PPK1_VIBPA
ID PPK1_VIBPA Reviewed; 696 AA.
AC Q87S51;
DT 30-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2003, sequence version 1.
DT 03-AUG-2022, entry version 96.
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=VP0573;
OS Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=223926;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIMD 2210633;
RX PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT distinct from that of V. cholerae.";
RL Lancet 361:743-749(2003).
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; BA000031; BAC58836.1; -; Genomic_DNA.
DR RefSeq; NP_796952.1; NC_004603.1.
DR RefSeq; WP_005460183.1; NC_004603.1.
DR AlphaFoldDB; Q87S51; -.
DR SMR; Q87S51; -.
DR STRING; 223926.28805556; -.
DR EnsemblBacteria; BAC58836; BAC58836; BAC58836.
DR GeneID; 1188048; -.
DR KEGG; vpa:VP0573; -.
DR PATRIC; fig|223926.6.peg.544; -.
DR eggNOG; COG0855; Bacteria.
DR HOGENOM; CLU_009678_6_1_6; -.
DR OMA; NIKWARK; -.
DR Proteomes; UP000002493; 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; 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_0000128667"
FT DOMAIN 428..462
FT /note="PLD phosphodiesterase"
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"
SQ SEQUENCE 696 AA; 81060 MW; E1FEF3B28337EEEA CRC64;
MSAEKLYIEK ELSWLSFNER VLQEAADKTV PLIERIRFLG IFSNNLDEFY KVRFADVKRR
ILINQERGGS DNSKRLLSKM QAKALKLNEQ FDELYSELIR EMARRRIFLV NEHQLDEAQE
KWITKYFRKE VMPHITPLLM KDEIDVLQFL KDEYAYIAVE LRKEDHSQYA LIEIPTDHLP
RFVMVPEQKG KRRKTIILLD NIIRYCLDEL FKGFFDYDEL AGYAMKMTRD AEYDLRNEIE
YSLLEQMSAG VNQRLTAMPV RFVYEREMPQ EMLDFLCSKL RISNYDNLIP GGRYHNFKDF
IAFPNVGREY LENKPMPPMK CADFEGYANS FEAIKAKDIL LYYPYHTFDH IGELVRQASF
DPKVLSIKIN IYRVAKDSRL MNSLIDAVHN GKNVTVVVEL QARFDEEANI EWSKVLTEAG
VHVIFGAPGL KIHSKLLMIS RREGDDIIRY AHIGTGNFHE KTARIYTDFS LLTADQEITN
EVRNVFGYIE NPYRPVKFNH LMVSPRNSRT QIYRLIDNEI ANAKAGKKAG LTIKVNNLVD
KGIVTRLYAA SNAGVKINMI IRGMCALVPG IEGVSENIRI ISIVDRFLEH PRVVITHNDG
DPQVYISSAD WMTRNIDHRI EVAAPVRDPR LKQRIIDITN IHFTDTVKAR LIDKEMSNSY
VPRGNRKKVR SQVAIYDYLK NIEKQTRRQK SDVSDT
