ID   PK21B_RUEPO             Reviewed;         344 AA.
AC   Q5LU04;
DT   20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=NDP-polyphosphate phosphotransferase 2 {ECO:0000305};
DE            EC=2.7.4.- {ECO:0000269|PubMed:24930102};
DE   AltName: Full=Polyphosphate kinase PPK2 2 {ECO:0000305};
DE   AltName: Full=RpPPK2-2 {ECO:0000303|PubMed:24930102};
GN   Name=ppk2 {ECO:0000312|EMBL:AAV94548.1};
GN   OrderedLocusNames=SPO1256 {ECO:0000312|EMBL:AAV94548.1};
OS   Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter
OS   pomeroyi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Ruegeria.
OX   NCBI_TaxID=246200;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX   PubMed=15602564; DOI=10.1038/nature03170;
RA   Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B.,
RA   Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., Brinkac L.M.,
RA   Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E., Sheldon W.M.,
RA   Ye W., Miller T.R., Carlton J., Rasko D.A., Paulsen I.T., Ren Q.,
RA   Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R.,
RA   Nelson W.C., Sullivan S.A., Rosovitz M.J., Haft D.H., Selengut J., Ward N.;
RT   "Genome sequence of Silicibacter pomeroyi reveals adaptations to the marine
RT   environment.";
RL   Nature 432:910-913(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX   PubMed=25780504; DOI=10.1186/1944-3277-9-11;
RA   Rivers A.R., Smith C.B., Moran M.A.;
RT   "An updated genome annotation for the model marine bacterium Ruegeria
RT   pomeroyi DSS-3.";
RL   Stand. Genomic Sci. 9:11-11(2014).
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX   PubMed=24930102; DOI=10.1007/s10529-014-1566-6;
RA   Achbergerova L., Nahalka J.;
RT   "Degradation of polyphosphates by polyphosphate kinases from Ruegeria
RT   pomeroyi.";
RL   Biotechnol. Lett. 36:2029-2035(2014).
CC   -!- FUNCTION: Uses inorganic polyphosphate (polyP) as a donor to convert
CC       NDP to NTP. PolyP hydrolysis is slightly faster with ADP, but it can
CC       also use GDP, CDP and UDP. {ECO:0000269|PubMed:24930102}.
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;
CC         Evidence={ECO:0000269|PubMed:24930102};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[phosphate](n) + CTP = [phosphate](n+1) + CDP;
CC         Xref=Rhea:RHEA:55408, Rhea:RHEA-COMP:9859, Rhea:RHEA-COMP:14280,
CC         ChEBI:CHEBI:16838, ChEBI:CHEBI:37563, ChEBI:CHEBI:58069;
CC         Evidence={ECO:0000269|PubMed:24930102};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[phosphate](n) + GTP = [phosphate](n+1) + GDP;
CC         Xref=Rhea:RHEA:55412, Rhea:RHEA-COMP:9859, Rhea:RHEA-COMP:14280,
CC         ChEBI:CHEBI:16838, ChEBI:CHEBI:37565, ChEBI:CHEBI:58189;
CC         Evidence={ECO:0000269|PubMed:24930102};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[phosphate](n) + UTP = [phosphate](n+1) + UDP;
CC         Xref=Rhea:RHEA:55404, Rhea:RHEA-COMP:9859, Rhea:RHEA-COMP:14280,
CC         ChEBI:CHEBI:16838, ChEBI:CHEBI:46398, ChEBI:CHEBI:58223;
CC         Evidence={ECO:0000269|PubMed:24930102};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:24930102};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=2.5 mM for ADP {ECO:0000269|PubMed:24930102};
CC         Note=kcat is 313 min(-1) with ADP as substrate.
CC         {ECO:0000269|PubMed:24930102};
CC       pH dependence:
CC         Optimum pH is 9. {ECO:0000269|PubMed:24930102};
CC   -!- SIMILARITY: Belongs to the polyphosphate kinase 2 (PPK2) family. Class
CC       I subfamily. {ECO:0000305}.
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DR   EMBL; CP000031; AAV94548.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q5LU04; -.
DR   SMR; Q5LU04; -.
DR   STRING; 246200.SPO1256; -.
DR   EnsemblBacteria; AAV94548; AAV94548; SPO1256.
DR   KEGG; sil:SPO1256; -.
DR   eggNOG; COG2326; Bacteria.
DR   HOGENOM; CLU_048699_0_1_5; -.
DR   OMA; TKLWFSV; -.
DR   BRENDA; 2.7.4.1; 8123.
DR   Proteomes; UP000001023; Chromosome.
DR   GO; GO:0008976; F:polyphosphate kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR022488; PPK2-related.
DR   InterPro; IPR022486; PPK2_PA0141.
DR   Pfam; PF03976; PPK2; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR03707; PPK2_P_aer; 1.
PE   1: Evidence at protein level;
KW   Kinase; Reference proteome; Transferase.
FT   CHAIN           1..344
FT                   /note="NDP-polyphosphate phosphotransferase 2"
FT                   /id="PRO_0000442594"
FT   REGION          1..60
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   344 AA;  39947 MW;  6A4F967EB512B2DD CRC64;
     METAKPIAPQ KDSKANGVDA TDPVVKVASP QDPAGDAKVE DATAPVAEVE PRTPRNRRLP
     TPENVRHAFE SGKYPYSRKM SRRPYEAEKA MLQAELLKVQ LWAQETGERF VLLFEGRDAA
     GKGGTIKRFM EHLNPRQARV VALNKPTWEE KGQWYYQRYV QELPTVGEMV FYDRSWYNRA
     GVERVMGFCT PNEYLEFMRQ TPDLERMLVR SGIRLYKYWF SVTQEEQQRR FKSRETDPLK
     QWKLSPIDKA SLDKWDDYTE AKEAMFFYTD TADAPWTIIK SNDKKRARLN CMRHFLSTID
     YPGKDKHVVG EPDPLIVGRA HHVIQKSEHI LGTALHPDQR ARQD