ID   PEPQ_SHEB9              Reviewed;         440 AA.
AC   A9KU92;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 86.
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};
GN   OrderedLocusNames=Sbal195_0021;
OS   Shewanella baltica (strain OS195).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=399599;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OS195;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Brettar I.,
RA   Rodrigues J., Konstantinidis K., Klappenbach J., Hofle M., Tiedje J.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Shewanella baltica OS195.";
RL   Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000891; ABX47203.1; -; Genomic_DNA.
DR   RefSeq; WP_006084787.1; NC_009997.1.
DR   AlphaFoldDB; A9KU92; -.
DR   SMR; A9KU92; -.
DR   MEROPS; M24.003; -.
DR   EnsemblBacteria; ABX47203; ABX47203; Sbal195_0021.
DR   GeneID; 11770391; -.
DR   KEGG; sbn:Sbal195_0021; -.
DR   HOGENOM; CLU_050675_0_0_6; -.
DR   OMA; DFWHKVA; -.
DR   Proteomes; UP000000770; 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; SSF53092; SSF53092; 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..440
FT                   /note="Xaa-Pro dipeptidase"
FT                   /id="PRO_1000085886"
FT   BINDING         244
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01279"
FT   BINDING         255
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01279"
FT   BINDING         255
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01279"
FT   BINDING         335
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01279"
FT   BINDING         380
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01279"
FT   BINDING         419
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01279"
FT   BINDING         419
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01279"
SQ   SEQUENCE   440 AA;  50131 MW;  A37C809ADE0349BC CRC64;
     MDQLAHHYRA HIAELNRRVA EILSREALSG LVIHSGQPHR MFLDDINYPF KANPHFKAWL
     PVLDNPNCWL VVNGRDKPQL IFYRPVDFWH KVSDVPDMFW TEYFDIKLLT KADKVAEFLP
     TDIANWAYLG EHLDVAEVLG FTSRNPDAVM SYLHYHRTTK TEYELECMRR ANQIAVQGHL
     AAKNAFYNGA SEFEIQQHYL SAVGQSENEV PYGNIIALNQ NAAILHYTAL EHQSPAKRLS
     FLIDAGASYF GYASDITRTY AFEKNRFDEL ITAMNKAQLE LIDMMRPGVR YPDLHLATHA
     KVAQMLLDFD LATGDVQGLI DQGITSAFFP HGLGHMLGLQ VHDVGGFSHD ERGTHIAAPE
     AHPFLRCTRI LAPNQVLTME PGLYIIDTLL NELKQDSRGQ QINWQTVDEL RPFGGIRIED
     NVIVHQDRNE NMTRELGLTD