ID E8N7Q6_MICTS Unreviewed; 404 AA.
AC E8N7Q6;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Metal-dependent amidase/aminoacylase/carboxypeptidase {ECO:0000313|EMBL:BAJ74312.1};
GN OrderedLocusNames=MTES_1348 {ECO:0000313|EMBL:BAJ74312.1};
OS Microbacterium testaceum (strain StLB037).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=979556 {ECO:0000313|EMBL:BAJ74312.1, ECO:0000313|Proteomes:UP000008975};
RN [1] {ECO:0000313|EMBL:BAJ74312.1, ECO:0000313|Proteomes:UP000008975}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=StLB037 {ECO:0000313|EMBL:BAJ74312.1,
RC ECO:0000313|Proteomes:UP000008975};
RX PubMed=21357489; DOI=10.1128/JB.00180-11;
RA Morohoshi T., Wang W.-Z., Someya N., Ikeda T.;
RT "Genome sequence of Microbacterium testaceum StLB037, an N-acylhomoserine
RT lactone-degrading bacterium isolated from potato leaves.";
RL J. Bacteriol. 193:2072-2073(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=StLB037;
RA Morohoshi T., Wang W.Z., Someya N., Ikeda T.;
RT "Genome sequence of Microbacterium testaceum StLB037.";
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP012052; BAJ74312.1; -; Genomic_DNA.
DR RefSeq; WP_013584437.1; NC_015125.1.
DR AlphaFoldDB; E8N7Q6; -.
DR STRING; 979556.MTES_1348; -.
DR KEGG; mts:MTES_1348; -.
DR eggNOG; COG1473; Bacteria.
DR HOGENOM; CLU_023257_6_0_11; -.
DR OrthoDB; 9777385at2; -.
DR Proteomes; UP000008975; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
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;
FT DOMAIN 185..280
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT REGION 280..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..300
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 404 AA; 43137 MW; 0526510AB9DAF3E9 CRC64;
MSVDLENLYI DLHAHPELSF QETRTAGVIA RHLTELGLEF EEGVGRTGIV TRIDNGDGPV
VWLRADTDGL PVEEQTGLAY ASTARGTDPA GNAVPVMHAC GHDMHITAMI GALERLVATT
DEWSGTVIAV FQPAEEYGAG ARAMLDDGIL DRYPKPDIVL GQHVTPLPAG TIGVRPGTQM
AASDGLTVVL HGRGGHGSRP HSTIDPVVMA AATVMRLQTI VSREVDPRDV AVVTVGSIHA
GLKNNIIPAE AKLELSLRYP DDAARDRVLE KVERIVRAEA QASGAEQTPT ITTDHTLPPT
INDPDATARL TAAFRRAFGE TSVVDPGMFT GSEDVSWFAR DAGVPLVYWF WGGVDPQAFA
DALAGGTIER DIPTNHSPFF APVMQPTIDR GVENLVVAAR EFLG
//
