ID PEPQ_YERPE Reviewed; 443 AA. AC Q0WAP4; Q74R11; Q8D1H7; DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot. DT 05-SEP-2006, sequence version 1. DT 27-MAR-2024, entry version 116. 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=YPO3765, y0465, YP_3283; OS Yersinia pestis. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Yersiniaceae; Yersinia. OX NCBI_TaxID=632; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CO-92 / Biovar Orientalis; RX PubMed=11586360; DOI=10.1038/35097083; RA Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G., RA Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L., RA Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M., RA Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T., RA Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S., RA Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J., RA Stevens K., Whitehead S., Barrell B.G.; RT "Genome sequence of Yersinia pestis, the causative agent of plague."; RL Nature 413:523-527(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KIM10+ / Biovar Mediaevalis; RX PubMed=12142430; DOI=10.1128/jb.184.16.4601-4611.2002; RA Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P., RA Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D., RA Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A., RA Nilles M.L., Matson J.S., Blattner F.R., Perry R.D.; RT "Genome sequence of Yersinia pestis KIM."; RL J. Bacteriol. 184:4601-4611(2002). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=91001 / Biovar Mediaevalis; RX PubMed=15368893; DOI=10.1093/dnares/11.3.179; RA Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D., RA Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L., RA Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H., RA Wang J., Huang P., Yang R.; RT "Complete genome sequence of Yersinia pestis strain 91001, an isolate RT avirulent to humans."; RL DNA Res. 11:179-197(2004). 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=H2O + Xaa-L-Pro dipeptide = an L-alpha-amino acid + L-proline; CC Xref=Rhea:RHEA:76407, ChEBI:CHEBI:15377, ChEBI:CHEBI:59869, CC ChEBI:CHEBI:60039, ChEBI:CHEBI:195196; EC=3.4.13.9; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01279}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|HAMAP- CC 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}. CC -!- SEQUENCE CAUTION: CC Sequence=AAM84054.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=AAS63450.1; Type=Erroneous initiation; Evidence={ECO:0000305}; 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; AL590842; CAL22352.1; -; Genomic_DNA. DR EMBL; AE009952; AAM84054.1; ALT_INIT; Genomic_DNA. DR EMBL; AE017042; AAS63450.1; ALT_INIT; Genomic_DNA. DR PIR; AE0458; AE0458. DR RefSeq; WP_002211547.1; NZ_WUCM01000112.1. DR RefSeq; YP_002348644.1; NC_003143.1. DR AlphaFoldDB; Q0WAP4; -. DR SMR; Q0WAP4; -. DR IntAct; Q0WAP4; 3. DR STRING; 214092.YPO3765; -. DR MEROPS; M24.003; -. DR PaxDb; 214092-YPO3765; -. DR DNASU; 1145412; -. DR EnsemblBacteria; AAS63450; AAS63450; YP_3283. DR GeneID; 57974943; -. DR KEGG; ype:YPO3765; -. DR KEGG; ypk:y0465; -. DR KEGG; ypm:YP_3283; -. DR PATRIC; fig|214092.21.peg.4287; -. DR eggNOG; COG0006; Bacteria. DR HOGENOM; CLU_050675_0_0_6; -. DR OMA; DFWHKVA; -. DR OrthoDB; 9806388at2; -. DR Proteomes; UP000000815; Chromosome. DR Proteomes; UP000001019; Chromosome. DR Proteomes; UP000002490; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0004177; F:aminopeptidase activity; IBA:GO_Central. 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; IBA:GO_Central. DR Gene3D; 3.90.230.10; Creatinase/methionine aminopeptidase superfamily; 1. DR Gene3D; 3.40.350.10; Creatinase/prolidase N-terminal domain; 1. DR HAMAP; MF_01279; X_Pro_dipeptid; 1. DR InterPro; IPR029149; Creatin/AminoP/Spt16_NTD. DR InterPro; IPR036005; Creatinase/aminopeptidase-like. DR InterPro; IPR048819; PepQ_N. DR InterPro; IPR000994; Pept_M24. DR InterPro; IPR001131; Peptidase_M24B_aminopep-P_CS. DR InterPro; IPR022846; X_Pro_dipept. DR PANTHER; PTHR43226; XAA-PRO AMINOPEPTIDASE 3; 1. DR PANTHER; PTHR43226:SF4; XAA-PRO AMINOPEPTIDASE 3; 1. DR Pfam; PF21216; PepQ_N; 1. DR Pfam; PF00557; Peptidase_M24; 1. DR SUPFAM; SSF55920; Creatinase/aminopeptidase; 1. DR PROSITE; PS00491; PROLINE_PEPTIDASE; 1. PE 3: Inferred from homology; KW Dipeptidase; Hydrolase; Manganese; Metal-binding; Metalloprotease; KW Protease; Reference proteome. FT CHAIN 1..443 FT /note="Xaa-Pro dipeptidase" FT /id="PRO_0000303879" 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; 50912 MW; 63FD90A35262F27E CRC64; METLASLYNE HLSTLQQRTR DVLERHQLDA LLIHSGELQR LFLDDRDYPF KVNPQFKAWV PVTEVPNCWL WVDGVNTPKL WFYSPVDYWH SVEPLPDSFW TKNIDVQPLL NADDIAQQLP VQRERVAYIG YAQQRAQALG FSAENINPQP VLDYLHYYRS YKTDYELACM REAQKTAVVG HRAAYEAFQS GMSEFDINLA YLMATGHRDT DVPYDNIVAL NEHSAVLHYT ILQHQPPAEI RSFLIDAGAE YNGYAADLTR TYTADRDSDF AALISDLNTE QLALIDTIKS GERYTDYHVQ MHQRIAKLLR THNLVTGISE EAMVEQGITC PFLPHGLGHP LGLQVHDTAG FMQDDKGTNL NAPSKYPYLR CTRVLQPRMV LTIEPGLYFI DSLLAPWRIG EFSKHFNWDR IDALKPYGGI RIEDNIVIHD KRVENMTRDL KLA //