ID   STRK_STRGR              Reviewed;         449 AA.
AC   P09401;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 2.
DT   04-NOV-2026, entry version 120.
DE   RecName: Full=Streptomycin-6-phosphate phosphatase;
DE            EC=3.1.3.39;
DE   Flags: Precursor;
GN   Name=strK;
OS   Streptomyces griseus.
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1911;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=N2-3-11;
RX   PubMed=1654502; DOI=10.1007/bf00260640;
RA   Mansouri K., Piepersberg W.;
RT   "Genetics of streptomycin production in Streptomyces griseus: nucleotide
RT   sequence of five genes, strFGHIK, including a phosphatase gene.";
RL   Mol. Gen. Genet. 228:459-469(1991).
CC   -!- FUNCTION: Specifically cleaves both streptomycin-6-phosphate and, more
CC       slowly, streptomycin-3''-phosphate during the biosynthesis of
CC       streptomycin.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=streptomycin 6-phosphate + H2O = streptomycin + phosphate;
CC         Xref=Rhea:RHEA:10688, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57787, ChEBI:CHEBI:58007; EC=3.1.3.39;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 1 Mg(2+) ion. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 2 Zn(2+) ions. {ECO:0000250};
CC   -!- PATHWAY: Antibiotic biosynthesis; streptomycin biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the alkaline phosphatase family. {ECO:0000305}.
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DR   EMBL; Y00459; CAA68522.1; -; Genomic_DNA.
DR   PIR; S17780; S17780.
DR   RefSeq; WP_003970245.1; NZ_BAABSR010000130.1.
DR   AlphaFoldDB; P09401; -.
DR   SMR; P09401; -.
DR   OMA; AAAHTMY; -.
DR   OrthoDB; 9794455at2; -.
DR   BioCyc; MetaCyc:MONOMER-14015; -.
DR   UniPathway; UPA00066; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004035; F:alkaline phosphatase activity; IEA:TreeGrafter.
DR   GO; GO:0050301; F:streptomycin-6-phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019872; P:streptomycin biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd16012; ALP; 1.
DR   Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR   InterPro; IPR001952; Alkaline_phosphatase.
DR   InterPro; IPR018299; Alkaline_phosphatase_AS.
DR   InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR   PANTHER; PTHR11596; ALKALINE PHOSPHATASE; 1.
DR   PANTHER; PTHR11596:SF5; ALKALINE PHOSPHATASE; 1.
DR   Pfam; PF00245; Alk_phosphatase; 1.
DR   PRINTS; PR00113; ALKPHPHTASE.
DR   SMART; SM00098; alkPPc; 1.
DR   SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
DR   PROSITE; PS00123; ALKALINE_PHOSPHATASE; 1.
PE   3: Inferred from homology;
KW   Antibiotic biosynthesis; Hydrolase; Magnesium; Metal-binding;
KW   Phosphoprotein; Secreted; Signal; Streptomycin biosynthesis; Zinc.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000255"
FT   CHAIN           33..449
FT                   /note="Streptomycin-6-phosphate phosphatase"
FT                   /id="PRO_0000024016"
FT   REGION          268..290
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        99
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10042"
FT   BINDING         50
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         50
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         151
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         153
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         321
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         326
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         330
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         368
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         369
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         412
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   449 AA;  46343 MW;  2B7BC9393F9686E8 CRC64;
     MRFAYGRLPW RRGAVLGSAL LVLVTAPAAS TATERSGPAP ARSVILLIGD GMGDAEITAA
     RNYSVGAAGR LAMDTLDASG RRTTYAVDER GRPVYVTDSA AGATAWATGR RTVNGRVSKS
     HDTDRPMPTL LELARDRGYA TGSVTTASVA DATPAALTAH VTDRSCKGPA DMAACPADTR
     AGGGEGSIAE QTVAARPDVL LGGGADHFAQ TVTDGPFRGR TVTQQARAAG YQVVRDRTQL
     AAARPGRPVL GLFAPEYVPV EWTGPPAAPG GTAPQRCATR NPGRPAGTPD LAESTRAALD
     LLTARAHHRG APGRGFFLQV EGASIDDRAH EADPCGQLGE TLAFDRAVAA ALDHAERHPR
     TLVIVTADHG HATQILPHDA RPAGLSATLV TDEGGVMQLG YGTALPGETQ EHTGVPVPVA
     ARGPLADRVR GVQDNTSLFG TVTAALGLR
//