ID   PEPX_STRR6              Reviewed;         757 AA.
AC   Q8DQ87;
DT   22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2003, sequence version 2.
DT   03-AUG-2022, entry version 115.
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}; Synonyms=pepXP;
GN   OrderedLocusNames=spr0794;
OS   Streptococcus pneumoniae (strain ATCC BAA-255 / R6).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=171101;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-255 / R6;
RX   PubMed=11544234; DOI=10.1128/jb.183.19.5709-5717.2001;
RA   Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S.,
RA   DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C.,
RA   Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E., LeBlanc D.J.,
RA   Lee L.N., Lefkowitz E.J., Lu J., Matsushima P., McAhren S.M., McHenney M.,
RA   McLeaster K., Mundy C.W., Nicas T.I., Norris F.H., O'Gara M., Peery R.B.,
RA   Robertson G.T., Rockey P., Sun P.-M., Winkler M.E., Yang Y.,
RA   Young-Bellido M., Zhao G., Zook C.A., Baltz R.H., Jaskunas S.R.,
RA   Rosteck P.R. Jr., Skatrud P.L., Glass J.I.;
RT   "Genome of the bacterium Streptococcus pneumoniae strain R6.";
RL   J. Bacteriol. 183:5709-5717(2001).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK99598.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE007317; AAK99598.1; ALT_INIT; Genomic_DNA.
DR   PIR; B97971; B97971.
DR   RefSeq; NP_358388.1; NC_003098.1.
DR   RefSeq; WP_001212040.1; NC_003098.1.
DR   AlphaFoldDB; Q8DQ87; -.
DR   SMR; Q8DQ87; -.
DR   STRING; 171101.spr0794; -.
DR   ESTHER; strpn-pepx; Lactobacillus_peptidase.
DR   MEROPS; S15.001; -.
DR   EnsemblBacteria; AAK99598; AAK99598; spr0794.
DR   GeneID; 60232683; -.
DR   KEGG; spr:spr0794; -.
DR   PATRIC; fig|171101.6.peg.881; -.
DR   eggNOG; COG2936; Bacteria.
DR   HOGENOM; CLU_011800_0_0_9; -.
DR   Proteomes; UP000000586; 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..757
FT                   /note="Xaa-Pro dipeptidyl-peptidase"
FT                   /id="PRO_0000220230"
FT   ACT_SITE        348
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00698"
FT   ACT_SITE        468
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00698"
FT   ACT_SITE        498
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00698"
SQ   SEQUENCE   757 AA;  86862 MW;  CFFBE85AD756F142 CRC64;
     MRFNQYSYIN FPKENVLSEL KKCGFDLQNT ANHKDSLETF LRRFFFTYQD TNYPLSILAA
     DKKTDLLTFF QSEDELTADI FYTVAFQLLG FSYLVDFEDS DVFRKETGFP IIYGDLIENL
     YQLLNTRTKK GNTLIDQLVS DGLIPEDNDY HYFNGKSLAT FSNQDVIREV VYVESRVDTD
     QKGLSDLVKV SIIRPRFDGK IPAIMTASPY HQGTNDKASD KALYKMEGEL EVKLPHKIEL
     EKPQLNLVQP QGKAELIAEA EEKLTHINSS YTLNDYFLPR GFANLYVSGV GTKDSTGFMT
     NGDYQQIEAY KNVIDWLNGR CRAFTDHTRQ RQVKADWSNG KVATTGLSYL GTMSNGLATT
     GVDGLEVIIA EAGISSWYNY YRENGLVTSP GGYPGEDFDS LAELTYSRNL LAGDYIRGNE
     AHQADLEKVK AQLDRKTGDY NQFWHDRNYL LNAHKVKAEV VFTHGSQDWN VKPLHVYQMF
     HALPTHINKH LFFHNGAHVY MNNWQSIDFR ESINALLTKK LLGQETDFQL PTVIWQDNTA
     PQTWLSLDNF GGQENCETFS LGQEEQAIQN QYPDKDFERY GKTYQTFNTE LYQGKANQIT
     INLPVTKDLH LNGRAQLNLR IKSSTNKGLL SAQLLEFGQK KYLQPYPAIL SARTIDNGRY
     HMLENLCELP FRPEAQRVVT KGYLNLQNRN DLLLVEDITA DEWMDVQFEL QPTIYKLKEG
     DTLRLVLYTT DFEITIRDNT DYHLTVDLAQ SMLTLPC