PEPQ_HAHCH
ID PEPQ_HAHCH Reviewed; 438 AA.
AC Q2S6U2;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 100.
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=HCH_07017;
OS Hahella chejuensis (strain KCTC 2396).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC Hahellaceae; Hahella.
OX NCBI_TaxID=349521;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 2396;
RX PubMed=16352867; DOI=10.1093/nar/gki1016;
RA Jeong H., Yim J.H., Lee C., Choi S.-H., Park Y.K., Yoon S.H., Hur C.-G.,
RA Kang H.-Y., Kim D., Lee H.H., Park K.H., Park S.-H., Park H.-S., Lee H.K.,
RA Oh T.K., Kim J.F.;
RT "Genomic blueprint of Hahella chejuensis, a marine microbe producing an
RT algicidal agent.";
RL Nucleic Acids Res. 33:7066-7073(2005).
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; CP000155; ABC33632.1; -; Genomic_DNA.
DR RefSeq; WP_011400682.1; NC_007645.1.
DR AlphaFoldDB; Q2S6U2; -.
DR SMR; Q2S6U2; -.
DR STRING; 349521.HCH_07017; -.
DR EnsemblBacteria; ABC33632; ABC33632; HCH_07017.
DR KEGG; hch:HCH_07017; -.
DR eggNOG; COG0006; Bacteria.
DR HOGENOM; CLU_050675_0_0_6; -.
DR OMA; DFWHKVA; -.
DR OrthoDB; 415910at2; -.
DR Proteomes; UP000000238; 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; Reference proteome.
FT CHAIN 1..438
FT /note="Xaa-Pro dipeptidase"
FT /id="PRO_0000303846"
FT BINDING 240
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01279"
FT BINDING 251
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01279"
FT BINDING 251
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01279"
FT BINDING 331
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01279"
FT BINDING 376
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01279"
FT BINDING 415
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01279"
FT BINDING 415
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01279"
SQ SEQUENCE 438 AA; 48837 MW; A6460CCDBB995894 CRC64;
MSDSAYQNHL SILRKRFDQA LLETDFDGVI LASGRLTYYF GDDHSHPFHP YAMAQQWAPF
DLMPDVFIHI QRGETPRLLW PAKQDFWHVV YPIPEGGWCD QWRVEPVSSL QEWLPQISGK
TAWIGPEYNE APGLNPNLSV NPEALLHRLN YQRAYKTEFE IDCLWRANQA GAAGHKAAQA
AFLTGKSECD VYRDFLAASG QLSNQEPYPG IVALNENAAV LHYEKKNPLK PDAMRTLLID
AGAAYGGYAS DITRTYTAGS GLFAELIERV NTLQLSIAAQ AVHGKAFSEL HQATLAGVAN
ILHETRICSL SVEAQLDKRI PQVFFPHGLG HLLGLQVHDV GGHQQDKTGT LRKPDESAPF
LRLTRTLEKD MVITIEPGLY FIPMLLDNMV KNIAGHGCDL DLIETLKPYG GIRIEDNVVV
QEGRSRNLTR EAFSALLA
