PPK1_CAMHC
ID PPK1_CAMHC Reviewed; 696 AA.
AC A7I3Z5;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 72.
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=CHAB381_1724;
OS Campylobacter hominis (strain ATCC BAA-381 / LMG 19568 / NCTC 13146 /
OS CH001A).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=360107;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-381 / LMG 19568 / NCTC 13146 / CH001A;
RA Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G.,
RA Mandrell R.E., Nelson K.E.;
RT "Complete genome sequence of Campylobacter hominis ATCC BAA-381, a
RT commensal isolated from the human gastrointestinal tract.";
RL Submitted (JUL-2007) 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; CP000776; ABS51664.1; -; Genomic_DNA.
DR RefSeq; WP_012109543.1; NC_009714.1.
DR AlphaFoldDB; A7I3Z5; -.
DR SMR; A7I3Z5; -.
DR STRING; 360107.CHAB381_1724; -.
DR EnsemblBacteria; ABS51664; ABS51664; CHAB381_1724.
DR KEGG; cha:CHAB381_1724; -.
DR eggNOG; COG0855; Bacteria.
DR HOGENOM; CLU_009678_1_1_7; -.
DR OMA; NIKWARK; -.
DR OrthoDB; 76567at2; -.
DR Proteomes; UP000002407; 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..696
FT /note="Polyphosphate kinase"
FT /id="PRO_1000079358"
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 581
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
SQ SEQUENCE 696 AA; 80340 MW; 028BA7CCA08EA930 CRC64;
MSENTNIFIN RELSWLKFNS RVLEQCKKDI PLLEKLKFLA IYCTNLDEFY MIRVAGLKQL
FTAGIVVSGN DEMTPLDQLR EIRAYLQNEK NELENEYFKI KNELANKGLF IKNYNELDEE
LSAKADEFFF TQIMPIIIPI AVDSTRPFPH LNNLSFALAV KLREENNPES VHFGMIRISR
VLPRFVKVAN DTYVPISSIV GRHAEEIFPG YKLISSAAFR VTRNADIVIE EEEADDFMII
LEEGLKLRRR GAFVRLQVQK DADPEILEFL NAHLKIFYKD VYEYSIPITL DGLWEITSNK
DFINLAYPPY APKTLPPFDE NVSIFSTMDK ENILIYHPYE SFDPVEKLIK EAAKDPKVIS
IRMTLYRVEK NSPIVQALID AANDGKQVTA MVELKARFDE ENNLHWAKAL EQAGAHVIYG
ITGFKVHAKI TQIIKKDAGK LKFYMHLGTG NYNGSSAKIY TDVSFFTTDE MFEKDTTNFF
HILSGYNKNR KLDKLSMSPM QIKERLLEMI MMETEYGEEG RIVAKMNALV DSDMVKALCK
ASAAGVKIDL IVRGICCLRP GIKGVSENIR VISIVGKYLE HARIFYFKHN NPGFYISSAD
WMPRNLERRL ELMTPIYDEN LQNKLKEILK LQIKDNNLAF ELKNSGSYEK VEVPDGCEKI
NNHEYLENYY NKLYKNIQKH RDDHISMIAT KLLKES
