PEPQ_SHIFL
ID PEPQ_SHIFL Reviewed; 443 AA.
AC Q83PG0; Q7UB58;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 124.
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};
GN OrderedLocusNames=SF3923, S3829;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
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; AE005674; AAN45358.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP18840.1; -; Genomic_DNA.
DR RefSeq; NP_709651.1; NC_004337.2.
DR RefSeq; WP_000444563.1; NZ_WPGW01000036.1.
DR AlphaFoldDB; Q83PG0; -.
DR SMR; Q83PG0; -.
DR STRING; 198214.SF3923; -.
DR MEROPS; M24.003; -.
DR EnsemblBacteria; AAN45358; AAN45358; SF3923.
DR EnsemblBacteria; AAP18840; AAP18840; S3829.
DR GeneID; 1024129; -.
DR KEGG; sfl:SF3923; -.
DR KEGG; sft:NCTC1_04240; -.
DR KEGG; sfx:S3829; -.
DR PATRIC; fig|198214.7.peg.4623; -.
DR HOGENOM; CLU_050675_0_0_6; -.
DR OrthoDB; 415910at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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..443
FT /note="Xaa-Pro dipeptidase"
FT /id="PRO_0000303868"
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"
FT CONFLICT 155
FT /note="L -> Q (in Ref. 2; AAP18840)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 443 AA; 50236 MW; D925C3215986F670 CRC64;
MESLASLYKN HIATLQERTR DALARFKLDA LLIHSGELFN VFLDDHPYPF KVNPQFKAWV
PVTQVPNCWL LVDGVNKPKL WFYLPVDYWH NVEPLPTSFW TEDVEVIALP KADGIGSLLP
AARGNIGYIG PVPERALQLG IEASNINPKG VIDYLHYYRS FKTEYELACM REAQKMAVNG
HRAAEEAFRS GMSEFDINIA YLTATGHRDT DVPYSNIVAL NEHAAVLHYT KLDHQAPEEM
RSFLLDAGAE YNGYAADLTR TWSAKSDNDY AQLVKDVNDE QLALIATMKA GVSYVDYHIQ
FHQRIAKLLR KHQIITDMSE EAMVENDLTG PFMPHGIGHP LGLQVHDVAG FMQDDSGTHL
AAPAKYPYLR YTRILQPGMV LTIEPGIYFI ESLLAPWREG QFSKHFNWQK IEALKPFGGI
RIEDNVVIHE NNVENMTRDL KLA
