PEPQ_LACDE
ID PEPQ_LACDE Reviewed; 368 AA.
AC Q9S6S1;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Xaa-Pro dipeptidase;
DE Short=X-Pro dipeptidase;
DE EC=3.4.13.9;
DE AltName: Full=Imidodipeptidase;
DE AltName: Full=Proline dipeptidase;
DE Short=Prolidase;
GN Name=pepQ;
OS Lactobacillus delbrueckii subsp. bulgaricus.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=1585;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=CNRZ 397;
RX PubMed=10075426; DOI=10.1099/13500872-145-2-437;
RA Morel F., Frot-Coutaz J., Aubel D., Portalier R., Atlan D.;
RT "Characterization of a prolidase from Lactobacillus delbrueckii subsp.
RT bulgaricus CNRZ 397 with an unusual regulation of biosynthesis.";
RL Microbiology 145:437-446(1999).
CC -!- FUNCTION: Strict dipeptidase active on Xaa-Pro dipeptides, except Gly-
CC Pro and Pro-Pro.
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 -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.0.;
CC Temperature dependence:
CC Optimum temperature is 50 degrees Celsius.;
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase M24B family. {ECO:0000305}.
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DR EMBL; Y13385; CAA73815.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9S6S1; -.
DR SMR; Q9S6S1; -.
DR MEROPS; M24.006; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
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 InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR InterPro; IPR000587; Creatinase_N.
DR InterPro; IPR000994; Pept_M24.
DR InterPro; IPR001131; Peptidase_M24B_aminopep-P_CS.
DR Pfam; PF01321; Creatinase_N; 1.
DR Pfam; PF00557; Peptidase_M24; 1.
DR SUPFAM; SSF53092; SSF53092; 1.
DR SUPFAM; SSF55920; SSF55920; 1.
DR PROSITE; PS00491; PROLINE_PEPTIDASE; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Dipeptidase; Hydrolase; Manganese; Metal-binding;
KW Metalloprotease; Protease.
FT CHAIN 1..368
FT /note="Xaa-Pro dipeptidase"
FT /id="PRO_0000185090"
FT BINDING 223
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 234
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 234
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 298
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 327
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 341
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 341
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 368 AA; 41066 MW; D58273ADF812F1EA CRC64;
MNLDKLQNWL QENGMDVAYV SSPTTINYFT GFITDPEERI FKLFAFKDAE PFLFCPALNY
EEAKASAWDG DVVGYLDSED PWGKIAEEIK QRTKDYQNWA VEKNGLTVAH YQALHAQFPD
SDFSKDLSDF IAHIRLFKTE SELVKLRKAG EEADFAFQIG FEALRNGVTE RAVVSQIEYQ
LKLQKGVMQT SFDTIVQAGK NAANPHQGPS MNTVQPNELV LFDLGTMHEG YASDSSRTVA
YGEPTDKMRE IYEVNRTAQQ AAIDAAKPGM TASELDGVAR KIITDAGYGE YFIHRLGHGI
GMEVHEFPSI ANGNDVVLEE GMCFSIEPGI YIPGFAGVRI EDCGVLTKEG FKPFTHTSKE
LKVLPVKE
