PPK1_PSEAE
ID PPK1_PSEAE Reviewed; 690 AA.
AC P0DP44; O24816; Q9S646;
DT 07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2017, sequence version 1.
DT 03-AUG-2022, entry version 22.
DE RecName: Full=Polyphosphate kinase {ECO:0000255|HAMAP-Rule:MF_00347, ECO:0000303|PubMed:9734809};
DE EC=2.7.4.1 {ECO:0000255|HAMAP-Rule:MF_00347, ECO:0000269|PubMed:9734809};
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, ECO:0000303|PubMed:9734809};
GN OrderedLocusNames=PA5242;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=9734809; DOI=10.1093/dnares/5.3.157;
RA Ishige K., Kameda A., Noguchi T., Shiba T.;
RT "The polyphosphate kinase gene of Pseudomonas aeruginosa.";
RL DNA Res. 5:157-162(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(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, ECO:0000269|PubMed:9734809}.
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 ECO:0000269|PubMed:9734809};
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG08627.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA22565.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB007598; BAA22565.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE004091; AAG08627.1; ALT_INIT; Genomic_DNA.
DR PIR; JE0187; JE0187.
DR RefSeq; NP_253929.1; NC_002516.2.
DR AlphaFoldDB; P0DP44; -.
DR SMR; P0DP44; -.
DR STRING; 287.DR97_2611; -.
DR EnsemblBacteria; AAG08627; AAG08627; PA5242.
DR GeneID; 879700; -.
DR KEGG; pae:PA5242; -.
DR PseudoCAP; PA5242; -.
DR HOGENOM; CLU_009678_5_0_6; -.
DR OMA; NIKWARK; -.
DR Proteomes; UP000002438; 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 1: Evidence at protein level;
KW ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..690
FT /note="Polyphosphate kinase"
FT /id="PRO_0000128652"
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 690 AA; 78293 MW; 7F215EDD7F35742E CRC64;
MDDSSLYIHR ELSQLQFNIR VLEQALDESY PLLERLKFLL IFSSNLDEFF EIRIAGLKKQ
ITFAREQAGA DGLLPHQALA RISELVHEQV SRQYRILNET LLPELAKHQI RFIRRRHWTL
KIKTWVRRFF RDEIAPIITP IGLDPTHPFP LLVNKSLNFI VELEGMDAFG RDSGLAIIPA
PRLLPRIIRL PEDVGGEGDN YVFLSSMIHA HADDLFPGMK VKGCYQFRLT RNADLSVDTE
DVEDLARALR GELFSRRYGD AVRLEVVDTC PQNLTNYLLK QFGLSESELY KVSGPVNLTR
LFSVTGLESH PELQYPPFTP AIPRLLQKKE NLFNVLSKLD VLLMHPFESF TPVIDLLRQA
AKDPNVLAIK QTLYRSGANS EIVDALVEAA RNGKEVTAVI ELRARFDEES NLQLASRLQQ
AGAVVIYGVV GFKTHAKMML ILRREDGELR RYAHLGTGNY HAGNARLYTD YSLLTADVAL
CEDLHKLFNQ LIGMGKTLRM KKLLHAPFTL KKNLLEMINR EAAQAALGQP AHIMAKVNSL
TDPKVIRALY KASQAGVRID LVVRGMCCLR PGIPGVSHNI HVRSIIGRFL EHSRIYYFLN
GGDEKLYLSS ADWMERNLDM RVETCFPVEG KKLVQRVKKE LETYLTDNTQ AWVLQADGSY
QRLSPTGNQN PRNTQATLLE KLAAPVLTAR
