PPK1_STRCO
ID PPK1_STRCO Reviewed; 746 AA.
AC Q9KZV6;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 03-AUG-2022, entry version 118.
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};
GN Name=ppk {ECO:0000255|HAMAP-Rule:MF_00347}; OrderedLocusNames=SCO4145;
GN ORFNames=SCD84.12c;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB88478.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AL939119; CAB88478.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_628322.1; NC_003888.3.
DR RefSeq; WP_011029463.1; NC_003888.3.
DR AlphaFoldDB; Q9KZV6; -.
DR SMR; Q9KZV6; -.
DR STRING; 100226.SCO4145; -.
DR PRIDE; Q9KZV6; -.
DR GeneID; 1099585; -.
DR KEGG; sco:SCO4145; -.
DR PATRIC; fig|100226.15.peg.4209; -.
DR eggNOG; COG0855; Bacteria.
DR HOGENOM; CLU_009678_5_0_11; -.
DR InParanoid; Q9KZV6; -.
DR PhylomeDB; Q9KZV6; -.
DR Proteomes; UP000001973; Chromosome.
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-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006799; P:polyphosphate biosynthetic process; IEA:UniProtKB-UniRule.
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; Reference proteome; Transferase.
FT CHAIN 1..746
FT /note="Polyphosphate kinase"
FT /id="PRO_0000128661"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 489
FT /note="Phosphohistidine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT BINDING 102
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT BINDING 429
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT BINDING 459
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT BINDING 522
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT BINDING 618
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT BINDING 646
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
SQ SEQUENCE 746 AA; 83486 MW; F19AD2A34D1DDE08 CRC64;
MRQPNTQAEA QHTQPSVGSI AAHRPNTVAA TVSGLEPDID ADLDAYEESE ESQDGGARLP
QGRFLDRERS WLAFNERVLE LAEDPSTPLL ERANFLAIFA SNLDEFFMVR VAGLKRRIAT
GVATRSASGL QPREVLEMIW ARSRELMARH AACFHEDVAP ALAEEGIHLV RWSELAEKEQ
ARLFTLFRHR IFPVLTPLAV DPAHPFPYIS GLSLNLAVVV RNPVTGHRHF ARVKVPPLLS
RFLEASPGRY VPVEDVIAAH LEELFPGMEV LEHHTFRLTR NEDLEVEEDD AENLLQALEK
ELMRRRLGPP VRLEVEESVD REVLDLLVRE LKIGEAEVYP LPGPLDLTGL FRIHSIDRPE
LKYPKFVAGT HRDLAEVESA SAPDIFAALR TKDVLLHHPY DSFSTSVQAF LEQAAADPDV
LAIKQTLYRT SGDSPIVDAL IEAAESGKQV LVLVEIKARF DESANIKWAR KLEESGCHVV
YGLVGLKTHC KLSLVVRQEG ETLRRYSHVG TGNYHPKTAR LYEDLGLLTS DPQVGADLSD
LFNRLSGYSR RETYRRLLVA PKSLRDGLVS RIHKEIQHHR AGRPAHVRIK VNSMVDEAVV
DACYRASQAG VPVDVWVRGI CALRPGVPGL SENIRVRSVL GRFLEHSRVF AFGNGGEPEV
WLGSADMMHR NLDRRIEALV RVTDPAHRAA LNRLLENGMS DGTASWHLGP DGEWTRHATD
ADGQPLRNIQ EMLIDARRRR RGTATP
