PEPQ_LACDL
ID PEPQ_LACDL Reviewed; 368 AA.
AC P46545;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 103.
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. lactis.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=29397;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DSM 7290;
RX PubMed=7770058; DOI=10.1007/bf00293152;
RA Stucky K., Klein J.R., Schueller A., Matern H., Henrich B., Plapp R.;
RT "Cloning and DNA sequence analysis of pepQ, a prolidase gene from
RT Lactobacillus delbrueckii subsp. lactis DSM7290 and partial
RT characterization of its product.";
RL Mol. Gen. Genet. 247:494-500(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DSM 7290;
RX PubMed=7851736; DOI=10.1111/j.1574-6968.1994.tb07299.x;
RA Klein J., Henrich B., Plapp R.;
RT "Cloning and nucleotide sequence analysis of the Lactobacillus delbrueckii
RT ssp. lactis DSM7290 cysteine aminopeptidase gene pepC.";
RL FEMS Microbiol. Lett. 124:291-299(1994).
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase M24B family. {ECO:0000305}.
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DR EMBL; Z34896; CAA84379.1; -; Genomic_DNA.
DR EMBL; Z54205; CAA90911.1; -; Genomic_DNA.
DR PIR; S55037; S52202.
DR RefSeq; WP_002876588.1; NZ_LS991409.1.
DR AlphaFoldDB; P46545; -.
DR SMR; P46545; -.
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 3: Inferred from homology;
KW Cytoplasm; Dipeptidase; Hydrolase; Manganese; Metal-binding;
KW Metalloprotease; Protease.
FT CHAIN 1..368
FT /note="Xaa-Pro dipeptidase"
FT /id="PRO_0000185091"
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; 41082 MW; 514121D9076384D0 CRC64;
MNLDKLQNWL QENGMDVAYV SSPTTINYFT GFITDPEERI FKLFAFKDAE PFLFCPALNY
EEAKASAWDG DVVGYLDSED PWSKIAEEIK KRTKDYQNWA VEKNGLTVAH YQALHAQFPD
SDFSKDLSDF IAHIRLFKTE SELVKLRKAG EEADFAFQIG FEALRNGVTE RAVVSQIEYQ
LKLQKGVMQT SFDTIVQAGK NAANPHQGPS MNTVQPNELV LFDLGTMHEG YASDSSRTVA
YGEPTDKMRE IYEVNRTAQQ AAIDAAKPGM TASELDGVAR KIITDAGYGE YFIHRLGHGI
GMEVHEFPSI ANGNDVVLEE GMCFSIEPGI YIPGFAGVRI EDCGVLTKDG FKPFTHTSKE
LKVLPVKE
