ID   PEPX_STRAW              Reviewed;         676 AA.
AC   Q82MI6;
DT   22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Putative Xaa-Pro dipeptidyl-peptidase;
DE            Short=X-Pro dipeptidyl-peptidase;
DE            EC=3.4.14.11;
DE   AltName: Full=X-prolyl-dipeptidyl aminopeptidase;
DE            Short=X-PDAP;
GN   OrderedLocusNames=SAV_1674;
OS   Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC
OS   14893 / NCIMB 12804 / NRRL 8165 / MA-4680).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=227882;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC   8165 / MA-4680;
RX   PubMed=11572948; DOI=10.1073/pnas.211433198;
RA   Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M.,
RA   Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T.,
RA   Sakaki Y., Hattori M.;
RT   "Genome sequence of an industrial microorganism Streptomyces avermitilis:
RT   deducing the ability of producing secondary metabolites.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC   8165 / MA-4680;
RX   PubMed=12692562; DOI=10.1038/nbt820;
RA   Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T.,
RA   Sakaki Y., Hattori M., Omura S.;
RT   "Complete genome sequence and comparative analysis of the industrial
RT   microorganism Streptomyces avermitilis.";
RL   Nat. Biotechnol. 21:526-531(2003).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolyzes Xaa-Pro-|- bonds to release unblocked, N-terminal
CC         dipeptides from substrates including Ala-Pro-|-p-nitroanilide and
CC         (sequentially) Tyr-Pro-|-Phe-Pro-|-Gly-Pro-|-Ile.; EC=3.4.14.11;
CC   -!- SIMILARITY: Belongs to the peptidase S15 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; BA000030; BAC69385.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q82MI6; -.
DR   SMR; Q82MI6; -.
DR   STRING; 227882.SAV_1674; -.
DR   ESTHER; straw-pepx; Lactobacillus_peptidase.
DR   EnsemblBacteria; BAC69385; BAC69385; SAVERM_1674.
DR   KEGG; sma:SAVERM_1674; -.
DR   eggNOG; COG2936; Bacteria.
DR   HOGENOM; CLU_011800_1_0_11; -.
DR   OMA; LYTASPY; -.
DR   Proteomes; UP000000428; Chromosome.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008239; F:dipeptidyl-peptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; -; 2.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR000383; Xaa-Pro-like_dom.
DR   InterPro; IPR013736; Xaa-Pro_dipept_C.
DR   Pfam; PF02129; Peptidase_S15; 1.
DR   Pfam; PF08530; PepX_C; 1.
DR   SMART; SM00939; PepX_C; 1.
DR   SUPFAM; SSF49785; SSF49785; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase; Hydrolase; Protease; Reference proteome; Serine protease.
FT   CHAIN           1..676
FT                   /note="Putative Xaa-Pro dipeptidyl-peptidase"
FT                   /id="PRO_0000220239"
FT   REGION          423..450
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        423..448
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        224
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        330
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        361
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   676 AA;  72714 MW;  39C455ADA0246412 CRC64;
     MIPPHRCLTD PLLQGSWPGY LPPMPKRARR MRLTTWRSPV TAVIAALLAA FLTPAAAHGA
     PRESAPVYSY ENAIRESVWV DTRLDGDGDG KTDRVAVDVV RPRELARQGR KIPVIMDASP
     YYSCCGRGNE SQKKTYDANG DVVRMPLFYD NYFVPRGYAF VGVDLAGTNR SDGCVDVGGR
     SDIQSAKAVI DWLNGRAHGY TSRTGTARAK ATWTNGRTGM IGKSWDGTVA NGVAATGVKG
     LKTIVPISAI SSWYDYYFAK GAPLYDSGPD WLSDYVDSPD ARTKCAAVQR KLVDEAPRTG
     DWTSLWTERD YVKDASKVRA SVFLVHGMQD LNVRAKNFGQ WWSALAKNGV ERKIWLSQTG
     HVDPFDFRRT AWVDTLHRWF DHELLGYDNG VDREPTADIE RHPDQWVTST LWPPRGTDAV
     TLRPGTGTQA GVGTLGLRTG SGTETFTDDP RLSETDWAAH IDESTASKAG FVTAPLAGDV
     RLSGSSKVTV TATPTTSTAH LSAVLVDLGP DTIRDYADGG EGITTLTDRT CWGASTAGDS
     ACFKNTRATT AAVDYTVLSR GWADLGNHAS ARKGVPLTPG KAYTITLDLA ATDHVVPKGH
     RLALIVAGTD KDLIDPPSST PTLTLDLART SARVPLVGGA AAFTRATAQS GTAADATVLD
     GVREPHTAHR VPGGGL