ID   V6L5V8_9ACTN            Unreviewed;       441 AA.
AC   V6L5V8;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Peptidase M20 {ECO:0000313|EMBL:EST39747.1};
GN   ORFNames=N566_00420 {ECO:0000313|EMBL:EST39747.1};
OS   Streptomycetaceae bacterium MP113-05.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae.
OX   NCBI_TaxID=1380770 {ECO:0000313|EMBL:EST39747.1, ECO:0000313|Proteomes:UP000017915};
RN   [1] {ECO:0000313|EMBL:EST39747.1, ECO:0000313|Proteomes:UP000017915}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MP113-05 {ECO:0000313|EMBL:EST39747.1,
RC   ECO:0000313|Proteomes:UP000017915};
RA   Valde M., Degnes K.F., Sletta H., Ruckert C., Kalinowski J., Zotchev S.B.;
RT   "Streptomyces bacterium from a marine sponge: physiological
RT   characterization and genome-based analysis of secondary metabolite
RT   biosynthesis potential.";
RL   Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
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:EST39747.1}.
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; AWQV01000003; EST39747.1; -; Genomic_DNA.
DR   AlphaFoldDB; V6L5V8; -.
DR   STRING; 1380770.N566_00420; -.
DR   PATRIC; fig|1380770.3.peg.81; -.
DR   HOGENOM; CLU_021802_11_2_11; -.
DR   OrthoDB; 7055905at2; -.
DR   Proteomes; UP000017915; 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   CDD; cd05675; M20_yscS_like; 1.
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   PIRSF; PIRSF036696; ACY-1; 2.
DR   SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR   PROSITE; PS00758; ARGE_DAPE_CPG2_1; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017915};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          201..329
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   441 AA;  47901 MW;  44C14DD58D788EE0 CRC64;
     MSQSSPVPER RGEDEVVDLC RDLIRIDTSN FGGNDARGER AAAEYVASML AEVGVEPKII
     ESERGRASVV ARIEGEDSSR PGLLIHGHTD VVPANAEDWT HHPFSGEIAD GCVWGRGAVD
     MKDMDAMTLA VMRDRMRSGR RPPRDVVLAF LADEEAGGIY GARHLVDHHA DLFEGVTEAI
     GEVGGFSFTV NENLRLYLVE TAQKGMHWMR LTVDGTAGHG SMTNADNAIT ELCEAVGRLG
     RHRFPVRATK TVRSFLDELS DALGTELDPE DMEETLTKLG GIAKIIGATL QNTAAPTQLG
     AGYKVNVIPG QATAHVDGRF LPGHEEEFLA DLDRVLGPRV RREDVHADKA LETTFDGALV
     EAMQSSLRAE DPVARAVPYM LSGGTDAKSF DDLGIRCFGF APLKLPPDLD FAGMFHGVDE
     RVPVDGLQFG VRVLDRFLDQ C
//