PPK1_STAES
ID PPK1_STAES Reviewed; 734 AA.
AC Q8CR71;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 106.
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=SE_2034;
OS Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176280;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12228 / FDA PCI 1200;
RX PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT "Genome-based analysis of virulence genes in a non-biofilm-forming
RT Staphylococcus epidermidis strain (ATCC 12228).";
RL Mol. Microbiol. 49:1577-1593(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; AE015929; AAO05675.1; -; Genomic_DNA.
DR RefSeq; NP_765589.1; NC_004461.1.
DR AlphaFoldDB; Q8CR71; -.
DR SMR; Q8CR71; -.
DR STRING; 176280.SE_2034; -.
DR EnsemblBacteria; AAO05675; AAO05675; SE_2034.
DR KEGG; sep:SE_2034; -.
DR PATRIC; fig|176280.10.peg.1987; -.
DR eggNOG; COG0855; Bacteria.
DR HOGENOM; CLU_009678_5_0_9; -.
DR OMA; NIKWARK; -.
DR Proteomes; UP000001411; 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; Transferase.
FT CHAIN 1..734
FT /note="Polyphosphate kinase"
FT /id="PRO_0000128657"
FT DOMAIN 447..481
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT REGION 705..734
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 452
FT /note="Phosphohistidine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT BINDING 67
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT BINDING 392
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT BINDING 422
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT BINDING 485
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT BINDING 581
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT BINDING 609
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
SQ SEQUENCE 734 AA; 85205 MW; F18E4240DA68B56B CRC64;
MHNKDKLMRC MYSMQTRLGE KDINLPQYYN NRELSWLDFN YRVLQESYDK NNPLLEKLNF
ISIFSSNLDE FFMVRVAGLK DQVKMGYDKP ENKAQMTPQE QLDAIKIKNT DYVNTQYQRY
NELIKELANY DIEMVKPEDL SDALIEKLEQ EFKLSVLPTL TPLGIDAYHP FPKLNNKSLN
IFVDIDTEDA INSAIVQIPS LIPRFLTLNE GTKQYVVMVE DVITYFINYL FTGYEVLNTF
TFRITRNADL TIHEDGAEDL LIEIERFLKE RKSGSAVRLE LDCRTSEKEN VEWLINQLEI
EDNDIYYLDG PLDLTFLFGL VDHLSHKLKY LTYEKYTPQP PRSLGNKNIY QLSLERDIFF
HHPYESFEPI VDFIRQAADD PNTIAIKQTL YRVSKDSPII NSLKEAAENG KQVTVLVELK
ARFDEENNVH WARMLEDAGC HVIYGMTHLK THSKIALVVK RINNELTSFV HLGTGNYNDK
TAKLYTDMGI ITTNKDIAED AINFFNYLSG YSTKPEYNKL IVAPYDIRDV FIDRIDKEIR
SHLQHGNGKI MMKMNSLTDK TIIEKLFEAS QAGVKIQLII RGICCLKPGI PGISENIEVV
SIVGRLLEHS RIYYFHNNSE AHIYLSSADV MTRNMIKRVE ILFPVEDKSI GQRLVNYMNL
QLSDNQKGRY QDAQGLYHYV ENNSSPLNSQ SYLMQEAIKY GEELKKQSVQ PSGQPVHSRR
GGSWMRKLKN TFKR
