ID   PEPX_STRMC              Reviewed;         763 AA.
AC   Q8L376;
DT   22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Xaa-Pro dipeptidyl-peptidase {ECO:0000255|HAMAP-Rule:MF_00698};
DE            EC=3.4.14.11 {ECO:0000255|HAMAP-Rule:MF_00698};
DE   AltName: Full=X-Pro dipeptidyl-peptidase {ECO:0000255|HAMAP-Rule:MF_00698};
DE   AltName: Full=X-prolyl-dipeptidyl aminopeptidase {ECO:0000255|HAMAP-Rule:MF_00698};
DE            Short=X-PDAP {ECO:0000255|HAMAP-Rule:MF_00698};
GN   Name=pepX {ECO:0000255|HAMAP-Rule:MF_00698};
OS   Streptococcus macedonicus.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=59310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ACA-DC 191;
RA   Georgalaki M.D., Papadelli M., Anastasiou R., Kalantzopoulos G.,
RA   Tsakalidou E.;
RT   "Streptococcus macedonicus pepX gene encoding X-prolyl-dipeptidyl-
RT   aminopeptidase.";
RL   Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Removes N-terminal dipeptides sequentially from polypeptides
CC       having unsubstituted N-termini provided that the penultimate residue is
CC       proline. {ECO:0000255|HAMAP-Rule:MF_00698}.
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         Evidence={ECO:0000255|HAMAP-Rule:MF_00698};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00698}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00698}.
CC   -!- SIMILARITY: Belongs to the peptidase S15 family. {ECO:0000255|HAMAP-
CC       Rule:MF_00698}.
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DR   EMBL; AF373012; AAM21314.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8L376; -.
DR   SMR; Q8L376; -.
DR   ESTHER; strma-PEPX; Lactobacillus_peptidase.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008239; F:dipeptidyl-peptidase activity; IEA:UniProtKB-UniRule.
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; -; 1.
DR   HAMAP; MF_00698; Aminopeptidase_S15; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR008252; Pept_S15_Xpro.
DR   InterPro; IPR015251; PepX_N_dom.
DR   InterPro; IPR036313; PepX_N_dom_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   Pfam; PF09168; PepX_N; 1.
DR   PRINTS; PR00923; LACTOPTASE.
DR   SMART; SM00939; PepX_C; 1.
DR   SMART; SM00940; PepX_N; 1.
DR   SUPFAM; SSF49785; SSF49785; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   SUPFAM; SSF81761; SSF81761; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase; Cytoplasm; Hydrolase; Protease; Serine protease.
FT   CHAIN           1..763
FT                   /note="Xaa-Pro dipeptidyl-peptidase"
FT                   /id="PRO_0000220227"
FT   ACT_SITE        349
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00698"
FT   ACT_SITE        469
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00698"
FT   ACT_SITE        499
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00698"
SQ   SEQUENCE   763 AA;  86866 MW;  51B7C3BBB75DAD1D CRC64;
     MKYNQFSFIP RPIAIAEQEL QALGFDITHQ QADKKALENF CRKIFFNYKD TDYPLHQLIA
     DFETDLLTFF NSERPLTADI FYTISLQLLG FIPHVDFTNT TDFLEKIAFP INYQKGHILE
     ALYHLLVSRQ KSGMTLLDDL ISKGLIPVDN NYHFFNGKSL ATFDTTDLIR EVVYVQSPLD
     TDQDGQLDLI KVNIIRPKTS HQLPTMMTAS PYHQGTNVVA NDKKLYKMEG DLAVKPARTI
     NVETRDFEPL AAPDVDLPIG ESEERFNFID PYTLNDYFLA RGFANIYVSG VGTAGSDGFM
     TSGDYAQVES FKAVIDWLNG KSIAFSSHRR DQKVVADWAS GLVCTTGKSY LGTMSTALAT
     TGVEGLKVII AESAISSWYD YYRENGLVCS PGGYPGEDLD VLTELTYSRN LLPGDYLRNN
     AHYQEFLDEQ SAQLDRASGD YNQFWHDRNY LPHADKVKAT CVFTHGLQDW NVKPRHIFNI
     FNALPDTVEK HAFLHHGEHV YMHNWQSIDF RESMNTLLSE KMLGQDNHFV LPTLIWQDNS
     QEQAWTSLAE FGSSNQATLA LGTDQKIIDN HYAKAEFERY SKNFRTFKSE LFTGKANAIC
     LDLPIKNDYH INGQITLHLT VKSSENKGIL SAQVLDYGEK KRFKDVPSVL DLYAIDNGCN
     FSREALKELP FTKAKERVIT KGVLNLQNRT DLLTIEDIPA NEWMTFDFTL QPSIYKLEKG
     DTLRVLLYTT DFEHTIRDNS NYILTVDLDK SNLEIPIENN VGL