PPK1_ECO57
ID PPK1_ECO57 Reviewed; 688 AA.
AC P0A7B2; P28688; Q47549;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 111.
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=Z3764, ECs3363;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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; AE005174; AAG57611.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB36786.1; -; Genomic_DNA.
DR PIR; C91049; C91049.
DR PIR; G85893; G85893.
DR RefSeq; NP_311390.1; NC_002695.1.
DR RefSeq; WP_000529576.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P0A7B2; -.
DR SMR; P0A7B2; -.
DR STRING; 155864.EDL933_3657; -.
DR PRIDE; P0A7B2; -.
DR EnsemblBacteria; AAG57611; AAG57611; Z3764.
DR EnsemblBacteria; BAB36786; BAB36786; ECs_3363.
DR GeneID; 66673634; -.
DR GeneID; 912733; -.
DR KEGG; ece:Z3764; -.
DR KEGG; ecs:ECs_3363; -.
DR PATRIC; fig|386585.9.peg.3513; -.
DR eggNOG; COG0855; Bacteria.
DR HOGENOM; CLU_009678_6_1_6; -.
DR OMA; NIKWARK; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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: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 INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..688
FT /note="Polyphosphate kinase"
FT /id="PRO_0000128641"
FT DOMAIN 430..464
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT ACT_SITE 435
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 375
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT BINDING 405
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT BINDING 468
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT BINDING 564
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT BINDING 592
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
SQ SEQUENCE 688 AA; 80432 MW; E1EA6C53432E6935 CRC64;
MGQEKLYIEK ELSWLSFNER VLQEAADKSN PLIERMRFLG IYSNNLDEFY KVRFAELKRR
IIISEEQGSN SHSRHLLGKI QSRVLKADQE FDGLYNELLL EMARNQIFLI NERQLSVNQQ
NWLRHYFKQY LRQHITPILI NPDTDLVQFL KDDYTYLAVE IIRGDTIRYA LLEIPSDKVP
RFVNLPPEAP RRRKPMILLD NILRYCLDDI FKGFFDYDAL NAYSMKMTRD AEYDLVHEME
ASLMELMSSS LKQRLTAEPV RFVYQRDMPN ALVEVLREKL TISRYDSIVP GGRYHNFKDF
INFPNVGKAN LVNKPLPRLR HIWFDKAQFR NGFDAIRERD VLLYYPYHTF EHVLELLRQA
SFDPSVLAIK INIYRVAKDS RIIDSMIHAA HNGKKVTVVV ELQARFDEEA NIHWAKRLTE
AGVHVIFSAP GLKIHAKLFL ISRKENGEVV RYAHIGTGNF NEKTARLYTD YSLLTADARI
TNEVRRVFNF IENPYRPVTF DYLMVSPQNS RRLLYEMVDR EIANAQQGLP SGITLKLNNL
VDKGLVDRLY AASSSGVPVN LLVRGMCSLI PNLEGISDNI RAISIVDRYL EHDRVYIFEN
GGDKKVYLSS ADWMTRNIDY RIEVATPLLD PRLKQRVLDI IDILFSDTVK ARYIDKELSN
RYVPRGNRRK VRAQLAIYDY IKSLEQPE
