PIP_SACS2
ID PIP_SACS2 Reviewed; 310 AA.
AC Q97UA2;
DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 99.
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=SSO3115;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
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; AE006641; AAK43219.1; -; Genomic_DNA.
DR PIR; D90495; D90495.
DR AlphaFoldDB; Q97UA2; -.
DR SMR; Q97UA2; -.
DR STRING; 273057.SSO3115; -.
DR ESTHER; sulso-pip; Proline_iminopeptidase.
DR MEROPS; S33.005; -.
DR EnsemblBacteria; AAK43219; AAK43219; SSO3115.
DR KEGG; sso:SSO3115; -.
DR PATRIC; fig|273057.12.peg.3224; -.
DR eggNOG; arCOG01648; Archaea.
DR HOGENOM; CLU_020336_15_1_2; -.
DR InParanoid; Q97UA2; -.
DR OMA; TWYRVTG; -.
DR PhylomeDB; Q97UA2; -.
DR Proteomes; UP000001974; 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; PR00793; PROAMNOPTASE.
DR SUPFAM; SSF53474; SSF53474; 1.
DR TIGRFAMs; TIGR01250; pro_imino_pep_2; 1.
PE 3: Inferred from homology;
KW Aminopeptidase; Hydrolase; Protease; Reference proteome.
FT CHAIN 1..310
FT /note="Proline iminopeptidase"
FT /id="PRO_0000080850"
FT DOMAIN 41..288
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT ACT_SITE 116
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 255
FT /evidence="ECO:0000250"
FT ACT_SITE 282
FT /note="Proton donor"
FT /evidence="ECO:0000250"
SQ SEQUENCE 310 AA; 35961 MW; B50DE89D0A323EC3 CRC64;
MSYYFITMKG YSINVEEGYK RIFGINIYYK LYRVKGSNRN LVTLHGGPGG SHDYLIPLAD
LSNYGINVLF YDQFGCGRSD DPKDTSDYTI DHGLEELEEL RKQVFGNDKI VLLGHSYGGA
LAIAYALKYQ QFLRGLIVSS GLSSVPYTVK EMRRLIEELP DKYKTIIKRY ESLGDFKNPE
YLDAVNFFYS QHLLRLKEMP EPVKRTFEYI GKRRTYEIMN GPNEFTIIGT IKDWDVTEQL
YKITVPTLIT VGKYDEVTVN VAQLIHKNIK GSRLVIFENS SHMAMWEEKD KYLEVIKEFI
DQVYSLNMVK