PPK1_VIBVY
ID PPK1_VIBVY Reviewed; 700 AA.
AC Q7MNJ0;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 105.
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=VV0727;
OS Vibrio vulnificus (strain YJ016).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=196600;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJ016;
RX PubMed=14656965; DOI=10.1101/gr.1295503;
RA Chen C.-Y., Wu K.-M., Chang Y.-C., Chang C.-H., Tsai H.-C., Liao T.-L.,
RA Liu Y.-M., Chen H.-J., Shen A.B.-T., Li J.-C., Su T.-L., Shao C.-P.,
RA Lee C.-T., Hor L.-I., Tsai S.-F.;
RT "Comparative genome analysis of Vibrio vulnificus, a marine pathogen.";
RL Genome Res. 13:2577-2587(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; BA000037; BAC93491.1; -; Genomic_DNA.
DR RefSeq; WP_011149582.1; NC_005139.1.
DR AlphaFoldDB; Q7MNJ0; -.
DR SMR; Q7MNJ0; -.
DR STRING; 672.VV93_v1c06740; -.
DR EnsemblBacteria; BAC93491; BAC93491; BAC93491.
DR KEGG; vvy:VV0727; -.
DR PATRIC; fig|196600.6.peg.744; -.
DR eggNOG; COG0855; Bacteria.
DR HOGENOM; CLU_009678_5_0_6; -.
DR OMA; NIKWARK; -.
DR OrthoDB; 76567at2; -.
DR Proteomes; UP000002675; Chromosome I.
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; 2.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Repeat; Transferase.
FT CHAIN 1..700
FT /note="Polyphosphate kinase"
FT /id="PRO_0000128669"
FT DOMAIN 428..462
FT /note="PLD phosphodiesterase 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT DOMAIN 585..615
FT /note="PLD phosphodiesterase 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT ACT_SITE 433
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 373
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT BINDING 403
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT BINDING 466
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT BINDING 562
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT BINDING 590
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
SQ SEQUENCE 700 AA; 81861 MW; A573AED675446DE1 CRC64;
MSADKFYIEK ELSWLSFNER VLQEAADKTV PLIERIRFLG IFSNNLDEFY KVRFSDVKRR
ILINREQGGN DISKHLLSKM QSKALKLNER FDELYNELIR DMARRHIFLV NESQLDEAQQ
KWIIKYFQKE VLPHITPLML TDEIDVLQFL KDEYAYIAVE LKQQEQAKYA LLEIPTDHLP
RFIMVPEQKG KRKKTIILLD NIIRFCLNDI FRGFFDYDEL NGYAMKMTRD AEYDLRHEVE
YSLLEQMSEG LSQRLTALPV RFVYERDMPE DMLKYLCYKL KISHYDSLIP GGRYHNFKDF
IAFPNVGRDY LENKPLPPLA CADFEGYANA FDAIRNQDIL LHYPYHSFEH ITELVRQASF
DPKVVSIKIN VYRVAKNSRL MNSLIDAVHN GKRVTVVVEL QARFDEEANI EWSKRLTDAG
VHVIFGVPGM KIHAKLLLIT RREEQGFVRY AHIGTGNFHE RTARIYTDFS LLTADQELAA
EVRGVFSYIM NPFRPIKFRH LIVSPRNSRS QLYRLLDREI HNAQAGKKAS ITLKVNNLVD
KGLISKLYAA SSAGVKIRMI IRGMCSLVPG LEGISENIEI ISIIDRFLEH PRVLVVHNDG
DPQVFISSAD WMERNIDNRI EVMSPVRDAR IKQRIIDILS IQFTDTVKAR RIDKEMSNNY
VERGNRKKIR SQIAIYDYLK NVEKHTRKQK GQVEPNDNNE
