ID A0A170XJP3_KLEOX Unreviewed; 443 AA. AC A0A170XJP3; DT 06-JUL-2016, integrated into UniProtKB/TrEMBL. DT 06-JUL-2016, sequence version 1. DT 05-DEC-2018, entry version 14. 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- CC terminal 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 CC aminoacyl-hydroxyproline analogs. No action on Pro-|-Pro.; CC EC=3.4.13.9; Evidence={ECO:0000256|HAMAP-Rule:MF_01279, CC ECO:0000256|SAAS:SAAS01100874}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|HAMAP- CC 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 ProteinModelPortal; A0A170XJP3; -. 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 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 Complete proteome {ECO:0000313|Proteomes:UP000077958}; KW Dipeptidase {ECO:0000256|HAMAP-Rule:MF_01279, KW ECO:0000256|SAAS:SAAS00016572, ECO:0000313|EMBL:SAP83745.1}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01279, KW ECO:0000256|SAAS:SAAS00016567, ECO:0000313|EMBL:SAP83745.1}; KW Manganese {ECO:0000256|HAMAP-Rule:MF_01279, KW ECO:0000256|SAAS:SAAS00016588}; 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:SAAS00424115}; KW Protease {ECO:0000256|HAMAP-Rule:MF_01279, KW ECO:0000256|SAAS:SAAS00016564}. FT DOMAIN 168 430 Peptidase_M24. {ECO:0000259|Pfam: FT PF00557}. FT METAL 246 246 Manganese 2. {ECO:0000256|HAMAP-Rule: FT MF_01279}. FT METAL 257 257 Manganese 1. {ECO:0000256|HAMAP-Rule: FT MF_01279}. FT METAL 257 257 Manganese 2. {ECO:0000256|HAMAP-Rule: FT MF_01279}. FT METAL 339 339 Manganese 1. {ECO:0000256|HAMAP-Rule: FT MF_01279}. FT METAL 384 384 Manganese 1. {ECO:0000256|HAMAP-Rule: FT MF_01279}. FT METAL 423 423 Manganese 1. {ECO:0000256|HAMAP-Rule: FT MF_01279}. FT METAL 423 423 Manganese 2. {ECO:0000256|HAMAP-Rule: FT 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 //