ID   PPK1_ACIBA              Reviewed;         692 AA.
AC   Q9X4M8;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 64.
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};
OS   Acinetobacter baumannii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=470;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=252;
RX   PubMed=10537215; DOI=10.1099/00221287-145-10-2931;
RA   Gavigan J.A., Marshall L.M., Dobson A.D.W.;
RT   "Regulation of polyphosphate kinase gene expression in Acinetobacter
RT   baumannii 252.";
RL   Microbiology 145:2931-2937(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}.
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; AF116175; AAD28429.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9X4M8; -.
DR   SMR; Q9X4M8; -.
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; Transferase.
FT   CHAIN           1..692
FT                   /note="Polyphosphate kinase"
FT                   /id="PRO_0000128631"
FT   ACT_SITE        443
FT                   /note="Phosphohistidine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT   BINDING         57
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT   BINDING         383
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT   BINDING         413
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT   BINDING         476
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT   BINDING         572
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT   BINDING         600
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
SQ   SEQUENCE   692 AA;  78980 MW;  C7EB0011DF332920 CRC64;
     MNSVVTQASP PVYGQVERYI NRELSILDFN LRVLEQAVDP LNPLLEKLNF LLIFSRNLDE
     FFEIRVATML EHFVQERDIQ TADGLSPQEI LHQISETAHA AIERQYQILN EQIFPQLREE
     GISFLRRGEL TQAQSNWVKK YFQEQVAPAL TPISLDPAHP FPRLVNKSLN FIVTLEGKDA
     FGRQIDLAVV PAPHSLPRVV RLPDELTEGK EHHVMLSSII HTHVSDSFPG MTATGCYQFR
     VTRNADLTLT EDVEDLAEAL KDELSSRRFG RAVRLEVNKN CPTHIYEYLL KEFDLDTHQL
     YRVDGPVNLA RLVSDFKRPY LRYEPHTPVI PKILKKSANI FSAMQKQDIL LHHPFESFSP
     VIRLLREAAQ DPHVLAIKQT LYRSGANSEI VQILAEAARN GKEVTAVIEL RARFDEESNI
     AVANVLQEAG AVVVYGIVGY KTHAKMILVV RRENQKLVRY AHLGTGNYHA GNAKIYTDYG
     LLTTNQDLCE DVHRIFQELT GMGKMVKLKK LLHAPFTLHS QLMNFIENEI VLAKAGKPAK
     IIIKVNALTE VQLINKLYEA SQAGVKIELI IRSICCLRPG LAGLSENIRV RSIVGRFLEH
     TRVYYFYNNG DTRVYCSSAD WMERNLFKRV EVCLPIENTG LKKRIYQQGL ENYLMDNQQS
     WLLQSDGSWC RNISTEDQKP HNAQQMLLGD II