PK22_PSESM
ID PK22_PSESM Reviewed; 498 AA.
AC Q886D9;
DT 20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Polyphosphate:AMP phosphotransferase {ECO:0000305};
DE Short=PAP {ECO:0000250|UniProtKB:Q83XD3};
DE EC=2.7.4.33 {ECO:0000269|PubMed:19001261};
DE AltName: Full=Polyphosphate kinase PPK2 {ECO:0000305};
GN OrderedLocusNames=PSPTO_1640 {ECO:0000312|EMBL:AAO55160.1};
OS Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=223283;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-871 / DC3000;
RX PubMed=12928499; DOI=10.1073/pnas.1731982100;
RA Buell C.R., Joardar V., Lindeberg M., Selengut J., Paulsen I.T.,
RA Gwinn M.L., Dodson R.J., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA Daugherty S.C., Brinkac L.M., Beanan M.J., Haft D.H., Nelson W.C.,
RA Davidsen T.M., Zafar N., Zhou L., Liu J., Yuan Q., Khouri H.M.,
RA Fedorova N.B., Tran B., Russell D., Berry K.J., Utterback T.R.,
RA Van Aken S.E., Feldblyum T.V., D'Ascenzo M., Deng W.-L., Ramos A.R.,
RA Alfano J.R., Cartinhour S., Chatterjee A.K., Delaney T.P., Lazarowitz S.G.,
RA Martin G.B., Schneider D.J., Tang X., Bender C.L., White O., Fraser C.M.,
RA Collmer A.;
RT "The complete genome sequence of the Arabidopsis and tomato pathogen
RT Pseudomonas syringae pv. tomato DC3000.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:10181-10186(2003).
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 AMP to ADP. Can also convert GMP to GDP, with lower efficiency.
CC {ECO:0000269|PubMed:19001261}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[phosphate](n) + ADP = [phosphate](n+1) + AMP;
CC Xref=Rhea:RHEA:57820, Rhea:RHEA-COMP:9859, Rhea:RHEA-COMP:14280,
CC ChEBI:CHEBI:16838, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216;
CC EC=2.7.4.33; Evidence={ECO:0000269|PubMed:19001261};
CC -!- SIMILARITY: Belongs to the polyphosphate kinase 2 (PPK2) family. Class
CC II subfamily. {ECO:0000305}.
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DR EMBL; AE016853; AAO55160.1; -; Genomic_DNA.
DR RefSeq; NP_791465.1; NC_004578.1.
DR RefSeq; WP_011103643.1; NC_004578.1.
DR AlphaFoldDB; Q886D9; -.
DR SMR; Q886D9; -.
DR STRING; 223283.PSPTO_1640; -.
DR EnsemblBacteria; AAO55160; AAO55160; PSPTO_1640.
DR GeneID; 1183277; -.
DR KEGG; pst:PSPTO_1640; -.
DR PATRIC; fig|223283.9.peg.1664; -.
DR eggNOG; COG2326; Bacteria.
DR HOGENOM; CLU_033786_0_2_6; -.
DR OMA; SPLDWQQ; -.
DR OrthoDB; 953793at2; -.
DR PhylomeDB; Q886D9; -.
DR Proteomes; UP000002515; Chromosome.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0043751; F:polyphosphate:AMP phosphotransferase activity; IEA:InterPro.
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; -; 2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR022489; PolyP_AMP_Tfrase.
DR InterPro; IPR022488; PPK2-related.
DR Pfam; PF03976; PPK2; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR TIGRFAMs; TIGR03708; poly_P_AMP_trns; 1.
PE 1: Evidence at protein level;
KW Kinase; Reference proteome; Repeat; Transferase.
FT CHAIN 1..498
FT /note="Polyphosphate:AMP phosphotransferase"
FT /id="PRO_0000442598"
FT REGION 11..234
FT /note="PPK2 1"
FT /evidence="ECO:0000305"
FT REGION 269..491
FT /note="PPK2 2"
FT /evidence="ECO:0000305"
SQ SEQUENCE 498 AA; 57955 MW; 334F148213842F45 CRC64;
MFESAEIGHA IDDDTYEAAL PSLREALLEA QIDLHEQAKR QIIVLINGIE GAGKGETVKL
LSEWMDPRLI EVRTFDQQTD EELAHPPVWR YWRQLPAKGR MGIFFGNWYS QMLQGRVHGQ
YKDAVLDQAI SGAERLEKML CDEGALIFKF WFHLSKKQMK LRLKTLKDDP LHSWRISPLD
WQQSKTYDKF VRFGERVLRR TSRDYAPWHV IEGVDANYRS LTVGRLLLEG MQAALNKVEP
ESSALTIGPL AIHNNERTLL DSLDLSLHLS KEDYQHELIA EQARLSGNLR DKRMKSHALV
AVFEGNDAAG KGGAIRRVAA ALDPRQYAIV PIAAPTQDER AQPYLWRFWR QIPARGKFTI
FDRSWYGRVL VERVEGFCSE SDWKRAYAEI NDFEEQLTEA GVVVVKFWLA IDEQTQLERF
QEREKIPFKR YKITEDDWRN RKKWPDYRQA VGDMVDRTST EIAPWTLIEA NDKRWARVKV
LRTINEALEK AFARDKKK