PIP_THEAC
ID PIP_THEAC Reviewed; 293 AA.
AC P96084;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Proline iminopeptidase;
DE Short=PIP;
DE EC=3.4.11.5;
DE AltName: Full=Prolyl aminopeptidase;
DE Short=PAP;
DE AltName: Full=Tricorn protease-interacting factor F1;
GN Name=pip; OrderedLocusNames=Ta0830;
OS Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS 15155 / AMRC-C165).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273075;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=8946961; DOI=10.1016/s0014-5793(96)01163-5;
RA Tamura T., Tamura N., Lottspeich F., Baumeister W.;
RT "Tricorn protease (TRI) interacting factor 1 from Thermoplasma acidophilum
RT is a proline iminopeptidase.";
RL FEBS Lett. 398:101-105(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=11029001; DOI=10.1038/35035069;
RA Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT acidophilum.";
RL Nature 407:508-513(2000).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX PubMed=12374735; DOI=10.1093/emboj/cdf552;
RA Goettig P., Groll M., Kim J.S., Huber R., Brandstetter H.;
RT "Structures of the tricorn-interacting aminopeptidase F1 with different
RT ligands explain its catalytic mechanism.";
RL EMBO J. 21:5343-5352(2002).
CC -!- FUNCTION: Cleaves H-Pro-AMC as well as a wide spectrum of amino acid
CC substrates and several peptide substrates without a proline at the N-
CC terminus. Proteases F1, F2 and F3 degrade oligopeptides produced by
CC Tricorn (themselves probably produced by the proteasome) yielding free
CC amino acids.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of N-terminal proline from a peptide.; EC=3.4.11.5;
CC -!- SUBUNIT: Part of the tricorn proteolytic complex.
CC -!- SIMILARITY: Belongs to the peptidase S33 family. {ECO:0000305}.
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DR EMBL; U72710; AAC44636.1; -; Genomic_DNA.
DR EMBL; AL445065; CAC11959.1; -; Genomic_DNA.
DR PIR; T37465; T37465.
DR PDB; 1MT3; X-ray; 2.00 A; A=1-293.
DR PDB; 1MTZ; X-ray; 1.80 A; A=1-293.
DR PDB; 1MU0; X-ray; 2.40 A; A=1-293.
DR PDB; 1XQV; X-ray; 2.30 A; A=1-293.
DR PDB; 1XQW; X-ray; 2.00 A; A=1-293.
DR PDB; 1XQX; X-ray; 2.10 A; A=1-293.
DR PDB; 1XQY; X-ray; 3.20 A; A=1-293.
DR PDB; 1XRL; X-ray; 1.82 A; A=1-293.
DR PDB; 1XRM; X-ray; 2.70 A; A=1-293.
DR PDB; 1XRN; X-ray; 2.80 A; A=1-293.
DR PDB; 1XRO; X-ray; 1.80 A; A=1-293.
DR PDB; 1XRP; X-ray; 2.30 A; A=1-293.
DR PDB; 1XRQ; X-ray; 2.80 A; A=1-293.
DR PDB; 1XRR; X-ray; 2.40 A; A=1-293.
DR PDBsum; 1MT3; -.
DR PDBsum; 1MTZ; -.
DR PDBsum; 1MU0; -.
DR PDBsum; 1XQV; -.
DR PDBsum; 1XQW; -.
DR PDBsum; 1XQX; -.
DR PDBsum; 1XQY; -.
DR PDBsum; 1XRL; -.
DR PDBsum; 1XRM; -.
DR PDBsum; 1XRN; -.
DR PDBsum; 1XRO; -.
DR PDBsum; 1XRP; -.
DR PDBsum; 1XRQ; -.
DR PDBsum; 1XRR; -.
DR AlphaFoldDB; P96084; -.
DR SMR; P96084; -.
DR STRING; 273075.Ta0830; -.
DR ESTHER; theac-pip; Proline_iminopeptidase.
DR MEROPS; S33.005; -.
DR EnsemblBacteria; CAC11959; CAC11959; CAC11959.
DR KEGG; tac:Ta0830; -.
DR eggNOG; arCOG01648; Archaea.
DR HOGENOM; CLU_020336_15_1_2; -.
