PK21_MYCTU
ID PK21_MYCTU Reviewed; 295 AA.
AC O05877; A5YKM3; F2GKA8; Q7D5V8;
DT 20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=GDP-polyphosphate phosphotransferase {ECO:0000305};
DE EC=2.7.4.- {ECO:0000269|PubMed:19843229};
DE AltName: Full=Polyphosphate kinase PPK2 {ECO:0000305};
GN Name=ppk2 {ECO:0000312|EMBL:ABQ58103.1};
GN OrderedLocusNames=Rv3232c {ECO:0000312|EMBL:CCP46051.1};
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=H37Rv;
RA Kim H.-Y., Ravikumar V.;
RT "Cloning and expression of polyphosphate kinase 2 from Mycobacterium
RT tuberculosis H37Rv.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH NDK, INDUCTION,
RP PHOSPHORYLATION AT HIS-115 AND HIS-247, AND MUTAGENESIS OF PHE-67; GLY-69;
RP GLY-74; LYS-75; HIS-115 AND HIS-247.
RX PubMed=19843229; DOI=10.1111/j.1365-2958.2009.06925.x;
RA Sureka K., Sanyal S., Basu J., Kundu M.;
RT "Polyphosphate kinase 2: a modulator of nucleoside diphosphate kinase
RT activity in mycobacteria.";
RL Mol. Microbiol. 74:1187-1197(2009).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC -!- FUNCTION: Uses inorganic polyphosphate (polyP) as a donor to convert
CC GDP to GTP. In addition, modulates nucleotide triphosphate synthesis
CC catalyzed by the nucleoside diphosphate kinase (Ndk) in favor of GTP
CC production over CTP or UTP. Plays an important role in survival of
CC M.tuberculosis in macrophages. {ECO:0000269|PubMed:19843229}.
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:19843229};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:55414;
CC Evidence={ECO:0000269|PubMed:19843229};
CC -!- SUBUNIT: Interacts with Ndk. {ECO:0000269|PubMed:19843229}.
CC -!- INDUCTION: Expression increases during the exponential phase of growth
CC and remains at a steady level up to the stationary phase.
CC {ECO:0000269|PubMed:19843229}.
CC -!- PTM: Autophosphorylated at His-115 and His-247 using polyP as a
CC phosphate donor. {ECO:0000269|PubMed:19843229}.
CC -!- SIMILARITY: Belongs to the polyphosphate kinase 2 (PPK2) family. Class
CC I subfamily. {ECO:0000305}.
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DR EMBL; EF555554; ABQ58103.1; -; Genomic_DNA.
DR EMBL; AL123456; CCP46051.1; -; Genomic_DNA.
DR RefSeq; NP_217749.1; NC_000962.3.
DR RefSeq; WP_003416928.1; NC_000962.3.
DR AlphaFoldDB; O05877; -.
DR SMR; O05877; -.
DR STRING; 83332.Rv3232c; -.
DR iPTMnet; O05877; -.
DR PaxDb; O05877; -.
DR PRIDE; O05877; -.
DR DNASU; 888760; -.
DR GeneID; 888760; -.
DR KEGG; mtu:Rv3232c; -.
DR PATRIC; fig|83332.111.peg.3610; -.
DR TubercuList; Rv3232c; -.
DR eggNOG; COG2326; Bacteria.
DR OMA; NPRICRV; -.
DR PhylomeDB; O05877; -.
DR BRENDA; 2.7.4.1; 3445.
DR BRENDA; 2.7.4.34; 3445.
DR PHI-base; PHI:3634; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IDA:MTBBASE.
DR GO; GO:0005525; F:GTP binding; IDA:MTBBASE.
DR GO; GO:0008976; F:polyphosphate kinase activity; IDA:MTBBASE.
DR GO; GO:0006183; P:GTP biosynthetic process; IMP:MTBBASE.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:MTBBASE.
DR GO; GO:0030808; P:regulation of nucleotide biosynthetic process; IDA:MTBBASE.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR016898; Polyphosphate_phosphotransfera.
DR InterPro; IPR022488; PPK2-related.
DR InterPro; IPR022486; PPK2_PA0141.
DR Pfam; PF03976; PPK2; 1.
DR PIRSF; PIRSF028756; PPK2_prd; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR03707; PPK2_P_aer; 1.
PE 1: Evidence at protein level;
KW Kinase; Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..295
FT /note="GDP-polyphosphate phosphotransferase"
FT /id="PRO_0000442586"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 115
FT /note="Phosphohistidine"
FT /evidence="ECO:0000305|PubMed:19843229"
FT MOD_RES 247
FT /note="Phosphohistidine"
FT /evidence="ECO:0000305|PubMed:19843229"
FT MUTAGEN 67
FT /note="F->A: Partial loss of GTP-synthesizing activity."
FT /evidence="ECO:0000269|PubMed:19843229"
FT MUTAGEN 69
FT /note="G->R: Partial loss of GTP-synthesizing activity."
FT /evidence="ECO:0000269|PubMed:19843229"
FT MUTAGEN 74
FT /note="G->R: Loss of GTP-synthesizing activity and lack of
FT autophosphorylation. Does not interact with Ndk."
FT /evidence="ECO:0000269|PubMed:19843229"
FT MUTAGEN 75
FT /note="K->A: Partial loss of GTP-synthesizing activity."
FT /evidence="ECO:0000269|PubMed:19843229"
FT MUTAGEN 115
FT /note="H->A: Partial loss of GTP-synthesizing activity and
FT decrease in autophosphorylation. Loss of GTP-synthesizing
FT activity and lack of autophosphorylation; when associated
FT with A-247."
FT /evidence="ECO:0000269|PubMed:19843229"
FT MUTAGEN 247
FT /note="H->A: Partial loss of GTP-synthesizing activity and
FT decrease in autophosphorylation. Loss of GTP-synthesizing
FT activity and lack of autophosphorylation; when associated
FT with A-115."
FT /evidence="ECO:0000269|PubMed:19843229"
SQ SEQUENCE 295 AA; 34124 MW; BAE7A32AE71FE634 CRC64;
MDIPSVDVST ATNDGASSRA KGHRSAAPGR RKISDAVYQA ELFRLQTEFV KLQEWARHSG
ARLVVIFEGR DGAGKGGAIK RITEYLNPRV ARIAALPAPT DRERGQWYYQ RYIAHLPAKG
EIVLFDRSWY NRAGVEKVMG FCTPQEYVLF LRQTPIFEQM LIDDGILLRK YWFSVSDAEQ
LRRFKARRND PVRQWKLSPM DLESVYRWED YSRAKDEMMV HTDTPVSPWY VVESDIKKHA
RLNMMAHLLS TIDYADVEKP KVKLPPRPLV SGNYRRPPRE LSTYVDDYVA TLIAR
