ID   PEPQ_SHIF8              Reviewed;         443 AA.
AC   Q0SZ37;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Xaa-Pro dipeptidase {ECO:0000255|HAMAP-Rule:MF_01279};
DE            Short=X-Pro dipeptidase {ECO:0000255|HAMAP-Rule:MF_01279};
DE            EC=3.4.13.9 {ECO:0000255|HAMAP-Rule:MF_01279};
DE   AltName: Full=Imidodipeptidase {ECO:0000255|HAMAP-Rule:MF_01279};
DE   AltName: Full=Proline dipeptidase {ECO:0000255|HAMAP-Rule:MF_01279};
DE            Short=Prolidase {ECO:0000255|HAMAP-Rule:MF_01279};
GN   Name=pepQ {ECO:0000255|HAMAP-Rule:MF_01279}; OrderedLocusNames=SFV_3653;
OS   Shigella flexneri serotype 5b (strain 8401).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=373384;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=8401;
RX   PubMed=16822325; DOI=10.1186/1471-2164-7-173;
RA   Nie H., Yang F., Zhang X., Yang J., Chen L., Wang J., Xiong Z., Peng J.,
RA   Sun L., Dong J., Xue Y., Xu X., Chen S., Yao Z., Shen Y., Jin Q.;
RT   "Complete genome sequence of Shigella flexneri 5b and comparison with
RT   Shigella flexneri 2a.";
RL   BMC Genomics 7:173-173(2006).
CC   -!- FUNCTION: Splits dipeptides with a prolyl residue in the C-terminal
CC       position. {ECO:0000255|HAMAP-Rule:MF_01279}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of Xaa-|-Pro dipeptides. Also acts on aminoacyl-
CC         hydroxyproline analogs. No action on Pro-|-Pro.; EC=3.4.13.9;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01279};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01279};
CC       Note=Binds 2 manganese ions per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01279};
CC   -!- SIMILARITY: Belongs to the peptidase M24B family. Bacterial-type
CC       prolidase subfamily. {ECO:0000255|HAMAP-Rule:MF_01279}.
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DR   EMBL; CP000266; ABF05678.1; -; Genomic_DNA.
DR   RefSeq; WP_000444553.1; NC_008258.1.
DR   AlphaFoldDB; Q0SZ37; -.
DR   SMR; Q0SZ37; -.
DR   MEROPS; M24.003; -.
DR   EnsemblBacteria; ABF05678; ABF05678; SFV_3653.
DR   KEGG; sfv:SFV_3653; -.
DR   HOGENOM; CLU_050675_0_0_6; -.
DR   OMA; DFWHKVA; -.
DR   BioCyc; SFLE373384:SFV_RS20160-MON; -.
DR   Proteomes; UP000000659; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008235; F:metalloexopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016795; F:phosphoric triester hydrolase activity; IEA:InterPro.
DR   GO; GO:0102009; F:proline dipeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.350.10; -; 1.
DR   Gene3D; 3.90.230.10; -; 1.
DR   HAMAP; MF_01279; X_Pro_dipeptid; 1.
DR   InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR   InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR   InterPro; IPR000994; Pept_M24.
DR   InterPro; IPR001131; Peptidase_M24B_aminopep-P_CS.
DR   InterPro; IPR022846; X_Pro_dipept.
DR   Pfam; PF00557; Peptidase_M24; 1.
DR   SUPFAM; SSF55920; SSF55920; 1.
DR   PROSITE; PS00491; PROLINE_PEPTIDASE; 1.
PE   3: Inferred from homology;
KW   Dipeptidase; Hydrolase; Manganese; Metal-binding; Metalloprotease;
KW   Protease.
FT   CHAIN           1..443
FT                   /note="Xaa-Pro dipeptidase"
FT                   /id="PRO_0000303869"
FT   BINDING         246
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01279"
FT   BINDING         257
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01279"
FT   BINDING         257
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01279"
FT   BINDING         339
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01279"
FT   BINDING         384
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01279"
FT   BINDING         423
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01279"
FT   BINDING         423
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01279"
SQ   SEQUENCE   443 AA;  50223 MW;  F08C18CF605406BB CRC64;
     MESLASLYKN HIATLQERTR DALARFKLDA LLIHSGELFN VFLDDHPYPF KVNPQFKAWV
     PVTQVPNCWL LVDGVNKPKL WFYLPVDYWH NVEPLPTSFW TEDVEVIALP KADGIGSLLP
     AARGNIGYIG LVQERALQLG IEASNINPKG VIDYLHYYRS FKTEYELACM REAQKMAVNG
     HRAAEEAFRS GMSEFDINIA YLTATGHRDT DVPYSNIVAL NEHAAVLHYT KLDHQAPEEM
     RSFLLDAGAE YNGYAADLTR TWSAKSDNDY AQLVKDVNDE QLALIATMKA GVSYVDYHIQ
     FHQRIAKLLR KHQIITDMSE EAMVENDLTG PFMPHGIGHP LGLQVHDVAG FMQDDSGTHL
     AAPAKYPYLR CTRILQPGMV LTIEPGIYFI ESLLAPWREG QFSKHFNWQK IEALKPFGGI
     RIEDNVVIHE NNVENMTRDL KLA