ID   PIP_THEVO               Reviewed;         295 AA.
AC   Q97A76;
DT   31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   03-AUG-2022, entry version 107.
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=TV0934; ORFNames=TVG0960913;
OS   Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC
OS   15438 / GSS1).
OC   Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC   Thermoplasmataceae; Thermoplasma.
OX   NCBI_TaxID=273116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1;
RX   PubMed=11121031; DOI=10.1073/pnas.97.26.14257;
RA   Kawashima T., Amano N., Koike H., Makino S., Higuchi S., Kawashima-Ohya Y.,
RA   Watanabe K., Yamazaki M., Kanehori K., Kawamoto T., Nunoshiba T.,
RA   Yamamoto Y., Aramaki H., Makino K., Suzuki M.;
RT   "Archaeal adaptation to higher temperatures revealed by genomic sequence of
RT   Thermoplasma volcanium.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:14257-14262(2000).
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. In conjunction with the three factors F1, F2 and F3, Tricorn
CC       degrades oligopeptides in a sequential manner, yielding free amino
CC       acids (By similarity). {ECO:0000250}.
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. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S33 family. {ECO:0000305}.
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DR   EMBL; BA000011; BAB60076.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q97A76; -.
DR   SMR; Q97A76; -.
DR   STRING; 273116.14325151; -.
DR   ESTHER; thevo-pip; Proline_iminopeptidase.
DR   EnsemblBacteria; BAB60076; BAB60076; BAB60076.
DR   KEGG; tvo:TVG0960913; -.
DR   eggNOG; arCOG01648; Archaea.
DR   HOGENOM; CLU_020336_15_1_2; -.
DR   OMA; TWYRVTG; -.
DR   PhylomeDB; Q97A76; -.
DR   Proteomes; UP000001017; 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; IPR002410; Peptidase_S33.
DR   InterPro; IPR005945; Pro_imino_pep.
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; SSF53474; 1.
DR   TIGRFAMs; TIGR01250; pro_imino_pep_2; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase; Hydrolase; Protease.
FT   CHAIN           1..295
FT                   /note="Proline iminopeptidase"
FT                   /id="PRO_0000080852"
FT   DOMAIN          35..279
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        107
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        246
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        273
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   295 AA;  33830 MW;  821B4C15E3EDD860 CRC64;
     MRKLSRCEDG YVKIQGIYIY YKVCKAENEK AKLMTLHGGP GMSHDYLLSL TDLAEKGITV
     LFYDQFGCGR SEEPEKEKFT IDYGVEEAEA VKKNIFGDDK VFLMGSSYGG ALALAYAVKY
     QAHLKGLIIS GGLSSVPLTV KEMQRLIDEL PEKYRNAIRK YGEVGDYQNP EYQEAVNYFY
     HQHLLRSEDW PPEVLKSLEY AEERNVYRTM NGPNEFTITG TIRDWDITDK IGIISVPTLI
     TVGEFDEVTQ NVAEVIHSKI DNSQLIVFKA CSHLTMWEDR DEYNRILLQF IEKNI