ID   PEPX_BACCR              Reviewed;         580 AA.
AC   Q81CB2;
DT   22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 101.
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=BC_2861;
OS   Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS   15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=226900;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373
RC   / NCTC 2599 / NRRL B-3711;
RX   PubMed=12721630; DOI=10.1038/nature01582;
RA   Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA   Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA   Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA   Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.;
RT   "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT   anthracis.";
RL   Nature 423:87-91(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}.
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DR   EMBL; AE016877; AAP09811.1; -; Genomic_DNA.
DR   RefSeq; NP_832610.1; NC_004722.1.
DR   RefSeq; WP_000038298.1; NC_004722.1.
DR   AlphaFoldDB; Q81CB2; -.
DR   SMR; Q81CB2; -.
DR   STRING; 226900.BC_2861; -.
DR   ESTHER; baccr-pepx; Lactobacillus_peptidase.
DR   MEROPS; S13.003; -.
DR   EnsemblBacteria; AAP09811; AAP09811; BC_2861.
DR   KEGG; bce:BC2861; -.
DR   PATRIC; fig|226900.8.peg.2923; -.
DR   HOGENOM; CLU_011800_1_0_9; -.
DR   OMA; WDKIKNW; -.
DR   Proteomes; UP000001417; 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; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR008252; Pept_S15_Xpro.
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   PRINTS; PR00923; LACTOPTASE.
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..580
FT                   /note="Putative Xaa-Pro dipeptidyl-peptidase"
FT                   /id="PRO_0000220237"
FT   ACT_SITE        207
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        319
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        350
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   580 AA;  64540 MW;  49B977988258A2EA CRC64;
     MSKKKMAITL SAMLSATIIP SFTMDVHAEK KEETKNTKIE LENGMTKPIY SLDEAIMDEN
     LYVETEVDSD QDGKKDRVSI KVMRPKTDPN VKVPVIYEMS PYRSGLKDVP VYNVDEELYA
     YEGKPYGAIN LGSYGNYYVP RGYAVILGES IGTGKSDGCP TTGDEQEILG TKSVIDWVNG
     RAKAFTEQGE EVQANWSTGN VGMTGVSYNG TLPNAVATTG VEGLKTIIPI AAISSWYDYY
     RANGAVIAPG GYQGEDTDNM AEAVLTRENP EVCGQVIKEL TAGQDRKTGN YNDFWDKRNY
     VKDAKNVKAS VFVVHGLNDW NVKTKQFAQW WEALGENNVP RKMWLHQGGH GGTSSNNWQQ
     TQNKWLDYWL YGIENGIMDE PMVDVQRENK TWQKIKNWPD PAAVPSKIRM YLSNKSVNLP
     LSMGSANKVF SFLDDAQIKS NQLVANPELE VANRLVYTMP VLQKDTRISG TPKISITGNI
     DRSVSNLTAL LVDYGGAKPE IVTRGWMDPQ NVKSIENSTA IQPGKDYTFT WDMQPDDYVF
     KAGHQIGVVL IASDYDYTIR PKAGTKLTVK LSEVTLPIVK