PK21A_PSEAE
ID PK21A_PSEAE Reviewed; 357 AA.
AC Q9I6Z1;
DT 20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2017, sequence version 2.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=GDP-polyphosphate phosphotransferase {ECO:0000305};
DE EC=2.7.4.34 {ECO:0000269|PubMed:12482933, ECO:0000269|PubMed:12486232};
DE AltName: Full=Polyphosphate kinase PPK2 1 {ECO:0000305};
GN Name=ppk2 {ECO:0000303|PubMed:12486232};
GN OrderedLocusNames=PA0141 {ECO:0000312|EMBL:AAG03531.1};
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2]
RP PROTEIN SEQUENCE OF 2-10, IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION,
RP CATALYTIC ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=PAOM5;
RX PubMed=12486232; DOI=10.1073/pnas.262655199;
RA Zhang H., Ishige K., Kornberg A.;
RT "A polyphosphate kinase (PPK2) widely conserved in bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16678-16683(2002).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBUNIT.
RC STRAIN=PAOM5;
RX PubMed=12482933; DOI=10.1073/pnas.262655299;
RA Ishige K., Zhang H., Kornberg A.;
RT "Polyphosphate kinase (PPK2), a potent, polyphosphate-driven generator of
RT GTP.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16684-16688(2002).
CC -!- FUNCTION: Uses inorganic polyphosphate (polyP) as a donor to convert
CC GDP to GTP and ADP to ATP. Shows a preference for GDP. Can also
CC catalyze the synthesis of polyP from GTP or ATP, but the rate of polyP
CC utilization is 75-fold greater than the rate of polyP synthesis.
CC {ECO:0000269|PubMed:12482933, ECO:0000269|PubMed:12486232}.
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; EC=2.7.4.34;
CC Evidence={ECO:0000269|PubMed:12482933, ECO:0000269|PubMed:12486232};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:55414;
CC Evidence={ECO:0000269|PubMed:12482933, ECO:0000269|PubMed:12486232};
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:12482933, ECO:0000269|PubMed:12486232};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:19575;
CC Evidence={ECO:0000269|PubMed:12482933, ECO:0000269|PubMed:12486232};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:12482933, ECO:0000269|PubMed:12486232};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:12482933, ECO:0000269|PubMed:12486232};
CC Note=Mg(2+) is preferred for polyP utilization and Mn(2+) is preferred
CC for polyP synthesis. {ECO:0000269|PubMed:12482933,
CC ECO:0000269|PubMed:12486232};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=300 uM for GDP {ECO:0000269|PubMed:12482933};
CC KM=750 uM for ADP {ECO:0000269|PubMed:12482933};
CC KM=0.68 mM for GTP {ECO:0000269|PubMed:12486232};
CC KM=0.5 mM for ATP {ECO:0000269|PubMed:12486232};
CC -!- SUBUNIT: Homotetramer. Also forms octamers.
CC {ECO:0000269|PubMed:12482933}.
CC -!- SIMILARITY: Belongs to the polyphosphate kinase 2 (PPK2) family. Class
CC I subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG03531.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305|PubMed:12486232};
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DR EMBL; AE004091; AAG03531.1; ALT_INIT; Genomic_DNA.
DR PIR; E83627; E83627.
DR RefSeq; NP_248831.1; NC_002516.2.
DR AlphaFoldDB; Q9I6Z1; -.
DR SMR; Q9I6Z1; -.
DR STRING; 287.DR97_3098; -.
DR PaxDb; Q9I6Z1; -.
DR PRIDE; Q9I6Z1; -.
DR EnsemblBacteria; AAG03531; AAG03531; PA0141.
DR GeneID; 879494; -.
DR KEGG; pae:PA0141; -.
DR PATRIC; fig|208964.12.peg.147; -.
DR PseudoCAP; PA0141; -.
DR HOGENOM; CLU_048699_2_1_6; -.
DR InParanoid; Q9I6Z1; -.
DR PhylomeDB; Q9I6Z1; -.
DR BioCyc; PAER208964:G1FZ6-143-MON; -.
DR BRENDA; 2.7.4.1; 5087.
DR BRENDA; 2.7.4.34; 5087.
DR Proteomes; UP000002438; 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 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 ATP synthesis; Direct protein sequencing; Kinase; Magnesium; Manganese;
KW Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12486232"
FT CHAIN 2..357
FT /note="GDP-polyphosphate phosphotransferase"
FT /id="PRO_0000442587"
FT REGION 1..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..83
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 357 AA; 40788 MW; 8E5F46D892D13FB7 CRC64;
MSEEPTVSPP SPEQPAAQPA KPARPAARRA PRKPATRRPR VASPAQKARE EIQAISQKPV
ALQVASAPHG SSEDSTSASL PANYPYHTRM RRNEYEKAKH DLQIELLKVQ SWVKETGQRV
VVLFEGRDAA GKGGTIKRFM EHLNPRGARI VALEKPSSQE QGQWYFQRYI QHLPTAGEMV
FFDRSWYNRA GVERVMGFCS PLQYLEFMRQ APELERMLTN SGILLFKYWF SVSREEQLRR
FISRRDDPLK HWKLSPIDIK SLDKWDDYTA AKQAMFFHTD TADAPWTVIK SDDKKRARLN
CIRHFLHSLD YPDKDRRIAH EPDPLLVGPA SRVIEEDEKV YAEAAAAPGH ANLDIPA
