ID Q2L2L0_BORA1 Unreviewed; 235 AA.
AC Q2L2L0;
DT 07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 07-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE SubName: Full=Peptidase E {ECO:0000313|EMBL:CAJ49015.1};
DE EC=3.4.13.21 {ECO:0000313|EMBL:CAJ49015.1};
GN Name=pepE {ECO:0000313|EMBL:CAJ49015.1};
GN OrderedLocusNames=BAV1406 {ECO:0000313|EMBL:CAJ49015.1};
OS Bordetella avium (strain 197N).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=360910 {ECO:0000313|EMBL:CAJ49015.1, ECO:0000313|Proteomes:UP000001977};
RN [1] {ECO:0000313|EMBL:CAJ49015.1, ECO:0000313|Proteomes:UP000001977}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=197N {ECO:0000313|EMBL:CAJ49015.1,
RC ECO:0000313|Proteomes:UP000001977};
RX PubMed=16885469; DOI=10.1128/JB.01927-05;
RA Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D.,
RA Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A.,
RA Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J.,
RA Parkhill J., Temple L.M.;
RT "Comparison of the genome sequence of the poultry pathogen Bordetella avium
RT with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals
RT extensive diversity in surface structures associated with host
RT interaction.";
RL J. Bacteriol. 188:6002-6015(2006).
CC -!- SIMILARITY: Belongs to the peptidase S51 family.
CC {ECO:0000256|ARBA:ARBA00006534}.
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DR EMBL; AM167904; CAJ49015.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2L2L0; -.
DR STRING; 360910.BAV1406; -.
DR MEROPS; S51.001; -.
DR KEGG; bav:BAV1406; -.
DR eggNOG; COG3340; Bacteria.
DR HOGENOM; CLU_071689_0_0_4; -.
DR Proteomes; UP000001977; 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:SF0; ALPHA-ASPARTYL DIPEPTIDASE-RELATED; 1.
DR PANTHER; PTHR20842; PROTEASE S51 ALPHA-ASPARTYL DIPEPTIDASE; 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:CAJ49015.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CAJ49015.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000001977};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
SQ SEQUENCE 235 AA; 24905 MW; 438552259DE401DE CRC64;
MMNALLLSNS SSDAGYLTHA QPWLAEFTTM LTGDGPALFV PFAGVGRSWD DYTQQVADAL
LPAGIAIRGL HHEADPACAL AEARLIIVGG GNTFHLLREL RRRGLLSLIA ERVRAGQAGY
VGWSAGANIA GPTLCTTNDM PIVDPGGFDA LGLVPFQINP HYTKAHPAGH RGETRDQRLA
EFCAVQPERQ VVALPEGDAL RVDGRGLALL GAHDAYLFQG ASAPRVLTPG RIALV
//
