ID C5BCB3_EDWI9 Unreviewed; 241 AA.
AC C5BCB3;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 24-JAN-2024, entry version 81.
DE SubName: Full=Peptidase E, putative {ECO:0000313|EMBL:ACR67404.1};
DE EC=3.4.13.21 {ECO:0000313|EMBL:ACR67404.1};
GN OrderedLocusNames=NT01EI_0149 {ECO:0000313|EMBL:ACR67404.1};
OS Edwardsiella ictaluri (strain 93-146).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Hafniaceae; Edwardsiella.
OX NCBI_TaxID=634503 {ECO:0000313|EMBL:ACR67404.1, ECO:0000313|Proteomes:UP000001485};
RN [1] {ECO:0000313|Proteomes:UP000001485}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=93-146 {ECO:0000313|Proteomes:UP000001485};
RA Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACR67404.1, ECO:0000313|Proteomes:UP000001485}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=93-146 {ECO:0000313|EMBL:ACR67404.1,
RC ECO:0000313|Proteomes:UP000001485};
RX PubMed=22247535; DOI=10.1128/JB.06522-11;
RA Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA Schuster S.C., Gipson J., Zaitshik J., Landry C., Banes M.M.,
RA Lawrence M.L.;
RT "Genome Sequence of Edwardsiella ictaluri 93-146, a Strain Associated with
RT a Natural Channel Catfish Outbreak of Enteric Septicemia of Catfish.";
RL J. Bacteriol. 194:740-741(2012).
CC -!- SIMILARITY: Belongs to the peptidase S51 family.
CC {ECO:0000256|ARBA:ARBA00006534}.
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DR EMBL; CP001600; ACR67404.1; -; Genomic_DNA.
DR RefSeq; WP_015869620.1; NC_012779.2.
DR AlphaFoldDB; C5BCB3; -.
DR STRING; 67780.B6E78_11895; -.
DR GeneID; 69537256; -.
DR KEGG; eic:NT01EI_0149; -.
DR PATRIC; fig|634503.3.peg.140; -.
DR HOGENOM; CLU_071689_0_0_6; -.
DR OMA; LFIPYAR; -.
DR OrthoDB; 3373764at2; -.
DR Proteomes; UP000001485; Chromosome.
DR GO; GO:0016805; F:dipeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd03146; GAT1_Peptidase_E; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR005320; Peptidase_S51.
DR PANTHER; PTHR20842; PROTEASE S51 ALPHA-ASPARTYL DIPEPTIDASE; 1.
DR PANTHER; PTHR20842:SF0; SI:DKEY-69O16.5; 1.
DR Pfam; PF03575; Peptidase_S51; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
PE 3: Inferred from homology;
KW Dipeptidase {ECO:0000313|EMBL:ACR67404.1};
KW Hydrolase {ECO:0000313|EMBL:ACR67404.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
SQ SEQUENCE 241 AA; 26724 MW; C459918EB50D0D83 CRC64;
MELFLLSNGK VSGESELLGY AKGMIQSMLL EKKIRRALLI PYALIRSSYD ARAAELEHSL
GITVESIHHH ADPVKALEEA ECILISGGNT WVLNQMLHEN GLIVPIQRAV RERGIPYIGW
SAGCNVATPS IRTTNDMPVR NSVVLPSLGL FPVQINPHYI DAHLSGHMGE TRDERIAEFC
AVNPSESVIA LREGSLLHVS GETLQYYSAK AQGYKVFRHG EETREYHDTQ ALAALVPFHC
R
//