PEPQ_YERPN
ID PEPQ_YERPN Reviewed; 443 AA.
AC Q1CN98; D1Q192;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 99.
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=YPN_0199;
GN ORFNames=YP516_0165;
OS Yersinia pestis bv. Antiqua (strain Nepal516).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=377628;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nepal516;
RX PubMed=16740952; DOI=10.1128/jb.00124-06;
RA Chain P.S.G., Hu P., Malfatti S.A., Radnedge L., Larimer F., Vergez L.M.,
RA Worsham P., Chu M.C., Andersen G.L.;
RT "Complete genome sequence of Yersinia pestis strains Antiqua and Nepal516:
RT evidence of gene reduction in an emerging pathogen.";
RL J. Bacteriol. 188:4453-4463(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nepal516;
RA Plunkett G. III, Anderson B.D., Baumler D.J., Burland V., Cabot E.L.,
RA Glasner J.D., Mau B., Neeno-Eckwall E., Perna N.T., Munk A.C., Tapia R.,
RA Green L.D., Rogers Y.C., Detter J.C., Bruce D.C., Brettin T.S.;
RT "Yersinia pestis Nepal516A whole genome shotgun sequencing project.";
RL Submitted (APR-2009) 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; CP000305; ABG16532.1; -; Genomic_DNA.
DR EMBL; ACNQ01000001; EEO78646.1; -; Genomic_DNA.
DR PIR; AE0458; AE0458.
DR RefSeq; WP_002211547.1; NZ_ACNQ01000001.1.
DR AlphaFoldDB; Q1CN98; -.
DR SMR; Q1CN98; -.
DR MEROPS; M24.003; -.
DR EnsemblBacteria; ABG16532; ABG16532; YPN_0199.
DR GeneID; 57974943; -.
DR KEGG; ypn:YPN_0199; -.
DR HOGENOM; CLU_050675_0_0_6; -.
DR OMA; DFWHKVA; -.
DR Proteomes; UP000008936; 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..443
FT /note="Xaa-Pro dipeptidase"
FT /id="PRO_0000303881"
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
