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Protein

Proline iminopeptidase

Gene

pip

Organism
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

Release of N-terminal proline from a peptide.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei105 – 1051Nucleophile
Active sitei244 – 2441By similarity
Active sitei271 – 2711Proton donor

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Protease

Enzyme and pathway databases

BioCyciRETL1328306-WGS:GSTH-6933-MONOMER.

Protein family/group databases

ESTHERitheac-pip. Proline_iminopeptidase.
MEROPSiS33.005.

Names & Taxonomyi

Protein namesi
Recommended name:
Proline iminopeptidase (EC:3.4.11.5)
Short name:
PIP
Alternative name(s):
Prolyl aminopeptidase
Short name:
PAP
Tricorn protease-interacting factor F1
Gene namesi
Name:pip
Ordered Locus Names:Ta0830
OrganismiThermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Taxonomic identifieri273075 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermoplasmataThermoplasmatalesThermoplasmataceaeThermoplasma
Proteomesi
  • UP000001024 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 293293Proline iminopeptidasePRO_0000080851Add
BLAST

Proteomic databases

PRIDEiP96084.

Interactioni

Subunit structurei

Part of the tricorn proteolytic complex.

Protein-protein interaction databases

STRINGi273075.Ta0830.

Structurei

Secondary structure

1
293
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 127Combined sources
Beta strandi15 – 228Combined sources
Beta strandi28 – 347Combined sources
Turni37 – 393Combined sources
Helixi43 – 5412Combined sources
Beta strandi56 – 616Combined sources
Helixi74 – 763Combined sources
Helixi79 – 9416Combined sources
Beta strandi99 – 1046Combined sources
Helixi106 – 11813Combined sources
Helixi119 – 1213Combined sources
Beta strandi122 – 1298Combined sources
Helixi134 – 14613Combined sources
Helixi150 – 16213Combined sources
Helixi168 – 18114Combined sources
Beta strandi185 – 1873Combined sources
Helixi190 – 20112Combined sources
Helixi204 – 2085Combined sources
Beta strandi211 – 2144Combined sources
Turni219 – 2224Combined sources
Turni226 – 2283Combined sources
Helixi229 – 2313Combined sources
Beta strandi236 – 2416Combined sources
Helixi248 – 25710Combined sources
Beta strandi262 – 2665Combined sources
Helixi273 – 2764Combined sources
Helixi278 – 29013Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP96084.
SMRiP96084. Positions 1-293.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP96084.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S33 family.Curated

Phylogenomic databases

eggNOGiarCOG01648. Archaea.
COG0596. LUCA.
HOGENOMiHOG000026004.
OMAiTWYRVTG.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
IPR022742. Hydrolase_4.
IPR002410. Peptidase_S33.
IPR005945. Pro_imino_pep.
[Graphical view]
PfamiPF12146. Hydrolase_4. 1 hit.
[Graphical view]
PIRSFiPIRSF005539. Pept_S33_TRI_F1. 1 hit.
PRINTSiPR00111. ABHYDROLASE.
PR00793. PROAMNOPTASE.
SUPFAMiSSF53474. SSF53474. 1 hit.
TIGRFAMsiTIGR01250. pro_imino_pep_2. 1 hit.

Sequencei

Sequence statusi: Complete.

P96084-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDQECIENYA KVNGIYIYYK LCKAPEEKAK LMTMHGGPGM SHDYLLSLRD
60 70 80 90 100
MTKEGITVLF YDQFGCGRSE EPDQSKFTID YGVEEAEALR SKLFGNEKVF
110 120 130 140 150
LMGSSYGGAL ALAYAVKYQD HLKGLIVSGG LSSVPLTVKE MNRLIDELPA
160 170 180 190 200
KYRDAIKKYG SSGSYENPEY QEAVNYFYHQ HLLRSEDWPP EVLKSLEYAE
210 220 230 240 250
RRNVYRIMNG PNEFTITGTI KDWDITDKIS AIKIPTLITV GEYDEVTPNV
260 270 280 290
ARVIHEKIAG SELHVFRDCS HLTMWEDREG YNKLLSDFIL KHL
Length:293
Mass (Da):33,487
Last modified:May 1, 1997 - v1
Checksum:i4FD91EE29668FB65
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U72710 Genomic DNA. Translation: AAC44636.1.
AL445065 Genomic DNA. Translation: CAC11959.1.
PIRiT37465.

Genome annotation databases

EnsemblBacteriaiCAC11959; CAC11959; CAC11959.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U72710 Genomic DNA. Translation: AAC44636.1.
AL445065 Genomic DNA. Translation: CAC11959.1.
PIRiT37465.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP96084.
SMRiP96084. Positions 1-293.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi273075.Ta0830.

Protein family/group databases

ESTHERitheac-pip. Proline_iminopeptidase.
MEROPSiS33.005.

Proteomic databases

PRIDEiP96084.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAC11959; CAC11959; CAC11959.

Phylogenomic databases

eggNOGiarCOG01648. Archaea.
COG0596. LUCA.
HOGENOMiHOG000026004.
OMAiTWYRVTG.

Enzyme and pathway databases

BioCyciRETL1328306-WGS:GSTH-6933-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP96084.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
IPR022742. Hydrolase_4.
IPR002410. Peptidase_S33.
IPR005945. Pro_imino_pep.
[Graphical view]
PfamiPF12146. Hydrolase_4. 1 hit.
[Graphical view]
PIRSFiPIRSF005539. Pept_S33_TRI_F1. 1 hit.
PRINTSiPR00111. ABHYDROLASE.
PR00793. PROAMNOPTASE.
SUPFAMiSSF53474. SSF53474. 1 hit.
TIGRFAMsiTIGR01250. pro_imino_pep_2. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).

Entry informationi

Entry nameiPIP_THEAC
AccessioniPrimary (citable) accession number: P96084
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 1997
Last modified: May 11, 2016
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.