PPK1_CAMJE
ID PPK1_CAMJE Reviewed; 694 AA.
AC Q9PMU0; Q0P8Q0;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 102.
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=Cj1359;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
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; AL111168; CAL35471.1; -; Genomic_DNA.
DR PIR; D81280; D81280.
DR RefSeq; WP_002860421.1; NC_002163.1.
DR RefSeq; YP_002344747.1; NC_002163.1.
DR AlphaFoldDB; Q9PMU0; -.
DR SMR; Q9PMU0; -.
DR IntAct; Q9PMU0; 3.
DR STRING; 192222.Cj1359; -.
DR PaxDb; Q9PMU0; -.
DR PRIDE; Q9PMU0; -.
DR EnsemblBacteria; CAL35471; CAL35471; Cj1359.
DR GeneID; 905652; -.
DR KEGG; cje:Cj1359; -.
DR PATRIC; fig|192222.6.peg.1341; -.
DR eggNOG; COG0855; Bacteria.
DR HOGENOM; CLU_009678_1_1_7; -.
DR OMA; NIKWARK; -.
DR Proteomes; UP000000799; 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..694
FT /note="Polyphosphate kinase"
FT /id="PRO_0000128637"
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