DR OMA; TWYRVTG; -.
DR EvolutionaryTrace; P96084; -.
DR Proteomes; UP000001024; Chromosome.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR022742; Hydrolase_4.
DR InterPro; IPR002410; Peptidase_S33.
DR InterPro; IPR005945; Pro_imino_pep.
DR Pfam; PF12146; Hydrolase_4; 1.
DR PIRSF; PIRSF005539; Pept_S33_TRI_F1; 1.
DR PRINTS; PR00111; ABHYDROLASE.
DR PRINTS; PR00793; PROAMNOPTASE.
DR SUPFAM; SSF53474; SSF53474; 1.
DR TIGRFAMs; TIGR01250; pro_imino_pep_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminopeptidase; Hydrolase; Protease; Reference proteome.
FT CHAIN 1..293
FT /note="Proline iminopeptidase"
FT /id="PRO_0000080851"
FT ACT_SITE 105
FT /note="Nucleophile"
FT ACT_SITE 244
FT /evidence="ECO:0000250"
FT ACT_SITE 271
FT /note="Proton donor"
FT STRAND 6..12
FT /evidence="ECO:0007829|PDB:1MTZ"
FT STRAND 15..22
FT /evidence="ECO:0007829|PDB:1MTZ"
FT STRAND 28..34
FT /evidence="ECO:0007829|PDB:1MTZ"
FT TURN 37..39
FT /evidence="ECO:0007829|PDB:1MTZ"
FT HELIX 43..54
FT /evidence="ECO:0007829|PDB:1MTZ"
FT STRAND 56..61
FT /evidence="ECO:0007829|PDB:1MTZ"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:1MTZ"
FT HELIX 79..94
FT /evidence="ECO:0007829|PDB:1MTZ"
FT STRAND 99..104
FT /evidence="ECO:0007829|PDB:1MTZ"
FT HELIX 106..118
FT /evidence="ECO:0007829|PDB:1MTZ"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:1MTZ"
FT STRAND 122..129
FT /evidence="ECO:0007829|PDB:1MTZ"
FT HELIX 134..146
FT /evidence="ECO:0007829|PDB:1MTZ"
FT HELIX 150..162
FT /evidence="ECO:0007829|PDB:1MTZ"
FT HELIX 168..181
FT /evidence="ECO:0007829|PDB:1MTZ"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:1XRP"
FT HELIX 190..201
FT /evidence="ECO:0007829|PDB:1MTZ"
FT HELIX 204..208
FT /evidence="ECO:0007829|PDB:1MTZ"
FT STRAND 211..214
FT /evidence="ECO:0007829|PDB:1XRQ"
FT TURN 219..222
FT /evidence="ECO:0007829|PDB:1MTZ"
FT TURN 226..228
FT /evidence="ECO:0007829|PDB:1MTZ"
FT HELIX 229..231
FT /evidence="ECO:0007829|PDB:1MTZ"
FT STRAND 236..241
FT /evidence="ECO:0007829|PDB:1MTZ"
FT HELIX 248..257
FT /evidence="ECO:0007829|PDB:1MTZ"
FT STRAND 262..266
FT /evidence="ECO:0007829|PDB:1MTZ"
FT HELIX 273..276
FT /evidence="ECO:0007829|PDB:1MTZ"
FT HELIX 278..290
FT /evidence="ECO:0007829|PDB:1MTZ"
SQ SEQUENCE 293 AA; 33487 MW; 4FD91EE29668FB65 CRC64;
MDQECIENYA KVNGIYIYYK LCKAPEEKAK LMTMHGGPGM SHDYLLSLRD MTKEGITVLF
YDQFGCGRSE EPDQSKFTID YGVEEAEALR SKLFGNEKVF LMGSSYGGAL ALAYAVKYQD
HLKGLIVSGG LSSVPLTVKE MNRLIDELPA KYRDAIKKYG SSGSYENPEY QEAVNYFYHQ
HLLRSEDWPP EVLKSLEYAE RRNVYRIMNG PNEFTITGTI KDWDITDKIS AIKIPTLITV
GEYDEVTPNV ARVIHEKIAG SELHVFRDCS HLTMWEDREG YNKLLSDFIL KHL
