(data stored in SCRATCH zone)

SWISSPROT: 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   11-DEC-2019, entry version 99.
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}.
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   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   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;
DR   PRODOM; P46545.
DR   SWISS-2DPAGE; P46545.
KW   Cytoplasm; Dipeptidase; Hydrolase; Manganese; Metal-binding;
KW   Metalloprotease; Protease.
FT   CHAIN           1..368
FT                   /note="Xaa-Pro dipeptidase"
FT                   /id="PRO_0000185091"
FT   METAL           223
FT                   /note="Manganese 2"
FT                   /evidence="ECO:0000250"
FT   METAL           234
FT                   /note="Manganese 1"
FT                   /evidence="ECO:0000250"
FT   METAL           234
FT                   /note="Manganese 2"
FT                   /evidence="ECO:0000250"
FT   METAL           298
FT                   /note="Manganese 1"
FT                   /evidence="ECO:0000250"
FT   METAL           327
FT                   /note="Manganese 1"
FT                   /evidence="ECO:0000250"
FT   METAL           341
FT                   /note="Manganese 1"
FT                   /evidence="ECO:0000250"
FT   METAL           341
FT                   /note="Manganese 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
//

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