ID   PPK1_CAMCO              Reviewed;         694 AA.
AC   O32350;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 79.
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   Campylobacter coli.
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=195;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Richardson P.T., Park S.F.;
RT   "Molecular characterisation of the polyphosphate kinase gene from
RT   Campylobacter coli.";
RL   Submitted (AUG-1996) 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; Y07620; CAA68899.1; -; Genomic_DNA.
DR   AlphaFoldDB; O32350; -.
DR   SMR; O32350; -.
DR   STRING; 1367491.BN865_07790c; -.
DR   eggNOG; COG0855; Bacteria.
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..694
FT                   /note="Polyphosphate kinase"
FT                   /id="PRO_0000128636"
FT   ACT_SITE        427
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         367
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT   BINDING         397
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT   BINDING         460
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT   BINDING         553
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT   BINDING         580
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
SQ   SEQUENCE   694 AA;  80114 MW;  D25A3A0B16827375 CRC64;
     MQTNPNMFLN RELSWLRFNS RVLDQCSRPL PLLERLKFVA IYCTNLDEFY MIRVAGLKQL
     FSAGVNISSS DEMSPLQQLK AIRKYLHKEK DLLEHYFNEI ISDLEKENLF IKNYENLDNN
     LKQKVYEYFF STIFPVIVPI AVDATHPFPH LNNLSFSLAV NICDNTHPEL IKFGMIRIPR
     VLPRFYEVSA NVYVPIESIV EKHTEEIFPG YKLLTSAAFR VTRNADMVIE EEEADDFMMI
     LEQGLKLRRK GAFVRLQIQK GADEQIVEFL NTHMKIFHKD VYEYSILLNL PSLWQIAGNK
     TFTHLLSPLY TPKTLPPFDE NLSIFDAIDK EDILIIQPFE SFDPVYKFIK EASKDPEVIS
     IRMTLYRVEK NSNIVQALIG AASAGIQVTV MVELKARFDE ENNLHWAKAL ENAGAHVIYG
     ITGFKVHAKV SQVIRKKGDK LKFYMHLSTG NYNASSAKIY TDVSYFTSKV EFARDTTSFF
     HILSGFSKNR RLQTLSMSPN QIKEKILEMI ALEASKGSEG VIIAKMNSLV DSDIIKALYE
     ASIKGTQIDL IVRGIFCLKP NEEFSKNILV RSIIGKYLEH ARVFYFKHSE PNYFISSADW
     MPRNLERRLE LMTPIYDERS KAKLAQFLRL QLSDNLLAYE LQNDGEYAKV ASNEKVIDSQ
     QILEEYVSKI YKTLKKDTDQ SRATHLASKL FKEN