ID   PPK1_VIBCH              Reviewed;         701 AA.
AC   Q9KU07; O86073;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 112.
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=VC_0723;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=El Tor Inaba 92A1552;
RA   Ogawa N., Fraley C., Kornberg A.;
RT   "The polyphosphate kinase and exopolyphosphatase genes of Vibrio
RT   cholerae.";
RL   Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(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; AF083928; AAC32883.1; -; Genomic_DNA.
DR   EMBL; AE003852; AAF93888.1; -; Genomic_DNA.
DR   PIR; D82289; D82289.
DR   RefSeq; NP_230372.1; NC_002505.1.
DR   RefSeq; WP_001271572.1; NZ_LT906614.1.
DR   AlphaFoldDB; Q9KU07; -.
DR   SMR; Q9KU07; -.
DR   STRING; 243277.VC_0723; -.
DR   DNASU; 2615732; -.
DR   EnsemblBacteria; AAF93888; AAF93888; VC_0723.
DR   GeneID; 57739438; -.
DR   KEGG; vch:VC_0723; -.
DR   PATRIC; fig|243277.26.peg.691; -.
DR   eggNOG; COG0855; Bacteria.
DR   HOGENOM; CLU_009678_6_1_6; -.
DR   OMA; NIKWARK; -.
DR   BioCyc; VCHO:VC0723-MON; -.
DR   Proteomes; UP000000584; Chromosome 1.
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:0019637; P:organophosphate metabolic process; IEA:UniProt.
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; IPR001736; PLipase_D/transphosphatidylase.
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.
DR   PROSITE; PS50035; PLD; 2.
PE   3: Inferred from homology;
KW   ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Repeat; Transferase.
FT   CHAIN           1..701
FT                   /note="Polyphosphate kinase"
FT                   /id="PRO_0000128666"
FT   DOMAIN          428..462
FT                   /note="PLD phosphodiesterase 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT   DOMAIN          585..615
FT                   /note="PLD phosphodiesterase 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT   ACT_SITE        433
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         373
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT   BINDING         403
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT   BINDING         466
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT   BINDING         562
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT   BINDING         590
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT   CONFLICT        130..131
FT                   /note="EV -> VM (in Ref. 1; AAC32883)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   701 AA;  81645 MW;  8BDECAEE7687C9D4 CRC64;
     MSADKLYIDK ELSWLSFNER VLQEAADKTV PLIERIRFLG IFSNNLDEFY KVRFADVKRQ
     ILINRERGGN DISKHLLSRM QSKALKLNQD FDNLYNELIL EMARRRIFLV NETQLDEIQL
     KWVKKYFHKE VLPHVTPIML RDDIDVMQFL KDEYAYIAVE MRSGDEFKYA LIEIPTDQLP
     RFVMLPEQKG KRRKTIILLD NIIRLCLDEI FRGFYDYDTL NGYAMKMTRD AEYDLRHEVE
     YSLLEQMSEG LSQRLTALPV RFVYEREMPE AMLKFLCYKL KISHYDSLIP GGRYHNFKDF
     ISFPNVGRDY LENKPLPPMT CADFEGYANA FDAIRAQDIL LHYPYHSFEH MTELVRQASF
     DPKVVSIKIN IYRVAKDSKL MNSLVDAVHN GKRVVVVVEL QARFDEEANI EWSRILTDAG
     VHVIFGVPGM KIHAKLLLIT RKEGDEFVRY AHIGTGNFHE RTARIYTDFA LLTANQELAA
     EVRAVFGYIE NPFRPVKFNH LIVSPRNSRT QIYRLLDSEI ANAKAGKKAA ITLKVNNLVD
     KGLINKLYGA SAAGVKIRMI IRGMCSLVPG VEGVSDNIEI ISIIDRFLEH PRVLVVHNDG
     NPQVFISSAD WMERNIDHRI EVMAPIRDER LKQRIIDILN IQFIDTVKAR RIDKEMSNQY
     VERGNRRKVR SQIAIYDYLK NVEKQTRKAK GQQETNDNSS Q