ID   PPK1_PSEAI              Reviewed;         690 AA.
AC   P0DP45; O24816; Q9S646;
DT   07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2017, sequence version 1.
DT   03-AUG-2022, entry version 17.
DE   RecName: Full=Polyphosphate kinase {ECO:0000255|HAMAP-Rule:MF_00347, ECO:0000303|PubMed:10224002};
DE            EC=2.7.4.1 {ECO:0000255|HAMAP-Rule:MF_00347, ECO:0000269|PubMed:10224002};
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, ECO:0000303|PubMed:10224002};
OS   Pseudomonas aeruginosa.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=8830;
RX   PubMed=10224002; DOI=10.1128/aem.65.5.2065-2071.1999;
RA   Zago A., Chugani S., Chakrabarty A.M.;
RT   "Cloning and characterization of polyphosphate kinase and
RT   exopolyphosphatase genes from Pseudomonas aeruginosa 8830.";
RL   Appl. Environ. Microbiol. 65:2065-2071(1999).
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, ECO:0000269|PubMed:10224002}.
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         ECO:0000269|PubMed:10224002};
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; AF087931; AAD29112.1; -; Genomic_DNA.
DR   AlphaFoldDB; P0DP45; -.
DR   SMR; P0DP45; -.
DR   eggNOG; COG0855; Bacteria.
DR   BRENDA; 2.7.4.1; 5087.
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   1: Evidence at protein level;
KW   ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW   Phosphoprotein; Transferase.
FT   CHAIN           1..690
FT                   /note="Polyphosphate kinase"
FT                   /id="PRO_0000440098"
FT   ACT_SITE        435
FT                   /note="Phosphohistidine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT   BINDING         45
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT   BINDING         375
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT   BINDING         405
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT   BINDING         468
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT   BINDING         564
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT   BINDING         592
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
SQ   SEQUENCE   690 AA;  78293 MW;  7F215EDD7F35742E CRC64;
     MDDSSLYIHR ELSQLQFNIR VLEQALDESY PLLERLKFLL IFSSNLDEFF EIRIAGLKKQ
     ITFAREQAGA DGLLPHQALA RISELVHEQV SRQYRILNET LLPELAKHQI RFIRRRHWTL
     KIKTWVRRFF RDEIAPIITP IGLDPTHPFP LLVNKSLNFI VELEGMDAFG RDSGLAIIPA
     PRLLPRIIRL PEDVGGEGDN YVFLSSMIHA HADDLFPGMK VKGCYQFRLT RNADLSVDTE
     DVEDLARALR GELFSRRYGD AVRLEVVDTC PQNLTNYLLK QFGLSESELY KVSGPVNLTR
     LFSVTGLESH PELQYPPFTP AIPRLLQKKE NLFNVLSKLD VLLMHPFESF TPVIDLLRQA
     AKDPNVLAIK QTLYRSGANS EIVDALVEAA RNGKEVTAVI ELRARFDEES NLQLASRLQQ
     AGAVVIYGVV GFKTHAKMML ILRREDGELR RYAHLGTGNY HAGNARLYTD YSLLTADVAL
     CEDLHKLFNQ LIGMGKTLRM KKLLHAPFTL KKNLLEMINR EAAQAALGQP AHIMAKVNSL
     TDPKVIRALY KASQAGVRID LVVRGMCCLR PGIPGVSHNI HVRSIIGRFL EHSRIYYFLN
     GGDEKLYLSS ADWMERNLDM RVETCFPVEG KKLVQRVKKE LETYLTDNTQ AWVLQADGSY
     QRLSPTGNQN PRNTQATLLE KLAAPVLTAR