ID D4M2T9_9FIRM Unreviewed; 200 AA.
AC D4M2T9;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Peptidase E {ECO:0000313|EMBL:CBL25551.1};
DE EC=3.4.13.21 {ECO:0000313|EMBL:CBL25551.1};
GN ORFNames=RTO_08480 {ECO:0000313|EMBL:CBL25551.1};
OS [Ruminococcus] torques L2-14.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Mediterraneibacter.
OX NCBI_TaxID=657313 {ECO:0000313|EMBL:CBL25551.1, ECO:0000313|Proteomes:UP000008956};
RN [1] {ECO:0000313|EMBL:CBL25551.1, ECO:0000313|Proteomes:UP000008956}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L2-14 {ECO:0000313|EMBL:CBL25551.1,
RC ECO:0000313|Proteomes:UP000008956};
RG metaHIT consortium -- http://www.metahit.eu/;
RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT "The genome sequence of Ruminococcus torques L2-14.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBL25551.1, ECO:0000313|Proteomes:UP000008956}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L2-14 {ECO:0000313|EMBL:CBL25551.1,
RC ECO:0000313|Proteomes:UP000008956};
RA Pajon A.;
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S51 family.
CC {ECO:0000256|ARBA:ARBA00006534}.
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DR EMBL; FP929055; CBL25551.1; -; Genomic_DNA.
DR AlphaFoldDB; D4M2T9; -.
DR STRING; 33039.ERS852502_02765; -.
DR KEGG; rto:RTO_08480; -.
DR PATRIC; fig|657313.3.peg.526; -.
DR HOGENOM; CLU_090997_0_0_9; -.
DR Proteomes; UP000008956; 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; cd03129; GAT1_Peptidase_E_like; 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:CBL25551.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CBL25551.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
SQ SEQUENCE 200 AA; 22293 MW; E31C9403BDAD7AC1 CRC64;
MKLFLCSHFS SVGSLIKEEI ENKKVAFIPT ASLREGYTGY VGSARKLFKK LGAIVTEIDI
STEAYSTIQF VFEDADVIYF TGGNSFFLID QLRKTGTDEL LKKELAKGKL MIGESAGAII
CAPSIQYIEQ MDEKPEDYSQ EDDAGLDLLD FYVLPHYLTA PFKKVTEKIM TEFSDLNLCP
INNRQGIVID GEGSKVICKD
//
