ID A0A160KSP0_9MICO Unreviewed; 439 AA.
AC A0A160KSP0;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Peptidase M20 dimerisation domain-containing protein {ECO:0000259|Pfam:PF07687};
GN ORFNames=A6122_1295 {ECO:0000313|EMBL:AND16439.1}, C5C18_03780
GN {ECO:0000313|EMBL:PPG08518.1};
OS Rathayibacter tritici.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Rathayibacter.
OX NCBI_TaxID=33888 {ECO:0000313|EMBL:AND16439.1, ECO:0000313|Proteomes:UP000077071};
RN [1] {ECO:0000313|EMBL:AND16439.1, ECO:0000313|Proteomes:UP000077071}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCPPB 1953 {ECO:0000313|EMBL:AND16439.1,
RC ECO:0000313|Proteomes:UP000077071};
RA Park J., Lee H.-H., Lee S.-W., Seo Y.-S.;
RT "Complete genome sequence of Rathayibacter tritici NCPPB 1953.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PPG08518.1, ECO:0000313|Proteomes:UP000239776}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GSPB 2748 {ECO:0000313|EMBL:PPG08518.1,
RC ECO:0000313|Proteomes:UP000239776};
RA Davis E.W.II., Tabima J.F., Weisberg A.J., Lopes L.D., Wiseman M.S.,
RA Wiseman M.S., Pupko T., Belcher M.S., Sechler A.J., Tancos M.A.,
RA Schroeder B.K., Murray T.D., Luster D.G., Schneider W.L., Rogers E.,
RA Andreote F.D., Grunwald N.J., Putnam M.L., Chang J.H.;
RT "Bacteriophage NCPPB3778 and a type I-E CRISPR drive the evolution of the
RT US Biological Select Agent, Rathayibacter toxicus.";
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
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DR EMBL; CP015515; AND16439.1; -; Genomic_DNA.
DR EMBL; PSUO01000004; PPG08518.1; -; Genomic_DNA.
DR RefSeq; WP_068253054.1; NZ_PSWT01000052.1.
DR AlphaFoldDB; A0A160KSP0; -.
DR STRING; 33888.A6122_1295; -.
DR KEGG; rtn:A6122_1295; -.
DR PATRIC; fig|33888.3.peg.1422; -.
DR OrthoDB; 7055905at2; -.
DR Proteomes; UP000077071; Chromosome.
DR Proteomes; UP000239776; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 1.10.150.900; -; 1.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR001261; ArgE/DapE_CS.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR PANTHER; PTHR43808; ACETYLORNITHINE DEACETYLASE; 1.
DR PANTHER; PTHR43808:SF32; CONSERVED PROTEIN; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000077071};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 199..330
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 439 AA; 46942 MW; DAD970A26F36E478 CRC64;
MPDSADVTGA TLDETALLAR DLIRFDTSNY GDGKAEPERP AAEYVAAKLR DLGLEPELID
SDPGRTSVVA RVTGEDRERG ALVVHGHLDV VPAIADNWSV DPFGGEIKDG MLWGRGAVDM
KNMDAMILAS LGDILREGRR PSRDLVIAFF ADEEAGGVRG SGYLARERPE LFAGATEAIS
EVGGYSIELA GKRAYLVQTG EKALMWLTLR AHGTAGHGSQ INATNAVTRL AQAIARIGSE
EWPTRLTDTT RELLDEVARL LGHDPQRSTP EELALATGTA SRFIAATLRT TANPSMLSAG
YKANVIPDTA EATIDVRVLP GEEDAVLERL TVLAGEHVEI LVQHRDIGLE VPFAGPLVES
MAASLRRFDP GAEVLPYLLS GGTDNKALST LGITGYGFAP LQLPSSLDFP AMFHGVDERV
PLDALVFGRK VLTDLLLSS
//
