ID   F4V8V8_ECOLX            Unreviewed;       388 AA.
AC   F4V8V8;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   SubName: Full=Peptidase M20D, amidohydrolase {ECO:0000313|EMBL:EGI38921.1};
GN   ORFNames=ECNG_04200 {ECO:0000313|EMBL:EGI38921.1};
OS   Escherichia coli TA280.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=656444 {ECO:0000313|EMBL:EGI38921.1, ECO:0000313|Proteomes:UP000004877};
RN   [1] {ECO:0000313|EMBL:EGI38921.1, ECO:0000313|Proteomes:UP000004877}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TA280 {ECO:0000313|EMBL:EGI38921.1,
RC   ECO:0000313|Proteomes:UP000004877};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Feldgarden M., Gordon D.M., Johnson J.R., Johnston B.D., Young S., Zeng Q.,
RA   Koehrsen M., Alvarado L., Berlin A.M., Borenstein D., Chapman S.B.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA   Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA   Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA   Walk T., White J., Yandava C., Haas B., Henn M.R., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Escherichia coli TA280.";
RL   Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; GL884380; EGI38921.1; -; Genomic_DNA.
DR   AlphaFoldDB; F4V8V8; -.
DR   HOGENOM; CLU_023257_0_1_6; -.
DR   Proteomes; UP000004877; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:1901564; P:organonitrogen compound metabolic process; IEA:UniProt.
DR   CDD; cd05666; M20_Acy1-like; 1.
DR   Gene3D; 3.30.70.360; -; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR017439; Amidohydrolase.
DR   InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   NCBIfam; TIGR01891; amidohydrolases; 1.
DR   PANTHER; PTHR11014:SF63; METALLOPEPTIDASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G09600)-RELATED; 1.
DR   PANTHER; PTHR11014; PEPTIDASE M20 FAMILY MEMBER; 1.
DR   Pfam; PF07687; M20_dimer; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   PIRSF; PIRSF005962; Pept_M20D_amidohydro; 1.
DR   SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EGI38921.1}.
FT   DOMAIN          184..279
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   388 AA;  42273 MW;  88E1E329DCC61725 CRC64;
     MIEHYIRGFE EELREIRHQI HENPELGLQE FKTSALVAEK LRQWGYEVEQ GLATTGVVAT
     LKVGDGEKSI GLRADMDALP IYENSGKPWA SKHPGLMHAC GHDGHTTILL GAARYFAETR
     RFNGTLRLIF QPAEEMINGG EIMVKEGLFD RFPCDVIFGM HNMPGLPVGK FFFQPGALMA
     SMDQFHITVR GCGGHGAIPH KAIDPVLVAA HITTALQSIV SRNVDPLEAA VITVGSIVAG
     EAANVIPDSA EMKISVRSLS RDTRQLLLTR IPALAQAQAV SFGATAEVTH VNGTPVLVND
     EEMARFAWQV ARKTFGEDRA EFGIKPLMGS EDFSFMLEAQ PKGAFLLFGN GDVGEGACMV
     HNPGYDFNDA SLVPACSYWG ALVEAWLQ
//