ID A0A170XJP3_KLEOX Unreviewed; 443 AA. AC A0A170XJP3; DT 06-JUL-2016, integrated into UniProtKB/TrEMBL. DT 06-JUL-2016, sequence version 1. DT 11-DEC-2019, entry version 18. DE RecName: Full=Xaa-Pro dipeptidase {ECO:0000256|HAMAP-Rule:MF_01279}; DE Short=X-Pro dipeptidase {ECO:0000256|HAMAP-Rule:MF_01279}; DE EC=3.4.13.9 {ECO:0000256|HAMAP-Rule:MF_01279}; DE AltName: Full=Imidodipeptidase {ECO:0000256|HAMAP-Rule:MF_01279}; DE AltName: Full=Proline dipeptidase {ECO:0000256|HAMAP-Rule:MF_01279}; DE Short=Prolidase {ECO:0000256|HAMAP-Rule:MF_01279}; GN Name=pepQ {ECO:0000256|HAMAP-Rule:MF_01279, GN ECO:0000313|EMBL:SAP83745.1}; GN ORFNames=SAMEA2273741_03664 {ECO:0000313|EMBL:SAP83745.1}; OS Klebsiella oxytoca. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Klebsiella. OX NCBI_TaxID=571 {ECO:0000313|EMBL:SAP83745.1, ECO:0000313|Proteomes:UP000077958}; RN [1] {ECO:0000313|EMBL:SAP83745.1, ECO:0000313|Proteomes:UP000077958} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=2880STDY5682666 {ECO:0000313|EMBL:SAP83745.1, RC ECO:0000313|Proteomes:UP000077958}; RG Pathogen Informatics; RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Splits dipeptides with a prolyl residue in the C-terminal CC position. {ECO:0000256|HAMAP-Rule:MF_01279, CC ECO:0000256|SAAS:SAAS01095084}. 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:0000256|HAMAP-Rule:MF_01279, CC ECO:0000256|SAAS:SAAS01116517}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01279}; CC Note=Binds 2 manganese ions per subunit. {ECO:0000256|HAMAP- CC Rule:MF_01279}; CC -!- SIMILARITY: Belongs to the peptidase M24B family. Bacterial-type CC prolidase subfamily. {ECO:0000256|HAMAP-Rule:MF_01279, CC ECO:0000256|SAAS:SAAS00588006}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; FKYV01000015; SAP83745.1; -; Genomic_DNA. DR RefSeq; WP_000444546.1; NZ_FKYV01000015.1. DR SMR; A0A170XJP3; -. DR EnsemblBacteria; SAP83745; SAP83745; SAMEA2273741_03664. DR Proteomes; UP000077958; Unassembled WGS sequence. 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 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 {ECO:0000256|HAMAP-Rule:MF_01279, KW ECO:0000256|SAAS:SAAS00131564, ECO:0000313|EMBL:SAP83745.1}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01279, ECO:0000256|SAAS:SAAS00424124, KW ECO:0000313|EMBL:SAP83745.1}; KW Manganese {ECO:0000256|HAMAP-Rule:MF_01279, ECO:0000256|SAAS:SAAS00424130}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01279, KW ECO:0000256|SAAS:SAAS00016576}; KW Metalloprotease {ECO:0000256|HAMAP-Rule:MF_01279, KW ECO:0000256|SAAS:SAAS00016593}; KW Protease {ECO:0000256|HAMAP-Rule:MF_01279, ECO:0000256|SAAS:SAAS00424123}. FT DOMAIN 168..430 FT /note="Peptidase_M24" FT /evidence="ECO:0000259|Pfam:PF00557" FT METAL 246 FT /note="Manganese 2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01279" FT METAL 257 FT /note="Manganese 1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01279" FT METAL 257 FT /note="Manganese 2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01279" FT METAL 339 FT /note="Manganese 1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01279" FT METAL 384 FT /note="Manganese 1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01279" FT METAL 423 FT /note="Manganese 1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01279" FT METAL 423 FT /note="Manganese 2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01279" SQ SEQUENCE 443 AA; 50162 MW; 82B4EF87C0DBB0B5 CRC64; MESLASLYKN HIATLQERTR DALARFKLDA LLIHSGELFN VFLDDHPYPF KVNPQFKAWV PVTQVPNCWL LVDGVNKPKL WFYLPVDYWH NVEPLPNSFW TEDVEVIALP KADGIGSLLP AARGNIGYIG PVPERALQLG 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 NSVENMTRDL KLA //