PPK1_SALTY
ID PPK1_SALTY Reviewed; 688 AA.
AC O86090;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 126.
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=STM2501;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=WRAY;
RA Kim K.S., Fraley C.D., Kornberg A.;
RT "Polyphosphate kinase (ppk) and exopolyphosphatase (ppx) genes in
RT Salmonella typhimurium.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(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; AF085682; AAC34890.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL21395.1; -; Genomic_DNA.
DR RefSeq; NP_461436.1; NC_003197.2.
DR RefSeq; WP_000529555.1; NC_003197.2.
DR AlphaFoldDB; O86090; -.
DR SMR; O86090; -.
DR STRING; 99287.STM2501; -.
DR PaxDb; O86090; -.
DR EnsemblBacteria; AAL21395; AAL21395; STM2501.
DR GeneID; 1254023; -.
DR KEGG; stm:STM2501; -.
DR PATRIC; fig|99287.12.peg.2640; -.
DR HOGENOM; CLU_009678_6_1_6; -.
DR OMA; NIKWARK; -.
DR PhylomeDB; O86090; -.
DR BioCyc; SENT99287:STM2501-MON; -.
DR Proteomes; UP000001014; 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_0000128656"
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; 80456 MW; 53A43A32AC38F6B3 CRC64;
MGQEKLYIEK ELSWLAFNER VLQEAADKSN PLIERMRFLG IYSNNLDEFY KVRFAELKRR
IIISEEQGSN SHSRHLLGKI QSRVLKADQE FDGLYNELLL EMARNQIFLI NERQLSVNQQ
SWLRHYFKHY LRQHITPILI NRETDLVQFL KDDYTYLAVE IIRGDTINYA LLEIPSDKVP
RFVNLPPETP RRRKPMILLD NILRYCLDDI FKGFFDYDAL NAYSMKMTRD AEYDLVHEME
SSLMELMSSS LKQRLTAEPV RFVYQRDMPA ALVDVLREKL TISRYDSIVP GGRYHNFKDF
INFPNVGKAN LVNKPLPRLR HLWFDKEKFR NGFDAIRERD VLLYYPYHTF EHVLELLRQA
SFDPSVLAIK INIYRVAKDS RIIDSMIHAA HNGKKVTVVV ELQARFDEEA NIHWAKRLTE
AGVHVIFSAP GLKIHAKLFL ISRKEGDDVV RYAHIGTGNF NEKTARLYTD YSLLTADARI
TNEVRRVFNF IENPYRPVTF DYLMVSPQNS RRLLYEMIDR EIANAQQGLP SGITLKLNNL
VDKGLVDRLY AASGSGVQVN LLVRGMCSLI PQLEGISDNI RAISIVDRYL EHDRVYIFEN
GGDKQVWLSS ADWMTRNIDY RIEVATPILD PRLKQRVLDI IDILFSDTVK ARFIDKELSN
RYVPRGNRRK VQAQLAIYDY IKSLEQPD
