ID   PEPX_STRMU              Reviewed;         758 AA.
AC   Q8DVS2;
DT   22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 113.
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=SMU_395;
OS   Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=210007;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700610 / UA159;
RX   PubMed=12397186; DOI=10.1073/pnas.172501299;
RA   Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA   Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA   Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT   "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT   pathogen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
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; AE014133; AAN58151.1; -; Genomic_DNA.
DR   RefSeq; NP_720845.1; NC_004350.2.
DR   RefSeq; WP_002262624.1; NC_004350.2.
DR   AlphaFoldDB; Q8DVS2; -.
DR   SMR; Q8DVS2; -.
DR   STRING; 210007.SMU_395; -.
DR   ESTHER; strmu-pepx; Lactobacillus_peptidase.
DR   PRIDE; Q8DVS2; -.
DR   EnsemblBacteria; AAN58151; AAN58151; SMU_395.
DR   KEGG; smu:SMU_395; -.
DR   PATRIC; fig|210007.7.peg.347; -.
DR   eggNOG; COG2936; Bacteria.
DR   HOGENOM; CLU_011800_0_0_9; -.
DR   OMA; LYTASPY; -.
DR   PhylomeDB; Q8DVS2; -.
DR   BRENDA; 3.4.14.11; 5941.
DR   Proteomes; UP000002512; 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..758
FT                   /note="Xaa-Pro dipeptidyl-peptidase"
FT                   /id="PRO_0000220228"
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   758 AA;  86741 MW;  7DBF08C326C042AF CRC64;
     MKYNQYSYIG TSVSQAEKEL KELGFQISSQ KTNKANLATF VSQVYFHNPD KDDVFKSIIA
     DSQTDLATFL HSDRELTEEI FYTIALQLLE FTPYIDFDEA KTFIKHSHFP IIFQPKHFLL
     NFYQLLGTRT KNGMTLIDKL VSQGFLPADN HYRYFNGKSL ATFDTNALIR EIVYVEAPLD
     TDKDGQLDLI KVNIIRPQTK AKLPVVMTAS PYHQGTNDKG ADKKLHQMEG ELTVKKAATI
     TVTDSHFQAL QVPSSNLPIS PAQESFSYID SYTLNDYFLA RGFANIYVSG VGTKDSDGFM
     TSGDYAQIES FKAVIDWLNG RTTAYTSHKR DKRVMADWTN GLVATTGKSY LGTMSTGLAT
     TGIKELKVII AESAISSWYD YYRENGLVCS PGGYPGEDID VLTELTYSRN LAAGDYLRNN
     AQYQKMLAEQ VKQIDRTSGD YNQFWQDRNY LPHAHKIKAH VVYTHGLQDW NVKPNQVYYI
     FNALPEEIQK HIFLHQGQHV YMHNWQSIDF RESMNALLSE ELLGLQNHFQ LPTIIWQDNS
     QVQTWKKLNN FGSHQTRQFS LGQEKKIIDN HYPSSDFKLY SDDYHAFKHD LFLKKANEIA
     IDLPIQEDML VNGQIKLNLT LKSSSNKGLL SAQVLDYGQK KRFSDLPTIL EHNSIDNGQN
     FSREALRELP FKKAPYRIIT KGVLNLQNRT DLLTIEDIFP NKWMTITFNL QASLYQLQKG
     DSLRIVLYTT DFEQTVRDNS NYILVVDLAK STIEIPIA