ID   PPK1_CAMJJ              Reviewed;         694 AA.
AC   A1W0X7;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 80.
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};
GN   OrderedLocusNames=CJJ81176_1361;
OS   Campylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=354242;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=81-176;
RA   Fouts D.E., Nelson K.E., Sebastian Y.;
RL   Submitted (DEC-2006) 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; CP000538; EAQ72926.1; -; Genomic_DNA.
DR   RefSeq; WP_002860421.1; NC_008787.1.
DR   AlphaFoldDB; A1W0X7; -.
DR   SMR; A1W0X7; -.
DR   STRING; 354242.CJJ81176_1361; -.
DR   EnsemblBacteria; EAQ72926; EAQ72926; CJJ81176_1361.
DR   KEGG; cjj:CJJ81176_1361; -.
DR   eggNOG; COG0855; Bacteria.
DR   HOGENOM; CLU_009678_1_1_7; -.
DR   OMA; NIKWARK; -.
DR   BRENDA; 2.7.4.1; 1087.
DR   Proteomes; UP000000646; 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; Transferase.
FT   CHAIN           1..694
FT                   /note="Polyphosphate kinase"
FT                   /id="PRO_1000079361"
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;  80460 MW;  8B5C1A762FDB8A74 CRC64;
     MQTSPDMFIN RELSWLRFNS RVLDQCSKNL PLLEKLKFIA IYCTNLDEFY MIRVAGLKQL
     FSAGVNASSS DEMTPLQQLK AIRKYLHQEK ELLERYFNEI TSELEKENLF IKHYENLDEN
     LKQKCDEYFF SNIFPVIVPI AVDATHPFPH LNNLSFSLAV KICDKAHPEL VKFGMIRIPR
     VLPRFYEVSA NIYVPIESIV HQHAEEIFPG YKLLASAAFR VTRNADMVIE EEEADDFMMI
     LEQGLKLRRK GAFVRLQIQK DADEQIVEFL NTHMKIFHKD VYEYSILLNL PSLWQIAGNK
     TFTHLLSPLY TPKTLPPFDE NLSIFDAVEK EDILIIQPFE SFDPVYKFIK EASKDPEVIS
     IRMTLYRVEK NSNIVQALID AASDGKQVTV MVELKARFDE ENNLHWAKAL ENAGAHVIYG
     ITGFKVHAKV SQVIRKQGDK LKFYMHLSTG NYNASSAKIY TDVSYFTSKA EFARDTTSFF
     HILSGFSKNR RLQTLSMSPN QIKEKVLEMI RIETSKKNEG VIVAKMNSLV DSDIIQALYE
     ASMEGVQIDL IIRGICCLKP DEEYSKNIRV RSIIGKYLEH ARVFYFKHSE PNYFISSADW
     MPRNLERRLE LMTPIYDERS KAKLAQFLRL QLSDNVLAYE LKNNGEYEKI PSSEKIIDSQ
     QTLEEYVSKI YKTLKKDTDQ SRATHLASKL FKEN