ID   PEPX_STRSV              Reviewed;         762 AA.
AC   A3CKT0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 94.
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}; OrderedLocusNames=SSA_0328;
OS   Streptococcus sanguinis (strain SK36).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=388919;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SK36;
RX   PubMed=17277061; DOI=10.1128/jb.01808-06;
RA   Xu P., Alves J.M., Kitten T., Brown A., Chen Z., Ozaki L.S., Manque P.,
RA   Ge X., Serrano M.G., Puiu D., Hendricks S., Wang Y., Chaplin M.D., Akan D.,
RA   Paik S., Peterson D.L., Macrina F.L., Buck G.A.;
RT   "Genome of the opportunistic pathogen Streptococcus sanguinis.";
RL   J. Bacteriol. 189:3166-3175(2007).
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; CP000387; ABN43785.1; -; Genomic_DNA.
DR   RefSeq; WP_011836436.1; NC_009009.1.
DR   RefSeq; YP_001034335.1; NC_009009.1.
DR   AlphaFoldDB; A3CKT0; -.
DR   SMR; A3CKT0; -.
DR   STRING; 388919.SSA_0328; -.
DR   ESTHER; strsv-pepx; Lactobacillus_peptidase.
DR   MEROPS; S15.001; -.
DR   PRIDE; A3CKT0; -.
DR   EnsemblBacteria; ABN43785; ABN43785; SSA_0328.
DR   KEGG; ssa:SSA_0328; -.
DR   PATRIC; fig|388919.9.peg.318; -.
DR   eggNOG; COG2936; Bacteria.
DR   HOGENOM; CLU_011800_0_0_9; -.
DR   OMA; LYTASPY; -.
DR   OrthoDB; 327988at2; -.
DR   Proteomes; UP000002148; Chromosome.
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; Reference proteome;
KW   Serine protease.
FT   CHAIN           1..762
FT                   /note="Xaa-Pro dipeptidyl-peptidase"
FT                   /id="PRO_1000045494"
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   762 AA;  87582 MW;  11D662D13B52F2F3 CRC64;
     MRFNQYSYAK TKRENMLIEL AELGFFYDSN RSDKENLEDF LRTSFFTYKN TDYPLKSWAA
     DSQTDLLSFF QSDRELTASV FYTVAFQLLE FSPFIDFTDV EAFRQETDFP ITFGDLLENL
     YQLLNTRTKN GNLLIDKLVS EGLIPEDNTH HCFNGKSLAT FSSHDAIREV VYVESRVDTD
     QDGRPDLIKV SIIRPRYQGP VPAVMTASPY HQGTNDPASD KALHDMNVDL AKKEPHQITV
     QDPELKLLQL DSPVPAQEVS ETEEKLGHIG TYTLNDYLLP RGFANLYVSG VGTKDSEGLM
     TSGDYQQIEA YKNVIDWLNG RCRAFTDHTR QREIKATWSN GKVATTGISY LGTMSNGLAT
     TGVDGLEVII AEAGISSWYN YYRENGLVTS PGGYPGEDFE SLTELTYSRN LRAGDYLRNN
     DAYQQNLEQQ RKDLDRQTGD YNQFWHDRNY LLHADKVKAE VVFTHGSQDW NVKPLHVYNM
     FRALPPHIKK HLFFHNGAHV YMNNWQSIDF RESINALLSK KLLGCESDFV LPAVIWQDNS
     QAQSWLTLED FGGQEQNLHL QLGQDCQSIQ NQYSEEDYNR FAKNYQSFKT ELFDGKVNQI
     TLDWTLEKDL FLNGATQLNL RLKSSTDKGL ISAQLLDFGL AKRHTPIPTP IEPRVMDNGR
     YYMLDNLVEL PFAETPHRVI TKGFLNLQNR TNLLSVEEVT PDQWLEFSFE LQPTIYKMKK
     GDQLRLVLYT TDFEHTVRDK IDYQLTVDLE QSSLDLPTMT SH