(data stored in ACNUC9435 zone)

HOGENOM: ECOK1_1_PE1006

ID   ECOK1_1_PE1006                       STANDARD;      PRT;   408 AA.
AC   ECOK1_1_PE1006; A1AA21;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Peptidase T; EC=3.4.11 4;AltName: Full=Aminotripeptidase;
DE   Short=Tripeptidase;AltName: Full=Tripeptide aminopeptidase;
DE   (ECOK1_1.PE1006).
GN   Name=pepT; OrderedLocusNames=Ecok1_10170; ORFNames=APECO1_209;
OS   ESCHERICHIA COLI APEC O1.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=405955;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ECOK1_1.PE1006.
CC       Escherichia coli APEC O1, complete genome.
CC       chromosome, complete sequence.
CC   -!- ANNOTATIONS ORIGIN:PEPT_ECOK1
CC   -!- FUNCTION: Cleaves the N-terminal amino acid of tripeptides (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: Release of the N-terminal residue from a
CC       tripeptide.
CC   -!- COFACTOR: Binds 2 zinc ions per subunit (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the peptidase M20B family.
CC   -!- GENE_FAMILY: HOG000032390 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; A1AA21; -.
DR   EMBL; CP000468; ABJ00511.1; -; Genomic_DNA.
DR   RefSeq; YP_852225.1; NC_008563.1.
DR   ProteinModelPortal; A1AA21; -.
DR   SMR; A1AA21; 1-408.
DR   STRING; A1AA21; -.
DR   EnsemblBacteria; EBESCT00000039492; EBESCP00000038009; EBESCG00000038542.
DR   GeneID; 4492297; -.
DR   GenomeReviews; CP000468_GR; Ecok1_10170.
DR   KEGG; ecv:APECO1_209; -.
DR   eggNOG; COG2195; -.
DR   GeneTree; EBGT00050000009694; -.
DR   OMA; HMDTAPD; -.
DR   ProtClustDB; PRK05469; -.
DR   BioCyc; ECOL405955:APECO1_209-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0045148; F:tripeptide aminopeptidase activity; IEA:EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006518; P:peptide metabolic process; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   HAMAP; MF_00550; Aminopeptidase_M20; 1; -.
DR   InterPro; IPR001261; ArgE/DapE_CS.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   InterPro; IPR010161; Peptidase_M20B.
DR   Pfam; PF07687; M20_dimer; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   PIRSF; PIRSF037215; Peptidase_M20B; 1.
DR   SUPFAM; SSF55031; Peptidase_M20_dimer; 1.
DR   TIGRFAMs; TIGR01882; Peptidase-T; 1.
DR   PROSITE; PS00758; ARGE_DAPE_CPG2_1; 1.
DR   PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1.
DR   HOGENOMDNA; ECOK1_1.PE1006; -.
KW   Aminopeptidase; Complete proteome; Cytoplasm; Hydrolase;
KW   Metal-binding; Metalloprotease; Protease; Zinc.
SQ   SEQUENCE   408 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MDKLLERFLN YVSLDTQSKA GVRQVPSTEG QWKLLHLLKE QLEEMGLINV TLSEKGTLMA
     TLPANVPGDI PAIGFISHVD TSPDCSGKNV NPQIVENYRG GDIALGIGDE VLSPVMFPVL
     HQLLGQTLIT TDGKTLLGAD DKAGIAEIMT ALAVLQQKNI PHGDIRVAFT PDEEVGKGAK
     HFDVDAFDAR WAYTVDGGGV GELEFENFNA ASVNIKIVGN NVHPGTAKGV MVNALSLAAR
     IHAEVPADES PEMTEGYEGF YHLASMKGTV ERADMHYIIR DFDRKQFEAR KRKMMEIAKK
     VGKGLHPDCY IELVIEDSYY NMREKVVEHP HILDIAQQAM RDCDIEPELK PIRGGTDGAQ
     LSFMGLPCPN LFTGGYNYHG KHEFVTLEGM EKAVQVIVRI AELTAQRK
//

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