PPK1_RHOBA
ID PPK1_RHOBA Reviewed; 852 AA.
AC Q7ULJ4;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-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=RB9470;
OS Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1).
OC Bacteria; Planctomycetes; Planctomycetia; Pirellulales; Pirellulaceae;
OC Rhodopirellula.
OX NCBI_TaxID=243090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10527 / NCIMB 13988 / SH1;
RX PubMed=12835416; DOI=10.1073/pnas.1431443100;
RA Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W.,
RA Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R.,
RA Reinhardt R.;
RT "Complete genome sequence of the marine planctomycete Pirellula sp. strain
RT 1.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(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; BX294149; CAD76283.1; -; Genomic_DNA.
DR RefSeq; NP_868898.1; NC_005027.1.
DR AlphaFoldDB; Q7ULJ4; -.
DR SMR; Q7ULJ4; -.
DR STRING; 243090.RB9470; -.
DR PRIDE; Q7ULJ4; -.
DR EnsemblBacteria; CAD76283; CAD76283; RB9470.
DR KEGG; rba:RB9470; -.
DR PATRIC; fig|243090.15.peg.4534; -.
DR eggNOG; COG0855; Bacteria.
DR HOGENOM; CLU_009678_5_0_0; -.
DR InParanoid; Q7ULJ4; -.
DR OMA; NIKWARK; -.
DR OrthoDB; 76567at2; -.
DR Proteomes; UP000001025; 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 SUPFAM; SSF140356; SSF140356; 1.
DR TIGRFAMs; TIGR03705; poly_P_kin; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..852
FT /note="Polyphosphate kinase"
FT /id="PRO_0000226301"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 58..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 251..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 258..303
FT /note="Insert"
FT COMPBIAS 9..36
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..290
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 584
FT /note="Phosphohistidine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT BINDING 131
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT BINDING 524
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT BINDING 554
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT BINDING 617
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT BINDING 713
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT BINDING 741
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
SQ SEQUENCE 852 AA; 95728 MW; F19C2B253FC1CC12 CRC64;
MATGVSSRDG SRERIRRRAV ARDHPGCGPH RLDRPIGHIR YPHRHSISFS PFASLTLSHD
PAPSQSVGKR PQKSTKTASR RKVETAAADA PRFINRELAW LEFNARVLDQ ADDPSVRLLE
RAKFLAITSS NLDEFMMVRV GSLKLQAVSG GGRRDPSGRT ATEQLQAISK RCQGHVDRQY
ELLRNELLPL LGEHKINQVD PAECSDRLLA AAERHFRGDV LAVLSPQALH DRRFPMLPGL
GIHLCVQLRP GDEIGPQRTP PPSDSLDNRV PSNLKRNSDT ANQQPTPAEN ISAPEDGAEQ
TEPETQFAVI PLGRTLGRVI PLPIEKPPIE KGVAPKESDD TSPIESGYSY ALLEDLVSHF
VDEFFPGREV IQCKPFRITR NADIELREDG AGDLLGGMEE VLESRRLSDV VRLEIDANAN
SEIRDYLIKS FNVDPQFVFD IDGPLDLTYL FALHGLKGMN TLRDDEWPPQ RSPRIDPAES
MFTSISDGDI MLMHPYESFD PVVRLLEEAS VDPDVLAVKQ ILYRTSRNSP IVAALMRAAE
RGKYVTAIVE LKARFDEARN IEWAREMEQA GVQVIYGIRG LKTHAKVCII VRREPQGLVR
YVHFGTGNYN EVTANLYGDI SVLTCDEILG TDATMFFNAV TGASQPQPLQ QLGMAPLTLR
RQILDLIQGE TERSRQGQKG EIIAKMNALV DTEVIDSLYM ASQAGVKIRL NVRGVCCLRP
GVPGMSETIE VVSIVDRFLE HARTFYFRHG GDHEMFISSA DWMPRNLDRR VELLVPVIDP
AARKRLRETL QLYFRDNQNA WRMQPDGSYQ RLKPRKNEAP MRVQETLYHQ VVENRKAGKH
APQSTFETHR PD
