PEPQ_LACHE
ID PEPQ_LACHE Reviewed; 368 AA.
AC O84913;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 113.
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 helveticus (Lactobacillus suntoryeus).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=1587;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=CNRZ 32;
RA Yuksel G.U., Steele J.L.;
RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
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; AF012084; AAC24966.1; -; Genomic_DNA.
DR RefSeq; WP_003627740.1; NZ_SCLV01000060.1.
DR AlphaFoldDB; O84913; -.
DR SMR; O84913; -.
DR STRING; 326425.lhe_1650; -.
DR MEROPS; M24.006; -.
DR GeneID; 66452647; -.
DR eggNOG; COG0006; Bacteria.
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_0000185092"
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; 41238 MW; F405E3D783DEE396 CRC64;
MNLDKLQQWL QDSNNDIAYI SNPITISYFT GYSMDPHERI FALLVFKDAN PFIFCPALNV
EEAKNSEWNG DVFGYLDSED PWELIADNVR KRTSDTHTWA IEKDDLSVAH YQYLRGEFPN
ASFTNDVSSF IERLRLYKTP EEIKKLQGAG AEADFAFKIG FDAIRTGVTE RSIAGQIDYQ
LKIQKGVMHE SFETIVQAGK NAANPHLGPT MNTVQPNELV LFDLGTMHDG YASDSSRTVA
YGTPSDKQRE IYEVDREAQQ AAIEAAKPGI TAEELDSVAR DIITKAGYGE YFIHRLGHGI
GKNVHEYPSI VQGNDLVLEE GMCFSIEPGI YIPGFAGVRI EDCGVVTKDG FKTFTHTDKD
LKIIPIRD
