PEPQ_XANCP
ID PEPQ_XANCP Reviewed; 441 AA.
AC Q8P5S9;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 112.
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=XCC3257;
OS Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB
OS 528 / LMG 568 / P 25).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=190485;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25;
RX PubMed=12024217; DOI=10.1038/417459a;
RA da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr.,
RA Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A.,
RA Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT specificities.";
RL Nature 417:459-463(2002).
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; AE008922; AAM42527.1; -; Genomic_DNA.
DR RefSeq; NP_638603.1; NC_003902.1.
DR RefSeq; WP_011038359.1; NC_003902.1.
DR AlphaFoldDB; Q8P5S9; -.
DR SMR; Q8P5S9; -.
DR STRING; 340.xcc-b100_0927; -.
DR MEROPS; M24.003; -.
DR EnsemblBacteria; AAM42527; AAM42527; XCC3257.
DR KEGG; xcc:XCC3257; -.
DR PATRIC; fig|190485.4.peg.3481; -.
DR eggNOG; COG0006; Bacteria.
DR HOGENOM; CLU_050675_0_0_6; -.
DR OMA; DFWHKVA; -.
DR Proteomes; UP000001010; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004177; F:aminopeptidase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008235; F:metalloexopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008233; F:peptidase activity; IBA:GO_Central.
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..441
FT /note="Xaa-Pro dipeptidase"
FT /id="PRO_0000303873"
FT BINDING 244
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01279"
FT BINDING 255
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01279"
FT BINDING 255
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01279"
FT BINDING 336
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01279"
FT BINDING 381
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01279"
FT BINDING 420
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01279"
FT BINDING 420
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01279"
SQ SEQUENCE 441 AA; 48251 MW; CC6846FA0A31CE5D CRC64;
MTQPSLSVLY SDHLRTLTAR ADQALQRGGF DHLVIPSGTT HYQLFDDRDY PFAVNPQFKA
WVPLTRMPHS WLVYTPGKRP TVIFYQPFDY WHVVPDAPSG WWVEHCDIHI IRTPEAALPL
LPARTERCAI LGEAASALGA CVPNNPAAVL DFLDYQRAFK TPYELAVMRL AQQLAVRGHR
AAEAAFRAGQ SEFGIHMAYC SAVGQDANEL PYGNIIALNE HGAVLHYTEL GRQAPQPLRS
FLIDAGASAH GYASDITRTY AADAGSEFQA LIDAVDAAQL RMGNAVRAGM DYKQLHVDAH
LSLMGILHDF GIITVSPEAA LATGVSAAFF PHGLGHLIGL QVHDVAGFAA SDRGGRIERP
DGHPYLRLTR VLEPGMVVTI EPGVYFIDML LDEVKKNGHA ASVNWDRVAQ FAPYGGIRIE
DEVVCTDGDP ENLTRPVFAA P
