(data stored in SCRATCH9089 zone)

SWISSPROT: PEPE_PASMU

ID   PEPE_PASMU              Reviewed;         234 AA.
AC   Q9CNH7;
DT   19-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   19-DEC-2001, sequence version 2.
DT   11-DEC-2019, entry version 100.
DE   RecName: Full=Peptidase E {ECO:0000255|HAMAP-Rule:MF_00510};
DE            EC=3.4.13.21 {ECO:0000255|HAMAP-Rule:MF_00510};
DE   AltName: Full=Alpha-aspartyl dipeptidase {ECO:0000255|HAMAP-Rule:MF_00510};
DE   AltName: Full=Asp-specific dipeptidase {ECO:0000255|HAMAP-Rule:MF_00510};
DE   AltName: Full=Dipeptidase E {ECO:0000255|HAMAP-Rule:MF_00510};
GN   Name=pepE {ECO:0000255|HAMAP-Rule:MF_00510}; OrderedLocusNames=PM0454;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
CC   -!- FUNCTION: Hydrolyzes dipeptides containing N-terminal aspartate
CC       residues. May play a role in allowing the cell to use peptide aspartate
CC       to spare carbon otherwise required for the synthesis of the aspartate
CC       family of amino acids. {ECO:0000255|HAMAP-Rule:MF_00510}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Dipeptidase E catalyzes the hydrolysis of dipeptides Asp-|-
CC         Xaa. It does not act on peptides with N-terminal Glu, Asn or Gln, nor
CC         does it cleave isoaspartyl peptides.; EC=3.4.13.21;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00510};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00510}.
CC   -!- SIMILARITY: Belongs to the peptidase S51 family. {ECO:0000255|HAMAP-
CC       Rule:MF_00510}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK02538.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; AE004439; AAK02538.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_005721773.1; NC_002663.1.
DR   SMR; Q9CNH7; -.
DR   MEROPS; S51.001; -.
DR   EnsemblBacteria; AAK02538; AAK02538; PM0454.
DR   GeneID; 29388862; -.
DR   KEGG; pmu:PM0454; -.
DR   eggNOG; ENOG4105EQ6; Bacteria.
DR   eggNOG; COG3340; LUCA.
DR   HOGENOM; HOG000281834; -.
DR   KO; K05995; -.
DR   OMA; KYTATVR; -.
DR   BioCyc; PMUL272843:G1FZ8-475-MONOMER; -.
DR   Proteomes; UP000000809; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016805; F:dipeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR   CDD; cd03146; GAT1_Peptidase_E; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   HAMAP; MF_00510; Peptidase_E; 1.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR005320; Peptidase_S51.
DR   InterPro; IPR023172; Peptidase_S51_dipeptidase-E.
DR   Pfam; PF03575; Peptidase_S51; 1.
DR   SUPFAM; SSF52317; SSF52317; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q9CNH7.
DR   SWISS-2DPAGE; Q9CNH7.
KW   Cytoplasm; Dipeptidase; Hydrolase; Protease; Reference proteome;
KW   Serine protease.
FT   CHAIN           1..234
FT                   /note="Peptidase E"
FT                   /id="PRO_0000209959"
FT   ACT_SITE        123
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00510"
FT   ACT_SITE        138
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00510"
FT   ACT_SITE        160
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00510"
SQ   SEQUENCE   234 AA;  26058 MW;  7788FC7E5463E6C8 CRC64;
     MKNMLLMSGS KYQNTDYLVH TLPWLQDFLA DYQGKTVAFV PYAGVRQSYD EYELKVQKAL
     AELNVAILSV HRAEKHAEII EKADVIAIGG GNTFCLLKGM YEHHLLPLIR EKVQSGTPYF
     GWSAGANVAG RSIMTTNDMP ITYPPSFDAL NLFPHQLNPH FISGKPAGHN GESREERLAE
     FLIVNPTANV YALPEGTALH IQGQQARVLG QHDVLLFSEN MQLATLPVNS VFDY
//

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