ID   PEPQ_SODGM              Reviewed;         442 AA.
AC   Q2NWT2;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   03-AUG-2022, entry version 100.
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=SG0118;
OS   Sodalis glossinidius (strain morsitans).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Bruguierivoracaceae; Sodalis.
OX   NCBI_TaxID=343509;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=morsitans;
RX   PubMed=16365377; DOI=10.1101/gr.4106106;
RA   Toh H., Weiss B.L., Perkin S.A.H., Yamashita A., Oshima K., Hattori M.,
RA   Aksoy S.;
RT   "Massive genome erosion and functional adaptations provide insights into
RT   the symbiotic lifestyle of Sodalis glossinidius in the tsetse host.";
RL   Genome Res. 16:149-156(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; AP008232; BAE73393.1; -; Genomic_DNA.
DR   RefSeq; WP_011409983.1; NZ_LN854557.1.
DR   AlphaFoldDB; Q2NWT2; -.
DR   SMR; Q2NWT2; -.
DR   STRING; 343509.SG0118; -.
DR   MEROPS; M24.003; -.
DR   EnsemblBacteria; BAE73393; BAE73393; SG0118.
DR   KEGG; sgl:SG0118; -.
DR   eggNOG; COG0006; Bacteria.
DR   HOGENOM; CLU_050675_0_0_6; -.
DR   OMA; DFWHKVA; -.
DR   OrthoDB; 415910at2; -.
DR   BioCyc; SGLO343509:SGP1_RS00995-MON; -.
DR   Proteomes; UP000001932; 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..442
FT                   /note="Xaa-Pro dipeptidase"
FT                   /id="PRO_0000303871"
FT   BINDING         245
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01279"
FT   BINDING         256
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01279"
FT   BINDING         256
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01279"
FT   BINDING         338
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01279"
FT   BINDING         383
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01279"
FT   BINDING         422
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01279"
FT   BINDING         422
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01279"
SQ   SEQUENCE   442 AA;  50656 MW;  E274C2A374DE4523 CRC64;
     MESLSSLYRD HIATLQQRTR EILQRQQLEG LLIHAGEPIS RFLDDHDYPF KVNPQFKAWF
     PVTRVPHCWL WVDGVNKPKL WYYLSIDYWY LVEPLPDSFW TPYVDIVPFA DPDEIAALLP
     PRDNVAYLGS SPHRASLLGM ERDFINPQPV LDYLHYHRAY KTDYELACMR EAQKSAVNGH
     RAAKEAFLSG MCEFDINIAY LSACGHRDTD VPYDNIIALN EHAAVLHYTR LDQHTPEHVM
     SFLIDAGTEY NGYAADLTRT YAAQKDSDFA ALIAAMNSEQ QALIATIETG VNYIDYHLQM
     HGRIAKLLKQ FDILSGLSED AMVTEGLTLP FLPHGLGHPL GLQVHDVAGF MQDDRGTSLA
     PQSRYTHLRC TRVLQPRMVL TIEPGLYFIE SLLAPWRANT FGRHFNWSRI ESFKPYGGIR
     IEDNIVIHDN HIENMTRALK LE