ID   PEPE_NOSS1              Reviewed;         242 AA.
AC   P58493;
DT   19-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   19-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 93.
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=alr7184;
OS   Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OG   Plasmid pCC7120alpha.
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=103690;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX   PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA   Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA   Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA   Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT   "Complete genomic sequence of the filamentous nitrogen-fixing
RT   cyanobacterium Anabaena sp. strain PCC 7120.";
RL   DNA Res. 8:205-213(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=BAB78268.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; BA000020; BAB78268.1; ALT_FRAME; Genomic_DNA.
DR   PIR; AH2500; AH2500.
DR   AlphaFoldDB; P58493; -.
DR   SMR; P58493; -.
DR   MEROPS; S51.001; -.
DR   EnsemblBacteria; BAB78268; BAB78268; BAB78268.
DR   KEGG; ana:alr7184; -.
DR   Proteomes; UP000002483; Plasmid pCC7120alpha.
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   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-UniRule.
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;
KW   Cytoplasm; Dipeptidase; Hydrolase; Plasmid; Protease; Reference proteome;
KW   Serine protease.
FT   CHAIN           1..242
FT                   /note="Peptidase E"
FT                   /id="PRO_0000209954"
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   242 AA;  27458 MW;  E2F6CBAE9C18F98F CRC64;
     MSKRLLLLSN STNIGEEYLF YARQEIKNFL GSSVKKIAFI PFAAVTSTYQ HYSEKVRKVF
     QDIGYEFDAI HLVESSHELI KNAEAVVVGG GNTFHLIHCL HETKLLDDIR NKVSNGTPYI
     GWSAGSNVAC PTIKTSNDMP IIEPISFQGL NLVPFQINPH YTNAVIPNHN GETREQRLED
     FLVLNPDIYV VGLPEGTMLK IEDSSIRLIG NKTIYLFKFG EEKQEYYPHD NLDFLLERAS
     FT