PPK1_THEVB
ID PPK1_THEVB Reviewed; 732 AA.
AC Q8DMA8;
DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2003, sequence version 2.
DT 03-AUG-2022, entry version 98.
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=tlr0213;
OS Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1).
OC Bacteria; Cyanobacteria; Pseudanabaenales; Thermosynechococcaceae;
OC Thermosynechococcus.
OX NCBI_TaxID=197221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C.,
RA Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takeuchi C., Yamada M., Tabata S.;
RT "Complete genome structure of the thermophilic cyanobacterium
RT Thermosynechococcus elongatus BP-1.";
RL DNA Res. 9:123-130(2002).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC07766.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BA000039; BAC07766.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_681004.1; NC_004113.1.
DR AlphaFoldDB; Q8DMA8; -.
DR SMR; Q8DMA8; -.
DR STRING; 197221.22293934; -.
DR EnsemblBacteria; BAC07766; BAC07766; BAC07766.
DR KEGG; tel:tlr0213; -.
DR PATRIC; fig|197221.4.peg.219; -.
DR eggNOG; COG0855; Bacteria.
DR OMA; AHPFPQV; -.
DR OrthoDB; 76567at2; -.
DR BRENDA; 2.7.4.1; 7763.
DR Proteomes; UP000000440; 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 3: Inferred from homology;
KW ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Repeat; Transferase.
FT CHAIN 1..732
FT /note="Polyphosphate kinase"
FT /id="PRO_0000128663"
FT REGION 699..718
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 477
FT /note="Phosphohistidine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT BINDING 61
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT BINDING 417
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT BINDING 447
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT BINDING 510
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT BINDING 606
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT BINDING 634
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
SQ SEQUENCE 732 AA; 83568 MW; BF7157127A7248BA CRC64;
MPSAKSPRRK APEPIDLDNP QYYFNRSLSW LEFNKRVLHE AYDPRTPLLE RLKFMAIFSS
NLDEFFMVRV AGLKQQVESG ILQVGADGMP PAEQLQAVRQ YLLPIVTEQH RYFDQELRAL
LAKESIFLTR FNELTPEQQA YLNDYFQAQV FPVLTPLAVD PAHPFPYISS LSLNLAVLIR
DPESGQERLA RVKVPNQFPR FVALPQHLHS PQGVHWLGVP LEEIIAHNLS ALFPGMEIEA
YFAFRITRSA DLELETDKAD DLLIAIEQEI RKRRFGSVVR LEVQRGIPPL LRQTLMEEMD
LEEIDVYELE GLLCLNDLFA FMGLPLPQFK DPEWQPQVPP SFQRVEERES MFDTSSEITT
LGTDYWEAVA NELFSLIREG DIIVHHPYHS FAATVQRFIT LAAHDPQVLA IKITLYRTSG
DSPIVSALIK AAENGKQVAV LVELKARFDE ENNILWARKL EKVGVHVVYG VPGLKTHTKT
VLVVRQEAGQ IRRYVHIGTG NYNPKTASLY EDLGLFSCRE ELGADLSELF NVLTGYARQR
DYRKLLVAPV TMRDRTLQLI YREIEHARNG QPARIIAKMN AITDTQVIRA LYEASQAGVD
IDLIIRGMCC LRPGVPGVSD RIRVISIIGR FLEHSRIFYF GNNGDPEYYI GSADWRSRNL
DRRVEAITPI EDPAIQLELK ERLEIMLADN RQAWELQPDG TYRQRQPAPG EAERGTHSVL
MARTLKDVQG SH
