ID D9WVF5_9ACTN Unreviewed; 448 AA.
AC D9WVF5;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Putative peptidase family M20/M25/M40 protein {ECO:0000313|EMBL:EFL22332.1};
GN ORFNames=SSOG_02044 {ECO:0000313|EMBL:EFL22332.1};
OS Streptomyces himastatinicus ATCC 53653.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces; Streptomyces violaceusniger group.
OX NCBI_TaxID=457427 {ECO:0000313|EMBL:EFL22332.1, ECO:0000313|Proteomes:UP000003963};
RN [1] {ECO:0000313|EMBL:EFL22332.1, ECO:0000313|Proteomes:UP000003963}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 53653 {ECO:0000313|EMBL:EFL22332.1,
RC ECO:0000313|Proteomes:UP000003963};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Microbial Sequencing Center;
RA Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A.M., Bochicchio J., 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 Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA Haas B., Nusbaum C., Birren B.;
RT "Annotation of Streptomyces hygroscopicus strain ATCC 53653.";
RL Submitted (FEB-2009) 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; GG657754; EFL22332.1; -; Genomic_DNA.
DR RefSeq; WP_009714153.1; NZ_GG657754.1.
DR AlphaFoldDB; D9WVF5; -.
DR STRING; 457427.SSOG_02044; -.
DR HOGENOM; CLU_021802_11_2_11; -.
DR OrthoDB; 7055905at2; -.
DR Proteomes; UP000003963; 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 SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS00758; ARGE_DAPE_CPG2_1; 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 Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 203..330
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 448 AA; 48313 MW; 4214E296FE15F30E CRC64;
MADTARPEAI DAQALEEVVR FTSELIAIDT TNRGGGECSE RPAAEYVAEM LGDVDIDPTL
LERSPGRTNV VARIEGTDRA APALLVHGHL DVVPAEPADW TVHPFSGEVR DGVVWGRGAI
DMKNMDAMVL AVVRAWARAG VRPRRDIVLA FTADEEDSAA WGSGYLADRH PELFEGCTEG
ISESGAFTFH AGPGLRLYPI AAGERGTAWL KLTARGRAGH GSKVNRANAV SRLAAAVARI
GDHRWPVRLT PTVKAALTEI AALQDIPADV DAPDFDVDEL LAKLGPAAAL IEPTVRNSAN
PTVLEAGYKI NVIPGSASAY IDGRMLPGGE DEFRETLDRL TGPDVDWEFH HREVPLQAPV
GPEAPTYEAM RAAVQRFDPG GHAVPYCMSG GTDAKQFSRL GIRGYGFSPL RLPEGFDYQA
LYHGVDERVP VDALHFGVRV LDHFLQRA
//