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Database: UniProt
Entry: D7BQD7_STRBB
LinkDB: D7BQD7_STRBB
Original site: D7BQD7_STRBB 
ID   D7BQD7_STRBB            Unreviewed;       467 AA.
AC   D7BQD7;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   SubName: Full=Peptidase {ECO:0000313|EMBL:ADI07166.1};
GN   OrderedLocusNames=SBI_04045 {ECO:0000313|EMBL:ADI07166.1};
OS   Streptomyces bingchenggensis (strain BCW-1).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=749414 {ECO:0000313|EMBL:ADI07166.1, ECO:0000313|Proteomes:UP000000377};
RN   [1] {ECO:0000313|EMBL:ADI07166.1, ECO:0000313|Proteomes:UP000000377}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BCW-1 {ECO:0000313|EMBL:ADI07166.1,
RC   ECO:0000313|Proteomes:UP000000377};
RX   PubMed=20581206; DOI=10.1128/JB.00596-10;
RA   Wang X.J., Yan Y.J., Zhang B., An J., Wang J.J., Tian J., Jiang L.,
RA   Chen Y.H., Huang S.X., Yin M., Zhang J., Gao A.L., Liu C.X., Zhu Z.X.,
RA   Xiang W.S.;
RT   "Genome sequence of the milbemycin-producing bacterium Streptomyces
RT   bingchenggensis.";
RL   J. Bacteriol. 192:4526-4527(2010).
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00520}.
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DR   EMBL; CP002047; ADI07166.1; -; Genomic_DNA.
DR   RefSeq; WP_014176639.1; NC_016582.1.
DR   AlphaFoldDB; D7BQD7; -.
DR   STRING; 749414.SBI_04045; -.
DR   KEGG; sbh:SBI_04045; -.
DR   PATRIC; fig|749414.3.peg.4183; -.
DR   eggNOG; COG0624; Bacteria.
DR   HOGENOM; CLU_029469_2_1_11; -.
DR   Proteomes; UP000000377; 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; IPR001792; Acylphosphatase-like_dom.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   PANTHER; PTHR43270; BETA-ALA-HIS DIPEPTIDASE; 1.
DR   PANTHER; PTHR43270:SF12; SUCCINYL-DIAMINOPIMELATE DESUCCINYLASE; 1.
DR   Pfam; PF07687; M20_dimer; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR   PROSITE; PS51160; ACYLPHOSPHATASE_3; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000000377}.
FT   DOMAIN          1..65
FT                   /note="Acylphosphatase-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51160"
SQ   SEQUENCE   467 AA;  50202 MW;  9669DB625C73C8A0 CRC64;
     MSNTPDTDIA VRAYVEAHRA AFLDDLAEWL RIPSVSADPA RADDVRRSAE WLAASLTATG
     FPVVETWPTA GAPAVFAEWP SDDPDAPTVL VYGHHDVQPA AREDGWHTEP FEPTVKDGRL
     YARGAADDKG QVFFHTLGVR AHLAATGRTA PAVNLKLIVE GEEESGSPHF AELIRAHADR
     LACDTVIVSD TGMWSEDTPT VCTGMRGLAD CQIDLHGPDQ DIHSGSFGGA VPNPATEAAR
     LAAALHDADR RVAIPGFYDG VVELTDRERE LFAELPFDEG AWLRSAHSHA TLGEAGHTTL
     ERIWARPTAE VNGIGGGYQG PGGKTIVPSY AQLKLSFRLV AGQDADKVEL AVREWVAARI
     PDGIRHEITF GNATRPCLTP LDHPALQSLA RAMERAFGTK IRFTREGGSG PAADLQDVLG
     APVLFLGISV PSDGWHAPNE KVELDLLLKG AETAAYLWGE LTQNRPV
//
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