PEPQ_ENT38
ID PEPQ_ENT38 Reviewed; 443 AA.
AC A4WFX3;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 89.
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=Ent638_3948;
OS Enterobacter sp. (strain 638).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Enterobacter.
OX NCBI_TaxID=399742;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=638;
RX PubMed=20485560; DOI=10.1371/journal.pgen.1000943;
RA Taghavi S., van der Lelie D., Hoffman A., Zhang Y.B., Walla M.D.,
RA Vangronsveld J., Newman L., Monchy S.;
RT "Genome sequence of the plant growth promoting endophytic bacterium
RT Enterobacter sp. 638.";
RL PLoS Genet. 6:E1000943-E1000943(2010).
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; CP000653; ABP62603.1; -; Genomic_DNA.
DR RefSeq; WP_015960908.1; NC_009436.1.
DR AlphaFoldDB; A4WFX3; -.
DR SMR; A4WFX3; -.
DR STRING; 399742.Ent638_3948; -.
DR MEROPS; M24.003; -.
DR EnsemblBacteria; ABP62603; ABP62603; Ent638_3948.
DR KEGG; ent:Ent638_3948; -.
DR eggNOG; COG0006; Bacteria.
DR HOGENOM; CLU_050675_0_0_6; -.
DR OMA; DFWHKVA; -.
DR OrthoDB; 415910at2; -.
DR Proteomes; UP000000230; 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_1000067402"
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; 50204 MW; F615860C45FEC016 CRC64;
MDSLAALYKN HIVTLQERTR DVLTRFKLDA LLIHSGELLN VFLDDHAYPF KVNPQFKAWV
PVTQVPNCWL LVDGVNKPKL WFYLPVDYWH NVEPLPTTFW TEEVDVIALP KADGIGSQLP
AARGNIAYIG PVPERALGLD IPADKINPKG VIDYLHYYRA YKTDYELSCM REAQKTAVNG
HQAAHEAFLS GMSEFDINQA YLTATGHRDT DVPYGNIVAL NEHASVLHYT KLDHRAPSEI
RSFLLDAGAE YNGYAADLTR TWAANSDTDF AHLIKDVNDE QLALISTMKA GTSYVDYHIQ
FHQRIAKLLR KHQIVTDMSE EAMVENDLTG PFMPHGIGHP LGLQVHDVAG FMQDDTGTHL
AAPSKYPYLR CTRVLEPRMV LTIEPGIYFI DSLLNPWREG QFSKHFNWQK IDALKPFGGI
RIEDNVVVHE NNIENMTRDQ KLA