PK21_RHOPA
ID PK21_RHOPA Reviewed; 289 AA.
AC Q6N140;
DT 20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=ADP-polyphosphate phosphotransferase {ECO:0000305};
DE EC=2.7.4.- {ECO:0000269|PubMed:19001261};
DE AltName: Full=Polyphosphate kinase PPK2 {ECO:0000305};
GN OrderedLocusNames=RPA4569 {ECO:0000312|EMBL:CAE30009.1};
OS Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Rhodopseudomonas.
OX NCBI_TaxID=258594;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-98 / CGA009;
RX PubMed=14704707; DOI=10.1038/nbt923;
RA Larimer F.W., Chain P., Hauser L., Lamerdin J.E., Malfatti S., Do L.,
RA Land M.L., Pelletier D.A., Beatty J.T., Lang A.S., Tabita F.R.,
RA Gibson J.L., Hanson T.E., Bobst C., Torres y Torres J.L., Peres C.,
RA Harrison F.H., Gibson J., Harwood C.S.;
RT "Complete genome sequence of the metabolically versatile photosynthetic
RT bacterium Rhodopseudomonas palustris.";
RL Nat. Biotechnol. 22:55-61(2004).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=19001261; DOI=10.1073/pnas.0807563105;
RA Nocek B., Kochinyan S., Proudfoot M., Brown G., Evdokimova E., Osipiuk J.,
RA Edwards A.M., Savchenko A., Joachimiak A., Yakunin A.F.;
RT "Polyphosphate-dependent synthesis of ATP and ADP by the family-2
RT polyphosphate kinases in bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:17730-17735(2008).
CC -!- FUNCTION: Uses inorganic polyphosphate (polyP) as a donor to convert
CC ADP to ATP. {ECO:0000269|PubMed:19001261}.
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:19001261};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:19575;
CC Evidence={ECO:0000269|PubMed:19001261};
CC -!- SIMILARITY: Belongs to the polyphosphate kinase 2 (PPK2) family. Class
CC I subfamily. {ECO:0000305}.
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DR EMBL; BX572607; CAE30009.1; -; Genomic_DNA.
DR RefSeq; WP_011160101.1; NC_005296.1.
DR AlphaFoldDB; Q6N140; -.
DR SMR; Q6N140; -.
DR STRING; 258594.RPA4569; -.
DR PRIDE; Q6N140; -.
DR EnsemblBacteria; CAE30009; CAE30009; RPA4569.
DR GeneID; 66895720; -.
DR KEGG; rpa:RPA4569; -.
DR eggNOG; COG2326; Bacteria.
DR HOGENOM; CLU_048699_1_0_5; -.
DR OMA; RTHYENV; -.
DR PhylomeDB; Q6N140; -.
DR BioCyc; RPAL258594:TX73_RS23345-MON; -.
DR Proteomes; UP000001426; Chromosome.
DR GO; GO:0008976; F:polyphosphate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006754; P:ATP biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006797; P:polyphosphate metabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR016898; Polyphosphate_phosphotransfera.
DR InterPro; IPR022300; PPK2-rel_1.
DR InterPro; IPR022488; PPK2-related.
DR Pfam; PF03976; PPK2; 1.
DR PIRSF; PIRSF028756; PPK2_prd; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR03709; PPK2_rel_1; 1.
PE 1: Evidence at protein level;
KW ATP synthesis; Kinase; Reference proteome; Transferase.
FT CHAIN 1..289
FT /note="ADP-polyphosphate phosphotransferase"
FT /id="PRO_0000442592"
SQ SEQUENCE 289 AA; 34057 MW; 9CC3C3A44BA46103 CRC64;
MKIKTKQFRV GEGEKVDLGK WPTKVDPFYE SKEHYHELLR TQVERLSDLQ QLLYASNRHA
VLLIFQAMDA AGKDGVIRHV LSGINPQGCQ VFSFKHPSAT ELQHDFLWRT TRDLPERGRI
GVFNRSYYEE VLIVRVHPDI LQSEAVPNGE NFGKSFWHKR YRSIRNLEQH LHANGTRIVK
FFLHLSKDEQ RKRFLARIDE PEKNWKFSAA DLEERQYWDD YMDAYEKCLS ETSSEDSPWY
AVPADDKENA RLIVSQVIAE TMESLKMSYP ETTPARRKEL LQMRQQLLK
