenomic databases

HOGENOMHBG515521.
OMAPTEFHVI.
ProtClustDBCLSK374918.

Enzyme and pathway databases

BioCycTACI273075:TA0830-MONOMER.

Family and domain databases

InterProIPR000073. AB_hydrolase_1.
IPR005945. Pept_S33_TRI_F1.
IPR002410. Peptidase_S33.
[Graphical view]
KOK01259.
PIRSFPIRSF005539. Pept_S33_TRI_F1. 1 hit.
PRINTSPR00111. ABHYDROLASE.
PR00793. PROAMNOPTASE.
TIGRFAMsTIGR01250. Pro_imino_pep_2. 1 hit.
ProtoNetSearch...

Entry information

Entry namePIP_THEAC
AccessionPrimary (citable) accession number: P96084
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 1997
Last modified: November 16, 2011
This is version 90 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