ID   PPK1_STRGR              Reviewed;         703 AA.
AC   Q9EUS8;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Polyphosphate kinase {ECO:0000255|HAMAP-Rule:MF_00347};
DE            EC=2.7.4.1 {ECO:0000255|HAMAP-Rule:MF_00347};
DE   AltName: Full=ATP-polyphosphate phosphotransferase {ECO:0000255|HAMAP-Rule:MF_00347};
DE   AltName: Full=Polyphosphoric acid kinase {ECO:0000255|HAMAP-Rule:MF_00347};
DE   Flags: Fragment;
GN   Name=ppk {ECO:0000255|HAMAP-Rule:MF_00347};
OS   Streptomyces griseus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1911;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DSM 40695 / ETH 7796 / Tue 10;
RA   Siekmoeller J., Fuechtenbusch B., Wittchen K.D., Kranz C., Pape H.;
RT   "Characterization of a membrane protein participating in the in-vitro
RT   formation of macrotetrolides from nonactinic acid and genes coding for a
RT   putative phosphate uptake system from Streptomyces griseus.";
RL   Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the reversible transfer of the terminal phosphate
CC       of ATP to form a long-chain polyphosphate (polyP). {ECO:0000255|HAMAP-
CC       Rule:MF_00347}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[phosphate](n) + ATP = [phosphate](n+1) + ADP;
CC         Xref=Rhea:RHEA:19573, Rhea:RHEA-COMP:9859, Rhea:RHEA-COMP:14280,
CC         ChEBI:CHEBI:16838, ChEBI:CHEBI:30616, ChEBI:CHEBI:456216; EC=2.7.4.1;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00347};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00347};
CC   -!- PTM: An intermediate of this reaction is the autophosphorylated ppk in
CC       which a phosphate is covalently linked to a histidine residue through a
CC       N-P bond. {ECO:0000255|HAMAP-Rule:MF_00347}.
CC   -!- SIMILARITY: Belongs to the polyphosphate kinase 1 (PPK1) family.
CC       {ECO:0000255|HAMAP-Rule:MF_00347}.
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DR   EMBL; AJ243674; CAC21099.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9EUS8; -.
DR   SMR; Q9EUS8; -.
DR   STRING; 1911.GCA_001715295_02629; -.
DR   PRIDE; Q9EUS8; -.
DR   GO; GO:0009358; C:polyphosphate kinase complex; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008976; F:polyphosphate kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0006799; P:polyphosphate biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.30.1840.10; -; 1.
DR   HAMAP; MF_00347; Polyphosphate_kinase; 1.
DR   InterPro; IPR003414; PP_kinase.
DR   InterPro; IPR041108; PP_kinase_C_1.
DR   InterPro; IPR024953; PP_kinase_middle.
DR   InterPro; IPR036830; PP_kinase_middle_dom_sf.
DR   InterPro; IPR025200; PPK_C_dom2.
DR   InterPro; IPR025198; PPK_N_dom.
DR   InterPro; IPR036832; PPK_N_dom_sf.
DR   PANTHER; PTHR30218; PTHR30218; 1.
DR   Pfam; PF02503; PP_kinase; 1.
DR   Pfam; PF13090; PP_kinase_C; 1.
DR   Pfam; PF17941; PP_kinase_C_1; 1.
DR   Pfam; PF13089; PP_kinase_N; 1.
DR   PIRSF; PIRSF015589; PP_kinase; 1.
DR   SUPFAM; SSF140356; SSF140356; 1.
DR   TIGRFAMs; TIGR03705; poly_P_kin; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW   Phosphoprotein; Transferase.
FT   CHAIN           <1..703
FT                   /note="Polyphosphate kinase"
FT                   /id="PRO_0000128662"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        449
FT                   /note="Phosphohistidine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT   BINDING         62
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT   BINDING         389
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT   BINDING         419
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT   BINDING         482
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT   BINDING         578
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT   BINDING         605
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT   NON_TER         1
SQ   SEQUENCE   703 AA;  79294 MW;  9D90F30C98D1B85A CRC64;
     IRSGRDADAY EPDRDGDELP QGRFLDRERS WLAFNERVLE LAEDPATPIL ERANFLAIFA
     SNLDEFFMVR VAGLKRRIAT GVATRSASGL QPREVLDLIW TRSRELMARH AACYQQDIAP
     DLSDEGIQLI RWPDLTEKEQ ARLFTFFRQR VFPVLTPLAV DPAHPFPYIS GLSLNLAVVV
     RNPVSGHRHF ARVKVPPLLT RFLEASPQRY VPIEDIIAAH LEELFPGMEV LAHHMFRVTR
     NEDLEVEEDD AENLLQALEK ELMRRRFGPP VRLEVEESID PYVLDLLVRE LKVSDAEVYP
     LPGPLELTGL FAIASLDRPE LKFPKFIAGT HRDLAEVESA SAPDIFAALR ERDVLLHHPY
     DSFSTSVQAF LEQAAGDPDV LAIKQTLYRT SGDSPIVDAL IDAAESGKQV LVLVEIKARF
     DEQANIKWAR KLEEAGCHVV YGLVGLKTHC KLSLVVRQEG DTLRRYSHVG TGNYHPKTAR
     LYEDLGLLTG DPQVGADLSD LFNRLSGYSR RETYRRLLVA PKSLRDGLIA RINKEIAHHR
     AGRPAYVRFK VNSMVDEAII DACCRAAQAG VPVDIWVRGI CAIRPASRLS ENIRVRSILG
     RFLEHSRVFS FGNGGEPEVW FGSADMMHRN LDRRIEALVR VTDPAHRAAL SRLLETGMAD
     TTASWHLGPD GNWTRHATDA DGQPLRHVQE MLIEARRRRR ATP