ID   E2SJE2_9FIRM            Unreviewed;       469 AA.
AC   E2SJE2;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=Putative dipeptidase {ECO:0000313|EMBL:EFP62466.1};
DE            EC=3.4.13.- {ECO:0000313|EMBL:EFP62466.1};
GN   ORFNames=HMPREF0983_01147 {ECO:0000313|EMBL:EFP62466.1};
OS   Erysipelotrichaceae bacterium 3_1_53.
OC   Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC   Erysipelotrichaceae.
OX   NCBI_TaxID=658659 {ECO:0000313|EMBL:EFP62466.1, ECO:0000313|Proteomes:UP000006223};
RN   [1] {ECO:0000313|EMBL:EFP62466.1, ECO:0000313|Proteomes:UP000006223}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3_1_53 {ECO:0000313|EMBL:EFP62466.1,
RC   ECO:0000313|Proteomes:UP000006223};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ward D., Earl A., Feldgarden M., Young S.K., Pearson M., Zeng Q.,
RA   Alvarado L., Berlin A., Bochicchio J., Chapman S.B., Chen Z., Freedman E.,
RA   Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D.,
RA   Howarth C., Jen D., Larson L., Mehta T., Neiman D., Park D., Roberts A.,
RA   Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T.,
RA   Walk T., White J., Yandava C., Allen-Vercoe E., Strauss J., Sibley C.,
RA   Daigneault M., Haas B., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Erysipelotrichaceae bacterium strain 3_1_53.";
RL   Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EFP62466.1}.
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DR   EMBL; ACTJ01000027; EFP62466.1; -; Genomic_DNA.
DR   AlphaFoldDB; E2SJE2; -.
DR   STRING; 658659.HMPREF0983_01147; -.
DR   eggNOG; COG0624; Bacteria.
DR   HOGENOM; CLU_031786_2_0_9; -.
DR   BioCyc; EBAC658659-HMP:GMFE-1158-MONOMER; -.
DR   Proteomes; UP000006223; Unassembled WGS sequence.
DR   GO; GO:0016805; F:dipeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   Gene3D; 3.30.70.360; -; 2.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR   InterPro; IPR010964; M20A_pepV-rel.
DR   InterPro; IPR002933; Peptidase_M20.
DR   NCBIfam; TIGR01887; dipeptidaselike; 1.
DR   PANTHER; PTHR43808; ACETYLORNITHINE DEACETYLASE; 1.
DR   PANTHER; PTHR43808:SF33; DIPEPTIDASE SAOUHSC_01868-RELATED; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   4: Predicted;
KW   Dipeptidase {ECO:0000256|ARBA:ARBA00022997, ECO:0000313|EMBL:EFP62466.1};
KW   Hydrolase {ECO:0000313|EMBL:EFP62466.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Protease {ECO:0000256|ARBA:ARBA00022997, ECO:0000313|EMBL:EFP62466.1}.
SQ   SEQUENCE   469 AA;  51931 MW;  0B6F35E1CA2F1077 CRC64;
     MHEVNRMNWL TELETYKDAF IQDLRGLIAI PSVRDDKTKA ANAPFGAGCR KALDYMLELG
     KREGFQIKDY DGYAGVIAYG EGEESVGVLA HLDIVPIGEG WSRDPFGGEI VDGYMFGRGT
     LDDKGPAMAG FYALKMLKDK GIRLNRKVML ILGCDEESGM ECMEYYKQHG EIPTLGFTPD
     ADFPVIYGEK GGLHVEMSGS CDTVITSMHA GERSNIVIGQ ASAQVKDWKD EYLDAFLFYL
     RAFGLKGSVE TIDENMATLH MEGVFAHAAM PYNGVNAALH LLNFIGCTYG DKFAHDTYAM
     LKDWQGKPLG IDMDGAYMGF LTMNTGIVNI ENNVASITID IRYPNDADPE CIMQGFHETA
     KALDYPLDIQ MKKNTKPLFV DPKSELVQTL SGVYQDYTKD TFTPNMTIGG GTYAKKFENF
     VAFGPELPNR KQPEHLFIGG CHQKDEAILV DDLMRAVAIY TAAAEQLAK
//