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 04-NOV-2026, entry version 151. 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; Methanobacteriati; Thermoplasmatota; Thermoplasmata; OC Thermoplasmatales; 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. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U72710; AAC44636.1; -; Genomic_DNA. DR EMBL; AL445065; CAC11959.1; -; Genomic_DNA. DR PIR; T37465; T37465. DR RefSeq; WP_010901242.1; NC_002578.1. 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 AlphaFoldDB; P96084; -. DR MDposit; P96084; -. DR SMR; P96084; -. DR FunCoup; P96084; 42. DR STRING; 273075.gene:9572044; -. DR ESTHER; theac-pip; Proline_iminopeptidase. DR MEROPS; S33.005; -. DR PaxDb; 273075-gene:9572044; -. DR EnsemblBacteria; CAC11959; CAC11959; CAC11959. DR KEGG; tac:Ta0830; -. DR eggNOG; arCOG01648; Archaea. DR HOGENOM; CLU_020336_15_1_2; -. DR InParanoid; P96084; -. DR OMA; AAFWTVD; -. DR OrthoDB; 7466at2157; -. DR EvolutionaryTrace; P96084; -. DR Proteomes; UP000001024; Chromosome. DR GO; GO:0016020; C:membrane; IEA:TreeGrafter. DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-EC. DR GO; GO:0006508; P:proteolysis; IEA:InterPro. DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1. DR InterPro; IPR000073; AB_hydrolase_1. DR InterPro; IPR029058; AB_hydrolase_fold. DR InterPro; IPR050266; AB_hydrolase_sf. DR InterPro; IPR002410; Peptidase_S33. DR InterPro; IPR005945; Pro_imino_pep. DR NCBIfam; TIGR01250; pro_imino_pep_2; 1. DR NCBIfam; NF045948; ProImpepThrmp; 1. DR PANTHER; PTHR43798:SF33; HYDROLASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G14860)-RELATED; 1. DR PANTHER; PTHR43798; MONOACYLGLYCEROL LIPASE; 1. DR Pfam; PF00561; Abhydrolase_1; 1. DR PIRSF; PIRSF005539; Pept_S33_TRI_F1; 1. DR PRINTS; PR00111; ABHYDROLASE. DR PRINTS; PR00793; PROAMNOPTASE. DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 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 205..209 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 //